FMO DATABASE

FMODB ID: 94J72

Calculation Name: 1UFH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	155
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1545650.499166
FMO2-HF: Nuclear repulsion	1482977.423987
FMO2-HF: Total energy	-62673.075179
FMO2-MP2: Total energy	-62857.795906

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: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.
-4.213	-0.968	2.07	-1.932	-3.381	-0.01

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 : -0.030 / q_NPA : -0.031

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	0.018	0.013	3.254	0.850	2.703	-0.010	-0.648	-1.195	0.002
4	A	5	LEU	0	0.019	0.009	5.297	0.110	0.144	-0.001	-0.004	-0.028	0.000
5	A	6	THR	0	-0.036	-0.024	9.038	0.144	0.144	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.031	0.015	11.301	-0.021	-0.021	0.000	0.000	0.000	0.000
7	A	8	MET	0	-0.011	0.015	15.078	-0.012	-0.012	0.000	0.000	0.000	0.000
8	A	9	GLN	0	0.064	0.031	16.390	0.079	0.079	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.002	-0.015	18.964	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.948	-0.958	21.511	-0.254	-0.254	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.865	-0.951	16.788	-0.401	-0.401	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.031	0.018	20.119	0.011	0.011	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.921	0.952	21.724	0.188	0.188	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.018	0.004	21.905	0.019	0.019	0.000	0.000	0.000	0.000
15	A	16	TYR	0	-0.046	-0.071	19.518	0.017	0.017	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.004	0.001	21.771	0.015	0.015	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.045	-0.031	24.957	0.022	0.022	0.000	0.000	0.000	0.000
18	A	19	TYR	0	-0.007	0.001	20.396	0.008	0.008	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.043	0.025	21.852	0.008	0.008	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.028	-0.001	24.172	0.017	0.017	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.951	0.997	27.555	0.163	0.163	0.000	0.000	0.000	0.000
22	A	23	HIS	0	0.079	0.051	22.297	0.010	0.010	0.000	0.000	0.000	0.000
23	A	24	TYR	0	0.005	-0.011	25.739	0.013	0.013	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.003	-0.010	27.114	0.011	0.011	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.922	-0.959	27.803	-0.145	-0.145	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.850	-0.921	24.669	-0.164	-0.164	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.904	0.958	28.297	0.121	0.121	0.000	0.000	0.000	0.000
28	A	29	VAL	0	0.001	0.019	31.292	0.008	0.008	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.870	0.944	26.837	0.142	0.142	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.058	-0.033	30.274	0.005	0.005	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.031	-0.002	32.141	0.006	0.006	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.114	-0.055	33.570	0.003	0.003	0.000	0.000	0.000	0.000
33	A	34	TRP	0	0.031	0.002	32.091	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.052	0.031	36.468	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.018	-0.004	36.830	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.934	-0.973	37.889	-0.075	-0.075	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.899	-0.938	39.282	-0.071	-0.071	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.062	-0.033	33.820	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	40	GLN	0	-0.016	-0.011	34.134	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.031	0.013	34.589	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.036	0.026	35.169	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.019	-0.046	29.741	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.965	0.977	31.225	0.125	0.125	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.010	-0.006	33.093	0.001	0.001	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.029	0.017	29.335	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	PHE	0	-0.024	-0.024	24.910	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.084	-0.032	29.588	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.903	-0.954	32.362	-0.090	-0.090	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.073	-0.021	26.549	0.001	0.001	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.064	-0.031	24.108	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.040	0.034	28.387	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.911	0.953	29.309	0.100	0.100	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.019	0.011	26.755	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.002	0.003	20.581	0.001	0.001	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.933	-0.956	23.444	-0.146	-0.146	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.121	-0.065	25.948	0.021	0.021	0.000	0.000	0.000	0.000
57	A	58	PRO	0	0.017	-0.011	25.360	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	59	HIS	0	0.042	0.013	24.382	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	HIS	0	0.010	0.031	22.568	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.021	0.013	17.392	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.017	0.012	17.795	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	63	TRP	0	0.024	0.000	12.311	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.016	-0.022	12.790	0.036	0.036	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.056	-0.024	8.435	-0.148	-0.148	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.957	0.965	7.785	1.068	1.068	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.003	0.014	3.667	-1.535	-1.300	0.004	-0.082	-0.157	0.000
67	A	68	ASN	0	-0.002	0.008	3.989	-0.851	-0.620	0.001	-0.051	-0.181	0.000
68	A	69	GLU	-1	-0.896	-0.955	6.484	-0.597	-0.597	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.915	0.963	9.978	0.432	0.432	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.829	-0.868	8.632	-0.487	-0.487	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.046	0.016	9.236	-0.324	-0.324	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.002	-0.008	7.267	0.159	0.159	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.010	-0.022	10.409	0.130	0.130	0.000	0.000	0.000	0.000
74	A	75	TRP	0	-0.049	0.009	12.319	-0.089	-0.089	0.000	0.000	0.000	0.000
75	A	76	LEU	0	0.014	-0.006	11.649	-0.020	-0.020	0.000	0.000	0.000	0.000
