FMO DATABASE

FMODB ID: NNY2Q

Calculation Name: 5ENU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5ENU

Chain ID: A

ChEMBL ID:

UniProt ID: B1YRI5

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptAll
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	157
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1551112.910099
FMO2-HF: Nuclear repulsion	1489840.914653
FMO2-HF: Total energy	-61271.995445
FMO2-MP2: Total energy	-61451.474699

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:-3:HIS)

Summations of interaction energy for fragment #1(A:-3: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.
-9.33	-2.683	6.439	-4.401	-8.683	-0.012

Interaction energy analysis for fragmet #1(A:-3:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.010

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	-1	HIS	0	0.004	-0.004	2.865	-2.394	1.946	1.543	-2.418	-3.465	-0.007
4	A	0	HIS	0	0.003	0.000	2.961	-5.597	-4.138	0.217	-0.824	-0.851	-0.008
5	A	1	MET	0	-0.035	-0.020	2.614	-1.972	-1.243	4.680	-1.156	-4.252	0.003
6	A	2	SER	0	0.011	0.009	5.820	0.573	0.573	0.000	0.000	0.000	0.000
7	A	3	VAL	0	-0.042	-0.019	9.441	0.236	0.236	0.000	0.000	0.000	0.000
8	A	4	GLU	-1	-0.873	-0.951	11.762	-0.299	-0.299	0.000	0.000	0.000	0.000
9	A	5	VAL	0	-0.038	-0.019	13.554	0.139	0.139	0.000	0.000	0.000	0.000
10	A	6	ASP	-1	-0.935	-0.967	15.494	0.224	0.224	0.000	0.000	0.000	0.000
11	A	7	ARG	1	0.846	0.926	10.221	-0.191	-0.191	0.000	0.000	0.000	0.000
12	A	8	GLN	0	-0.043	-0.018	8.249	-0.124	-0.124	0.000	0.000	0.000	0.000
13	A	9	VAL	0	-0.012	-0.008	8.951	0.056	0.056	0.000	0.000	0.000	0.000
14	A	10	PRO	0	-0.004	-0.004	5.126	0.259	0.378	-0.001	-0.003	-0.115	0.000
15	A	11	ASP	-1	-0.755	-0.859	6.912	0.237	0.237	0.000	0.000	0.000	0.000
16	A	12	PHE	0	-0.023	-0.018	7.238	-0.271	-0.271	0.000	0.000	0.000	0.000
17	A	13	THR	0	0.032	-0.005	9.817	0.100	0.100	0.000	0.000	0.000	0.000
18	A	14	ALA	0	-0.016	0.000	12.776	-0.150	-0.150	0.000	0.000	0.000	0.000
19	A	15	PRO	0	0.046	0.018	15.652	0.067	0.067	0.000	0.000	0.000	0.000
20	A	16	ALA	0	0.008	0.000	19.433	-0.021	-0.021	0.000	0.000	0.000	0.000
21	A	17	THR	0	-0.056	-0.038	21.976	0.002	0.002	0.000	0.000	0.000	0.000
22	A	18	GLY	0	-0.007	0.000	25.772	0.018	0.018	0.000	0.000	0.000	0.000
23	A	19	GLY	0	0.000	0.009	23.351	0.014	0.014	0.000	0.000	0.000	0.000
24	A	20	ASP	-1	-0.973	-0.980	17.620	0.000	0.000	0.000	0.000	0.000	0.000
25	A	21	ILE	0	-0.011	-0.002	17.326	0.033	0.033	0.000	0.000	0.000	0.000
26	A	22	SER	0	0.012	0.004	12.096	-0.095	-0.095	0.000	0.000	0.000	0.000
27	A	23	LEU	0	-0.029	-0.001	10.854	-0.019	-0.019	0.000	0.000	0.000	0.000
28	A	24	SER	0	0.001	-0.046	12.086	0.029	0.029	0.000	0.000	0.000	0.000
29	A	25	ASP	-1	-0.840	-0.907	14.355	0.322	0.322	0.000	0.000	0.000	0.000
30	A	26	LEU	0	-0.090	-0.041	17.001	-0.067	-0.067	0.000	0.000	0.000	0.000
31	A	27	LYS	1	0.891	0.958	13.423	-0.990	-0.990	0.000	0.000	0.000	0.000
32	A	28	GLY	0	-0.023	-0.010	17.645	-0.041	-0.041	0.000	0.000	0.000	0.000
33	A	29	ARG	1	0.783	0.875	20.501	-0.312	-0.312	0.000	0.000	0.000	0.000
