FMO DATABASE

FMODB ID: YZ282

Calculation Name: 1ANU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ANU

Chain ID: A

ChEMBL ID:

UniProt ID: Q06851

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	OptH
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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1147244.612375
FMO2-HF: Nuclear repulsion	1096516.645824
FMO2-HF: Total energy	-50727.966551
FMO2-MP2: Total energy	-50879.341002

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:1:VAL)

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

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.
-20.122	-7.25	10.111	-7.883	-15.099	-0.062

Interaction energy analysis for fragmet #1(A:1:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : -0.004

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	3	VAL	0	0.034	0.022	3.055	-1.683	0.580	0.055	-0.867	-1.452	0.003
4	A	4	GLU	-1	-0.911	-0.955	4.875	0.335	0.369	-0.001	-0.004	-0.029	0.000
5	A	5	ILE	0	-0.002	0.017	8.522	0.005	0.005	0.000	0.000	0.000	0.000
6	A	6	GLY	0	0.021	0.008	11.660	0.046	0.046	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.930	0.961	14.291	-0.112	-0.112	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.015	0.021	17.736	0.014	0.014	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.007	-0.012	20.756	-0.003	-0.003	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.034	0.013	24.509	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.016	0.005	27.138	0.001	0.001	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.026	0.010	30.436	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.014	-0.001	31.721	0.003	0.003	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.078	-0.035	29.486	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.022	-0.019	25.840	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.008	-0.003	22.596	0.006	0.006	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.866	-0.955	19.755	-0.059	-0.059	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.042	-0.015	15.466	0.014	0.014	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.018	0.006	13.867	-0.021	-0.021	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.035	0.018	8.526	0.010	0.010	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.025	-0.025	8.621	0.009	0.009	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.046	0.028	4.293	-0.360	-0.114	0.000	-0.022	-0.224	0.000
23	A	23	ARG	1	0.855	0.904	3.757	-0.715	-0.397	0.001	-0.083	-0.236	0.000
24	A	24	GLY	0	0.004	0.006	2.434	-2.254	-0.689	2.574	-2.047	-2.093	-0.019
25	A	25	VAL	0	-0.031	-0.001	2.567	-4.285	-1.449	1.638	-1.715	-2.759	-0.021
26	A	26	PRO	0	0.010	0.015	2.218	0.149	0.069	1.655	-0.302	-1.273	0.001
27	A	27	SER	0	0.010	-0.019	4.961	-0.016	0.001	-0.001	-0.003	-0.013	0.000
28	A	28	LYS	1	0.897	0.960	8.512	0.255	0.255	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.039	0.024	7.388	0.031	0.031	0.000	0.000	0.000	0.000
30	A	30	ILE	0	-0.041	-0.014	2.801	-0.743	-0.190	0.135	-0.140	-0.547	0.000
31	A	31	ALA	0	0.048	0.016	6.802	0.117	0.117	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.042	-0.025	8.941	0.046	0.046	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.033	-0.016	5.926	-0.114	-0.114	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.831	-0.889	8.756	-0.383	-0.383	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.018	0.002	7.074	-0.077	-0.077	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.013	0.005	11.589	0.061	0.061	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.004	0.002	9.502	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.980	0.980	15.025	0.138	0.138	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.019	-0.010	18.187	0.009	0.009	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.846	-0.936	20.726	-0.056	-0.056	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.012	-0.005	24.477	0.005	0.005	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.067	-0.025	26.541	0.006	0.006	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.057	-0.012	25.794	0.005	0.005	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.025	-0.020	21.558	0.005	0.005	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.859	-0.925	25.499	-0.061	-0.061	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.012	-0.015	20.568	0.004	0.004	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.047	-0.021	23.807	0.000	0.000	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.008	-0.002	22.827	0.000	0.000	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.033	-0.016	16.166	0.005	0.005	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.903	-0.935	18.505	-0.102	-0.102	0.000	0.000	0.000	0.000
51	A	51	PRO	0	-0.002	-0.001	15.042	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.005	-0.013	13.384	0.024	0.024	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.938	-0.978	14.236	-0.064	-0.064	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.107	-0.039	7.890	0.011	0.011	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.026	-0.005	11.246	-0.033	-0.033	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.007	-0.015	13.518	0.027	0.027	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.769	-0.853	15.817	-0.146	-0.146	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.019	-0.017	17.833	0.008	0.008	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.078	-0.033	20.811	0.008	0.008	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.055	0.010	17.266	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	61	THR	0	-0.023	-0.020	17.561	-0.015	-0.015	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.849	0.953	19.984	0.132	0.132	0.000	0.000	0.000	0.000
63	A	63	SER	0	0.062	0.018	14.640	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	64	PHE	0	-0.088	-0.038	12.575	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.852	-0.918	15.432	-0.161	-0.161	0.000	0.000	0.000	0.000