76	A	77	TRP	0	-0.021	-0.014	14.832	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.004	0.003	16.229	0.013	0.013	0.000	0.000	0.000	0.000
78	A	79	HIS	0	-0.035	-0.012	19.102	0.010	0.010	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.038	-0.003	21.015	0.008	0.008	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.901	-0.938	23.048	-0.052	-0.052	0.000	0.000	0.000	0.000
81	A	82	PRO	0	-0.034	-0.024	25.437	0.005	0.005	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.920	-0.958	26.504	-0.009	-0.009	0.000	0.000	0.000	0.000
83	A	84	HIS	0	0.014	0.032	26.955	0.009	0.009	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.023	0.002	28.661	0.007	0.007	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.093	-0.058	26.822	0.011	0.011	0.000	0.000	0.000	0.000
86	A	87	GLN	0	0.008	0.006	23.853	0.008	0.008	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.810	-0.870	22.859	-0.062	-0.062	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.024	0.002	19.368	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.017	-0.012	20.975	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.002	-0.013	16.390	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	92	TYR	0	0.003	-0.012	19.409	0.015	0.015	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.800	-0.884	19.221	-0.307	-0.307	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.049	-0.027	10.459	-0.041	-0.041	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.015	0.013	14.192	0.052	0.052	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.003	0.002	9.445	-0.088	-0.088	0.000	0.000	0.000	0.000
96	A	97	TYR	0	0.080	0.037	13.030	0.132	0.132	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.944	-0.988	14.201	-0.266	-0.266	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.042	0.025	15.019	0.010	0.010	0.000	0.000	0.000	0.000
99	A	100	TYR	0	-0.101	-0.119	10.043	0.004	0.004	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.840	0.928	10.593	0.283	0.283	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.003	-0.004	12.819	0.038	0.038	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.940	0.974	9.115	0.387	0.387	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.007	0.000	8.346	0.020	0.020	0.000	0.000	0.000	0.000
104	A	105	TYR	0	0.048	0.016	4.317	-0.265	-0.164	-0.001	-0.007	-0.093	0.000
105	A	106	ALA	0	0.014	0.017	6.243	-0.251	-0.251	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.984	0.986	8.303	0.255	0.255	0.000	0.000	0.000	0.000
107	A	108	GLN	0	0.003	0.004	2.298	-3.717	-2.955	2.078	-1.138	-1.702	-0.012
108	A	109	ALA	0	0.019	0.006	5.275	0.144	0.173	-0.001	-0.002	-0.025	0.000
109	A	110	LEU	0	0.014	0.009	7.130	0.216	0.216	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.023	0.025	6.282	0.140	0.140	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.013	0.005	5.159	0.255	0.255	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.005	0.002	7.023	0.079	0.079	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.884	-0.939	10.609	0.246	0.246	0.000	0.000	0.000	0.000
114	A	115	GLN	0	-0.013	-0.016	6.946	0.132	0.132	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.015	0.010	10.597	0.000	0.000	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.056	0.025	12.288	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.896	0.950	14.323	-0.159	-0.159	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.125	-0.060	14.202	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	120	MET	0	-0.043	-0.020	16.153	-0.030	-0.030	0.000	0.000	0.000	0.000
120	A	121	GLY	0	-0.029	-0.003	18.570	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	122	ILE	0	-0.067	-0.013	18.031	-0.009	-0.009	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.901	0.941	19.532	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.904	0.955	20.936	0.045	0.045	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.021	0.012	15.134	-0.013	-0.013	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.032	-0.064	19.609	0.007	0.007	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.005	0.009	18.374	-0.020	-0.020	0.000	0.000	0.000	0.000
127	A	128	HIS	0	0.034	0.034	21.993	0.023	0.023	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.014	-0.018	21.284	-0.022	-0.022	0.000	0.000	0.000	0.000
129	A	130	PHE	0	-0.006	0.001	23.386	0.017	0.017	0.000	0.000	0.000	0.000
130	A	131	ALA	0	0.075	0.030	25.073	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	132	HIS	0	-0.014	-0.017	26.287	0.009	0.009	0.000	0.000	0.000	0.000
132	A	133	ASN	0	-0.044	-0.027	21.786	0.001	0.001	0.000	0.000	0.000	0.000
133	A	134	GLN	0	0.053	0.007	22.190	-0.012	-0.012	0.000	0.000	0.000	0.000
134	A	135	THR	0	-0.056	-0.023	17.516	0.009	0.009	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.024	0.020	17.526	-0.015	-0.015	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.900	0.939	18.249	0.100	0.100	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.994	0.996	19.295	0.137	0.137	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.033	-0.002	11.786	0.003	0.003	0.000	0.000	0.000	0.000
139	A	140	TYR	0	0.050	-0.007	15.233	-0.021	-0.021	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.881	-0.929	17.332	-0.083	-0.083	0.000	0.000	0.000	0.000
141	A	142	GLN	0	-0.069	-0.062	15.501	-0.020	-0.020	0.000	0.000	0.000	0.000
142	A	143	THR	0	-0.095	-0.066	13.284	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	144	GLY	0	0.007	0.042	15.058	0.013	0.013	0.000	0.000	0.000	0.000
144	A	145	PHE	0	-0.037	-0.004	15.313	0.009	0.009	0.000	0.000	0.000	0.000
145	A	146	GLN	0	-0.021	-0.020	19.956	0.003	0.003	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.891	-0.932	23.722	-0.085	-0.085	0.000	0.000	0.000	0.000
147	A	148	THR	0	-0.044	-0.028	26.147	0.006	0.006	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.879	-0.923	28.649	-0.054	-0.054	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.022	-0.021	29.461	-0.008	-0.008	0.000	0.000	0.000	0.000
150	A	151	VAL	0	-0.004	0.010	31.661	0.005	0.005	0.000	0.000	0.000	0.000
151	A	152	MET	0	-0.022	-0.015	33.138	-0.003	-0.003	0.000	0.000	0.000	0.000
152	A	153	SER	0	0.017	-0.006	35.857	0.003	0.003	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.958	0.979	38.420	0.042	0.042	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.982	1.004	40.316	0.065	0.065	0.000	0.000	0.000	0.000
155	A	156	LEU	0	0.016	0.013	43.467	0.001	0.001	0.000	0.000	0.000	0.000

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