34	A	30	LYS	1	0.852	0.932	20.293	-0.168	-0.168	0.000	0.000	0.000	0.000
35	A	31	LEU	0	-0.015	-0.013	16.851	-0.026	-0.026	0.000	0.000	0.000	0.000
36	A	32	VAL	0	0.004	0.008	20.224	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	33	LEU	0	0.008	0.005	16.099	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	34	TYR	0	-0.006	0.000	20.224	-0.023	-0.023	0.000	0.000	0.000	0.000
39	A	35	PHE	0	0.056	0.017	16.023	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	36	TYR	0	-0.014	-0.051	22.196	0.001	0.001	0.000	0.000	0.000	0.000
41	A	37	PRO	0	-0.039	-0.036	25.089	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	38	LYS	1	0.836	0.900	26.336	0.189	0.189	0.000	0.000	0.000	0.000
43	A	39	ASP	-1	-0.673	-0.772	27.803	-0.122	-0.122	0.000	0.000	0.000	0.000
44	A	40	ASN	0	-0.009	-0.011	29.880	0.006	0.006	0.000	0.000	0.000	0.000
45	A	41	THR	0	-0.005	0.010	31.576	0.006	0.006	0.000	0.000	0.000	0.000
46	A	42	PRO	0	0.066	0.030	34.060	0.005	0.005	0.000	0.000	0.000	0.000
47	A	43	GLY	0	0.017	0.025	33.470	0.008	0.008	0.000	0.000	0.000	0.000
48	A	44	CYS	0	-0.030	0.009	29.589	0.004	0.004	0.000	0.000	0.000	0.000
49	A	45	THR	0	-0.005	-0.006	31.060	0.008	0.008	0.000	0.000	0.000	0.000
50	A	46	THR	0	-0.006	-0.010	33.874	0.010	0.010	0.000	0.000	0.000	0.000
51	A	47	GLU	-1	-0.781	-0.892	28.200	-0.082	-0.082	0.000	0.000	0.000	0.000
52	A	48	GLY	0	0.019	0.020	30.126	0.011	0.011	0.000	0.000	0.000	0.000
53	A	49	LEU	0	0.015	-0.010	31.049	0.012	0.012	0.000	0.000	0.000	0.000
54	A	50	GLN	0	0.022	0.012	33.705	0.002	0.002	0.000	0.000	0.000	0.000
55	A	51	PHE	0	0.021	0.003	26.863	0.011	0.011	0.000	0.000	0.000	0.000
56	A	52	ARG	1	0.799	0.895	31.216	0.015	0.015	0.000	0.000	0.000	0.000
57	A	53	GLU	-1	-0.980	-0.983	33.284	0.008	0.008	0.000	0.000	0.000	0.000
58	A	54	LEU	0	0.029	0.004	33.228	0.009	0.009	0.000	0.000	0.000	0.000
59	A	55	TYR	0	-0.010	-0.009	27.593	0.010	0.010	0.000	0.000	0.000	0.000
60	A	56	PRO	0	0.006	-0.014	31.791	0.014	0.014	0.000	0.000	0.000	0.000
61	A	57	LYS	1	0.922	0.965	33.810	-0.039	-0.039	0.000	0.000	0.000	0.000
62	A	58	PHE	0	0.064	0.033	27.791	0.010	0.010	0.000	0.000	0.000	0.000
63	A	59	LYS	1	0.812	0.911	27.355	-0.113	-0.113	0.000	0.000	0.000	0.000
64	A	60	LYS	1	0.935	0.966	30.052	-0.082	-0.082	0.000	0.000	0.000	0.000
65	A	61	ALA	0	-0.007	0.009	29.606	0.005	0.005	0.000	0.000	0.000	0.000
66	A	62	GLY	0	0.007	0.013	27.339	0.014	0.014	0.000	0.000	0.000	0.000
67	A	63	ALA	0	-0.027	-0.009	24.618	0.028	0.028	0.000	0.000	0.000	0.000
68	A	64	GLU	-1	-0.768	-0.864	22.669	0.123	0.123	0.000	0.000	0.000	0.000
69	A	65	ILE	0	-0.011	-0.003	23.708	0.001	0.001	0.000	0.000	0.000	0.000
70	A	66	ILE	0	0.030	0.010	19.107	0.001	0.001	0.000	0.000	0.000	0.000
71	A	67	GLY	0	0.023	0.014	22.238	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	68	VAL	0	-0.024	-0.006	18.099	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	69	SER	0	0.017	-0.009	21.423	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	70	ARG	1	0.879	0.921	20.135	0.408	0.408	0.000	0.000	0.000	0.000
75	A	71	ASP	-1	-0.806	-0.849	22.129	-0.210	-0.210	0.000	0.000	0.000	0.000
