FMO DATABASE

FMODB ID: 72LNK

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	OptAll
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	-1549377.775744
FMO2-HF: Nuclear repulsion	1486703.221267
FMO2-HF: Total energy	-62674.554477
FMO2-MP2: Total energy	-62859.319494

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.
-7.66	-6.877	8.039	-4.143	-4.678	-0.021

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 : 0.000 / q_NPA : 0.000

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	0.022	0.016	3.671	1.136	3.391	-0.018	-1.010	-1.228	0.004
4	A	5	LEU	0	0.012	0.009	5.507	-0.047	-0.047	0.000	0.000	0.000	0.000
5	A	6	THR	0	-0.030	-0.021	8.889	0.104	0.104	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.034	0.000	11.274	0.027	0.027	0.000	0.000	0.000	0.000
7	A	8	MET	0	0.000	0.032	15.130	-0.042	-0.042	0.000	0.000	0.000	0.000
8	A	9	GLN	0	-0.008	-0.013	16.513	0.116	0.116	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.016	-0.010	19.154	0.007	0.007	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.959	-0.974	22.004	-0.432	-0.432	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.735	-0.831	16.264	-0.849	-0.849	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.061	0.023	20.135	0.019	0.019	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.945	0.976	21.887	0.303	0.303	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.012	0.009	22.014	0.034	0.034	0.000	0.000	0.000	0.000
15	A	16	TYR	0	-0.030	-0.055	19.471	0.019	0.019	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.029	0.019	21.785	0.025	0.025	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.052	-0.024	24.999	0.038	0.038	0.000	0.000	0.000	0.000
18	A	19	TYR	0	-0.015	-0.001	20.119	0.017	0.017	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.011	-0.010	21.782	0.014	0.014	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.043	-0.037	24.320	0.032	0.032	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.942	1.000	27.551	0.226	0.226	0.000	0.000	0.000	0.000
22	A	23	HIS	0	0.076	0.042	22.574	0.009	0.009	0.000	0.000	0.000	0.000
23	A	24	TYR	0	0.037	0.003	25.896	0.025	0.025	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.015	0.005	27.316	0.018	0.018	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.905	-0.963	28.540	-0.174	-0.174	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.752	-0.849	25.136	-0.119	-0.119	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.884	0.961	28.498	0.098	0.098	0.000	0.000	0.000	0.000
28	A	29	VAL	0	0.005	0.018	31.602	0.011	0.011	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.826	0.910	26.408	0.132	0.132	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.032	-0.015	30.312	0.009	0.009	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.069	-0.032	32.188	0.009	0.009	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.100	-0.047	33.513	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	TRP	0	0.025	-0.007	32.243	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.032	0.029	36.886	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.010	-0.019	36.919	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.905	-0.956	37.939	-0.084	-0.084	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.879	-0.933	39.107	-0.071	-0.071	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.042	-0.025	34.022	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	40	GLN	0	-0.007	-0.007	34.150	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.004	0.010	34.813	-0.008	-0.008	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.032	0.011	35.798	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.028	-0.037	29.960	0.001	0.001	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.941	0.971	31.464	0.149	0.149	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.015	0.009	33.204	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.052	0.036	29.413	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	47	PHE	0	0.013	-0.011	25.879	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.100	-0.064	29.645	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.901	-0.960	32.497	-0.087	-0.087	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.046	-0.016	26.855	0.005	0.005	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.046	-0.019	24.304	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.024	0.024	28.628	-0.013	-0.013	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.782	0.883	28.749	0.134	0.134	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.003	-0.006	26.792	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.007	-0.008	20.363	0.013	0.013	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.824	-0.891	23.508	-0.155	-0.155	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.088	-0.045	26.012	0.026	0.026	0.000	0.000	0.000	0.000
57	A	58	PRO	0	0.045	0.006	25.547	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	59	HIS	0	0.004	-0.002	24.553	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	60	HIS	0	-0.015	0.023	22.681	0.007	0.007	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.010	0.009	17.506	-0.022	-0.022	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.000	0.000	17.772	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	63	TRP	0	0.008	-0.012	12.332	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.014	-0.034	13.335	0.027	0.027	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.036	-0.005	8.868	-0.119	-0.119	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.835	0.893	8.041	1.349	1.349	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.013	-0.002	3.010	-1.440	-0.826	0.075	-0.225	-0.463	0.000
67	A	68	ASN	0	-0.012	-0.016	4.044	-1.213	-1.014	0.000	-0.056	-0.143	0.000
68	A	69	GLU	-1	-0.886	-0.945	6.624	-1.775	-1.775	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.897	0.956	10.074	1.200	1.200	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.815	-0.877	8.628	-1.624	-1.624	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.009	0.000	9.298	-0.505	-0.505	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.019	0.004	7.113	0.274	0.274	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.021	-0.026	10.263	0.272	0.272	0.000	0.000	0.000	0.000
74	A	75	TRP	0	-0.061	-0.012	12.413	-0.114	-0.114	0.000	0.000	0.000	0.000
75	A	76	LEU	0	0.005	-0.007	11.785	0.029	0.029	0.000	0.000	0.000	0.000