66	A	66	THR	0	-0.060	-0.040	15.651	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	67	ALA	0	-0.001	0.013	17.916	0.019	0.019	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.008	-0.001	19.682	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.009	0.000	21.626	0.016	0.016	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.015	-0.003	24.134	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.884	-0.936	26.127	-0.078	-0.078	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.878	0.936	23.315	0.126	0.126	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.894	0.956	23.357	0.071	0.071	0.000	0.000	0.000	0.000
74	A	74	ILE	0	0.003	0.006	18.937	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.014	-0.007	16.408	0.017	0.017	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.005	-0.003	15.767	-0.019	-0.019	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.006	-0.007	11.863	0.035	0.035	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.013	-0.002	12.694	-0.044	-0.044	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.017	-0.008	9.030	0.043	0.043	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.020	-0.004	11.539	-0.061	-0.061	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.765	-0.847	12.520	-0.198	-0.198	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.893	-0.961	14.232	-0.158	-0.158	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.148	-0.084	17.544	0.021	0.021	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.022	0.010	17.879	0.015	0.015	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.135	-0.078	18.275	0.010	0.010	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.065	0.035	14.285	0.004	0.004	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.066	-0.032	14.364	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.052	-0.031	15.205	0.017	0.017	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.034	0.024	10.169	-0.025	-0.025	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.014	0.002	6.947	0.050	0.050	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.015	-0.011	8.028	-0.071	-0.071	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.905	0.958	9.021	0.120	0.120	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.801	-0.907	6.333	0.346	0.346	0.000	0.000	0.000	0.000
94	A	94	GLY	0	-0.030	-0.024	7.716	0.026	0.026	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.015	-0.010	8.878	-0.031	-0.031	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.047	0.024	8.162	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.032	0.016	10.271	0.000	0.000	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.892	0.946	13.355	0.087	0.087	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.017	0.024	14.722	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.966	0.991	18.211	0.088	0.088	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.015	0.003	21.943	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	102	THR	0	0.018	0.012	23.933	0.008	0.008	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.018	0.003	25.997	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.890	0.935	28.102	0.051	0.051	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.005	-0.007	29.739	0.004	0.004	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.004	-0.007	29.399	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.040	-0.006	29.183	0.005	0.005	0.000	0.000	0.000	0.000
108	A	108	PRO	0	0.031	0.007	24.585	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.031	0.019	23.273	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	110	TYR	0	-0.027	-0.018	19.493	0.001	0.001	0.000	0.000	0.000	0.000
111	A	111	ILE	0	0.001	-0.003	15.003	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.019	-0.013	14.887	0.012	0.012	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.003	-0.018	10.330	-0.023	-0.023	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-1.013	-0.996	12.792	-0.167	-0.167	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.929	-0.964	13.450	-0.279	-0.279	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.056	-0.040	7.781	-0.032	-0.032	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.015	0.029	10.817	0.069	0.069	0.000	0.000	0.000	0.000
118	A	118	GLY	0	-0.016	-0.010	10.669	-0.041	-0.041	0.000	0.000	0.000	0.000
119	A	119	PHE	0	-0.030	-0.053	2.166	-1.061	-0.543	1.746	-0.595	-1.668	-0.006
120	A	120	ALA	0	0.038	0.040	6.345	-0.193	-0.193	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.845	-0.938	6.215	-0.577	-0.577	0.000	0.000	0.000	0.000
122	A	122	ASN	0	-0.034	-0.045	7.414	0.049	0.049	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.996	-0.967	10.612	-0.213	-0.213	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.066	-0.044	11.238	0.030	0.030	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.025	0.008	9.019	0.023	0.023	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.866	-0.951	7.948	-0.934	-0.934	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.061	-0.028	3.058	-1.037	-0.245	0.133	-0.164	-0.760	0.000
128	A	128	LYS	1	0.934	0.971	4.114	-0.085	0.267	-0.001	-0.054	-0.297	0.000
129	A	129	VAL	0	0.015	0.008	2.480	-6.975	-3.893	2.169	-1.885	-3.366	-0.020
130	A	130	SER	0	-0.075	-0.034	3.577	1.149	1.525	0.008	-0.002	-0.382	0.000
131	A	131	PHE	0	0.046	0.020	5.387	-0.256	-0.256	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.056	-0.021	7.746	0.180	0.180	0.000	0.000	0.000	0.000
133	A	133	ASP	-1	-0.795	-0.906	10.358	-0.179	-0.179	0.000	0.000	0.000	0.000
134	A	134	GLY	0	-0.031	-0.026	13.343	0.048	0.048	0.000	0.000	0.000	0.000
135	A	135	GLY	0	-0.013	-0.002	15.597	-0.011	-0.011	0.000	0.000	0.000	0.000
136	A	136	VAL	0	-0.018	-0.010	18.471	0.014	0.014	0.000	0.000	0.000	0.000
137	A	137	ASN	0	-0.035	-0.030	21.886	0.004	0.004	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.003	0.012	19.233	0.003	0.003	0.000	0.000	0.000	0.000

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