76	A	72	SER	0	0.028	0.028	24.291	0.011	0.011	0.000	0.000	0.000	0.000
77	A	73	LEU	0	0.111	0.055	22.886	0.012	0.012	0.000	0.000	0.000	0.000
78	A	74	ARG	1	1.006	1.011	26.150	0.154	0.154	0.000	0.000	0.000	0.000
79	A	75	SER	0	-0.115	-0.069	28.491	0.012	0.012	0.000	0.000	0.000	0.000
80	A	76	HIS	1	0.828	0.879	22.989	0.165	0.165	0.000	0.000	0.000	0.000
81	A	77	ASP	-1	-0.812	-0.916	28.206	-0.057	-0.057	0.000	0.000	0.000	0.000
82	A	78	ASN	0	-0.072	-0.046	30.338	0.015	0.015	0.000	0.000	0.000	0.000
83	A	79	PHE	0	-0.042	-0.015	29.123	0.006	0.006	0.000	0.000	0.000	0.000
84	A	80	LYS	1	0.864	0.903	28.386	0.002	0.002	0.000	0.000	0.000	0.000
85	A	81	ALA	0	-0.003	0.005	31.539	0.009	0.009	0.000	0.000	0.000	0.000
86	A	82	LYS	1	0.871	0.928	34.905	0.082	0.082	0.000	0.000	0.000	0.000
87	A	83	LEU	0	-0.046	-0.018	32.829	0.000	0.000	0.000	0.000	0.000	0.000
88	A	84	GLU	-1	-0.845	-0.910	35.631	0.002	0.002	0.000	0.000	0.000	0.000
89	A	85	LEU	0	-0.040	-0.005	29.773	0.008	0.008	0.000	0.000	0.000	0.000
90	A	86	PRO	0	0.002	0.018	31.018	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	87	PHE	0	0.000	-0.001	26.043	0.006	0.006	0.000	0.000	0.000	0.000
92	A	88	PRO	0	0.039	0.026	22.807	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	89	LEU	0	-0.026	-0.012	23.680	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	90	ILE	0	0.102	0.040	16.757	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	91	SER	0	-0.099	-0.072	20.622	-0.022	-0.022	0.000	0.000	0.000	0.000
96	A	92	ASP	-1	-0.675	-0.819	15.781	-0.506	-0.506	0.000	0.000	0.000	0.000
97	A	93	ALA	0	-0.063	-0.046	18.521	-0.045	-0.045	0.000	0.000	0.000	0.000
98	A	94	ASP	-1	-0.891	-0.946	14.989	-0.662	-0.662	0.000	0.000	0.000	0.000
99	A	95	GLU	-1	-0.847	-0.900	15.975	-0.717	-0.717	0.000	0.000	0.000	0.000
100	A	96	ALA	0	0.044	0.048	11.656	-0.085	-0.085	0.000	0.000	0.000	0.000
101	A	97	LEU	0	-0.005	-0.017	11.767	-0.086	-0.086	0.000	0.000	0.000	0.000
102	A	98	CYS	0	-0.106	-0.089	13.666	0.040	0.040	0.000	0.000	0.000	0.000
103	A	99	ALA	0	-0.024	-0.006	12.489	0.020	0.020	0.000	0.000	0.000	0.000
104	A	100	LEU	0	0.010	0.017	7.747	-0.084	-0.084	0.000	0.000	0.000	0.000
105	A	101	PHE	0	0.010	-0.014	11.018	0.112	0.112	0.000	0.000	0.000	0.000
106	A	102	ASP	-1	-0.860	-0.900	14.200	-0.521	-0.521	0.000	0.000	0.000	0.000
107	A	103	VAL	0	0.018	0.016	15.850	0.087	0.087	0.000	0.000	0.000	0.000
108	A	104	ILE	0	-0.056	-0.023	18.099	0.060	0.060	0.000	0.000	0.000	0.000
109	A	105	LYS	1	0.873	0.919	20.274	0.276	0.276	0.000	0.000	0.000	0.000
110	A	106	MET	0	0.014	0.014	23.208	0.019	0.019	0.000	0.000	0.000	0.000
111	A	107	LYS	1	0.854	0.923	25.459	0.316	0.316	0.000	0.000	0.000	0.000
112	A	108	LYS	1	0.855	0.915	29.217	0.277	0.277	0.000	0.000	0.000	0.000
113	A	109	MET	0	-0.024	-0.018	31.859	0.016	0.016	0.000	0.000	0.000	0.000
114	A	110	TYR	0	0.035	0.012	35.222	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	111	GLY	0	0.041	0.038	36.143	0.001	0.001	0.000	0.000	0.000	0.000
116	A	112	LYS	1	0.931	0.958	30.773	0.266	0.266	0.000	0.000	0.000	0.000