76	A	77	TRP	0	-0.039	-0.020	14.820	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	78	ILE	0	0.006	0.001	16.293	0.035	0.035	0.000	0.000	0.000	0.000
78	A	79	HIS	0	-0.005	-0.011	19.191	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.016	-0.008	21.089	0.025	0.025	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.874	-0.919	23.191	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	82	PRO	0	-0.029	-0.021	25.644	0.014	0.014	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.893	-0.949	26.776	0.050	0.050	0.000	0.000	0.000	0.000
83	A	84	HIS	0	0.014	0.033	27.202	0.011	0.011	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.034	0.008	28.890	0.015	0.015	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.044	-0.034	27.322	0.014	0.014	0.000	0.000	0.000	0.000
86	A	87	GLN	0	0.031	0.029	24.427	0.038	0.038	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.784	-0.859	23.236	0.105	0.105	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.006	0.004	19.504	-0.017	-0.017	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.016	-0.012	21.070	0.019	0.019	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.008	-0.016	15.799	-0.026	-0.026	0.000	0.000	0.000	0.000
91	A	92	TYR	0	-0.001	-0.004	19.513	0.011	0.011	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.797	-0.858	19.545	-0.316	-0.316	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.023	-0.019	10.973	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.014	0.013	14.309	0.065	0.065	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.012	0.003	9.188	-0.126	-0.126	0.000	0.000	0.000	0.000
96	A	97	TYR	0	0.051	0.023	13.074	0.165	0.165	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.827	-0.918	14.295	-0.464	-0.464	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.017	0.008	14.575	0.016	0.016	0.000	0.000	0.000	0.000
99	A	100	TYR	0	-0.026	-0.025	9.922	0.028	0.028	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.796	0.900	10.629	0.428	0.428	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.001	-0.007	13.134	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.863	0.921	8.839	0.803	0.803	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.013	0.012	7.719	-0.054	-0.054	0.000	0.000	0.000	0.000
104	A	105	TYR	0	0.030	0.004	4.134	0.370	0.485	-0.001	-0.015	-0.098	0.000
105	A	106	ALA	0	0.028	0.025	6.018	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.935	0.952	8.500	-0.302	-0.302	0.000	0.000	0.000	0.000
107	A	108	GLN	0	0.019	0.017	1.936	-6.418	-8.859	7.984	-2.835	-2.708	-0.025
108	A	109	ALA	0	0.028	0.013	5.290	0.368	0.409	-0.001	-0.002	-0.038	0.000
109	A	110	LEU	0	0.014	0.012	7.194	0.209	0.209	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.034	0.017	6.525	0.065	0.065	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.002	0.009	5.359	0.253	0.253	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.004	0.002	7.340	-0.143	-0.143	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.825	-0.867	10.792	0.759	0.759	0.000	0.000	0.000	0.000
114	A	115	GLN	0	-0.025	-0.024	6.141	0.135	0.135	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.008	0.013	11.012	-0.113	-0.113	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.034	0.013	12.482	-0.068	-0.068	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.826	0.866	14.381	-0.684	-0.684	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.101	-0.055	13.705	-0.055	-0.055	0.000	0.000	0.000	0.000
119	A	120	MET	0	-0.048	-0.021	15.753	-0.062	-0.062	0.000	0.000	0.000	0.000
120	A	121	GLY	0	-0.010	0.008	18.323	-0.035	-0.035	0.000	0.000	0.000	0.000
121	A	122	ILE	0	-0.074	-0.018	18.253	-0.013	-0.013	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.841	0.895	19.733	-0.140	-0.140	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.809	0.900	21.459	-0.089	-0.089	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.017	0.011	15.351	-0.020	-0.020	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.019	-0.032	19.703	0.018	0.018	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.018	0.000	18.471	-0.019	-0.019	0.000	0.000	0.000	0.000
127	A	128	HIS	0	0.030	0.022	21.776	0.022	0.022	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.014	-0.017	21.744	-0.020	-0.020	0.000	0.000	0.000	0.000
129	A	130	PHE	0	0.004	0.017	23.813	0.015	0.015	0.000	0.000	0.000	0.000
130	A	131	ALA	0	0.053	0.021	25.642	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	132	HIS	0	-0.049	-0.041	26.009	0.020	0.020	0.000	0.000	0.000	0.000
132	A	133	ASN	0	-0.051	-0.027	21.953	-0.010	-0.010	0.000	0.000	0.000	0.000
133	A	134	GLN	0	0.044	0.005	22.336	0.017	0.017	0.000	0.000	0.000	0.000
134	A	135	THR	0	0.009	-0.001	17.560	0.027	0.027	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.011	0.017	17.749	0.009	0.009	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.829	0.896	18.471	0.001	0.001	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.878	0.922	18.909	-0.033	-0.033	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.066	-0.027	11.978	0.045	0.045	0.000	0.000	0.000	0.000
139	A	140	TYR	0	0.044	0.004	15.459	0.044	0.044	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.779	-0.885	17.615	0.140	0.140	0.000	0.000	0.000	0.000
141	A	142	GLN	0	-0.048	-0.019	15.985	0.074	0.074	0.000	0.000	0.000	0.000
142	A	143	THR	0	-0.046	-0.035	12.930	0.106	0.106	0.000	0.000	0.000	0.000
143	A	144	GLY	0	0.020	0.024	15.091	0.044	0.044	0.000	0.000	0.000	0.000
144	A	145	PHE	0	-0.017	0.003	15.194	-0.017	-0.017	0.000	0.000	0.000	0.000
145	A	146	GLN	0	-0.043	-0.030	19.954	-0.014	-0.014	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.857	-0.906	23.734	0.041	0.041	0.000	0.000	0.000	0.000
147	A	148	THR	0	-0.034	-0.033	26.264	0.004	0.004	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.881	-0.907	28.480	0.046	0.046	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.029	-0.023	29.247	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	151	VAL	0	0.003	0.010	31.568	0.000	0.000	0.000	0.000	0.000	0.000
151	A	152	MET	0	-0.029	-0.015	33.282	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	153	SER	0	0.008	-0.003	36.021	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.965	0.980	38.665	0.005	0.005	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.982	1.004	39.985	0.042	0.042	0.000	0.000	0.000	0.000
155	A	156	LEU	0	0.028	0.015	43.842	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)