117	A	113	GLU	-1	-0.818	-0.892	27.696	-0.345	-0.345	0.000	0.000	0.000	0.000
118	A	114	VAL	0	-0.042	-0.029	28.677	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	115	ARG	1	0.929	0.941	17.722	0.701	0.701	0.000	0.000	0.000	0.000
120	A	116	GLY	0	-0.007	-0.010	24.996	0.015	0.015	0.000	0.000	0.000	0.000
121	A	117	ILE	0	0.045	0.035	20.920	-0.023	-0.023	0.000	0.000	0.000	0.000
122	A	118	GLU	-1	-0.882	-0.913	22.689	-0.237	-0.237	0.000	0.000	0.000	0.000
123	A	119	ARG	1	0.814	0.879	23.304	0.120	0.120	0.000	0.000	0.000	0.000
124	A	120	SER	0	0.025	0.001	21.449	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	121	THR	0	-0.082	-0.038	21.896	0.014	0.014	0.000	0.000	0.000	0.000
126	A	122	PHE	0	0.044	0.035	17.581	-0.014	-0.014	0.000	0.000	0.000	0.000
127	A	123	LEU	0	-0.009	0.009	19.880	0.003	0.003	0.000	0.000	0.000	0.000
128	A	124	ILE	0	0.021	0.017	14.754	0.002	0.002	0.000	0.000	0.000	0.000
129	A	125	ASP	-1	-0.776	-0.885	17.324	0.451	0.451	0.000	0.000	0.000	0.000
130	A	126	ALA	0	-0.002	0.003	17.808	0.042	0.042	0.000	0.000	0.000	0.000
131	A	127	ASP	-1	-0.861	-0.928	16.141	0.592	0.592	0.000	0.000	0.000	0.000
132	A	128	GLY	0	-0.002	0.010	13.505	0.169	0.169	0.000	0.000	0.000	0.000
133	A	129	VAL	0	-0.015	-0.008	12.783	0.122	0.122	0.000	0.000	0.000	0.000
134	A	130	LEU	0	-0.026	-0.012	13.954	-0.097	-0.097	0.000	0.000	0.000	0.000
135	A	131	ARG	1	0.863	0.916	15.798	-0.346	-0.346	0.000	0.000	0.000	0.000
136	A	132	GLN	0	0.016	0.012	19.254	-0.016	-0.016	0.000	0.000	0.000	0.000
137	A	133	ALA	0	0.007	0.002	19.257	0.009	0.009	0.000	0.000	0.000	0.000
138	A	134	TRP	0	0.011	0.007	21.325	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	135	ARG	1	0.851	0.902	16.520	0.350	0.350	0.000	0.000	0.000	0.000
140	A	136	GLY	0	0.023	0.016	24.173	0.008	0.008	0.000	0.000	0.000	0.000
141	A	137	ILE	0	-0.033	0.004	26.416	0.010	0.010	0.000	0.000	0.000	0.000
142	A	138	LYS	1	0.880	0.926	29.088	0.043	0.043	0.000	0.000	0.000	0.000
143	A	139	VAL	0	0.017	-0.001	30.930	0.007	0.007	0.000	0.000	0.000	0.000
144	A	140	PRO	0	-0.002	-0.010	32.708	0.009	0.009	0.000	0.000	0.000	0.000
145	A	141	GLY	0	0.063	0.047	35.266	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	142	HIS	0	0.015	0.013	26.329	0.010	0.010	0.000	0.000	0.000	0.000
147	A	143	VAL	0	-0.006	-0.008	30.121	0.009	0.009	0.000	0.000	0.000	0.000
148	A	144	ASP	-1	-0.853	-0.934	31.066	0.021	0.021	0.000	0.000	0.000	0.000
149	A	145	ASP	-1	-0.899	-0.931	30.065	0.010	0.010	0.000	0.000	0.000	0.000
150	A	146	VAL	0	-0.051	-0.028	25.572	0.016	0.016	0.000	0.000	0.000	0.000
151	A	147	LEU	0	-0.028	-0.020	27.727	0.021	0.021	0.000	0.000	0.000	0.000
152	A	148	SER	0	-0.017	-0.027	30.264	0.015	0.015	0.000	0.000	0.000	0.000
153	A	149	ALA	0	0.006	0.007	26.040	0.012	0.012	0.000	0.000	0.000	0.000
154	A	150	VAL	0	-0.024	-0.017	25.125	0.022	0.022	0.000	0.000	0.000	0.000
155	A	151	GLN	0	-0.058	-0.036	26.982	0.016	0.016	0.000	0.000	0.000	0.000
156	A	152	ALA	0	-0.012	0.011	28.670	0.007	0.007	0.000	0.000	0.000	0.000
157	A	153	LEU	0	-0.050	-0.012	22.502	0.018	0.018	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:HIS)