FMO DATABASE

FMODB ID: 17QKZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1154643.529822
FMO2-HF: Nuclear repulsion	1103914.633976
FMO2-HF: Total energy	-50728.895847
FMO2-MP2: Total energy	-50880.42509

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.
-24.13	-11.992	13.729	-9.534	-16.33	-0.078

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 : -0.019 / 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	3	VAL	0	0.025	0.022	3.115	-2.087	0.358	0.205	-1.090	-1.559	-0.001
4	A	4	GLU	-1	-0.833	-0.892	4.923	0.257	0.290	-0.001	-0.004	-0.028	0.000
5	A	5	ILE	0	0.017	0.032	8.573	-0.020	-0.020	0.000	0.000	0.000	0.000
6	A	6	GLY	0	0.014	0.002	11.863	0.045	0.045	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.786	0.881	13.237	-0.033	-0.033	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.002	0.012	17.882	0.006	0.006	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.013	-0.001	21.022	0.005	0.005	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.023	0.004	24.785	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.007	0.015	27.406	0.004	0.004	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.015	0.009	30.701	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.008	0.005	31.960	0.002	0.002	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.076	-0.049	29.581	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.016	-0.022	25.800	0.000	0.000	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.024	-0.013	22.795	0.004	0.004	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.798	-0.892	19.337	-0.099	-0.099	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.026	-0.009	15.589	0.013	0.013	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.017	0.007	13.801	-0.017	-0.017	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.021	0.007	8.818	0.014	0.014	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.014	-0.012	8.582	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.047	0.019	4.255	-0.279	-0.044	0.000	-0.023	-0.212	0.000
23	A	23	ARG	1	0.839	0.878	3.745	-0.307	-0.025	0.001	-0.059	-0.224	0.000
24	A	24	GLY	0	-0.008	-0.005	2.815	-2.808	-0.549	0.949	-1.510	-1.698	-0.016
25	A	25	VAL	0	-0.029	-0.009	2.620	-5.005	-1.744	1.127	-1.786	-2.602	-0.021
26	A	26	PRO	0	0.004	0.019	2.266	-0.031	0.197	1.457	-0.376	-1.308	0.003
27	A	27	SER	0	-0.011	-0.025	4.741	0.116	0.131	-0.001	-0.005	-0.009	0.000
28	A	28	LYS	1	0.784	0.876	8.186	0.599	0.599	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.027	0.015	7.362	0.081	0.081	0.000	0.000	0.000	0.000
30	A	30	ILE	0	-0.051	-0.031	2.530	-0.787	-0.191	0.329	-0.179	-0.746	0.000
31	A	31	ALA	0	0.024	0.012	6.647	0.153	0.153	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.046	-0.038	8.976	0.087	0.087	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.047	-0.016	6.842	-0.135	-0.135	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.847	-0.900	8.940	-0.316	-0.316	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.018	0.001	7.517	-0.047	-0.047	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.020	0.003	11.968	0.035	0.035	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.004	-0.014	9.592	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.865	0.925	15.255	0.090	0.090	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.011	-0.003	18.297	0.001	0.001	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.716	-0.844	21.054	-0.035	-0.035	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.013	0.023	24.846	0.003	0.003	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.104	-0.063	27.150	0.004	0.004	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.070	-0.031	26.107	0.004	0.004	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.027	-0.011	21.796	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.799	-0.884	25.399	-0.053	-0.053	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.012	-0.002	21.006	0.002	0.002	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.017	-0.005	23.984	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.001	-0.002	22.765	0.001	0.001	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.012	-0.008	16.155	0.005	0.005	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.796	-0.845	18.722	-0.124	-0.124	0.000	0.000	0.000	0.000
51	A	51	PRO	0	0.042	0.022	14.892	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.009	-0.010	13.756	0.028	0.028	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.822	-0.918	13.599	-0.210	-0.210	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.069	-0.014	7.673	0.013	0.013	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.026	0.000	10.983	-0.047	-0.047	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.000	-0.003	12.900	0.038	0.038	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.758	-0.846	15.452	-0.189	-0.189	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.034	-0.017	17.701	0.010	0.010	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.069	-0.029	20.667	0.014	0.014	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.064	0.025	16.908	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	61	THR	0	-0.023	-0.028	17.423	-0.017	-0.017	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.712	0.864	19.744	0.193	0.193	0.000	0.000	0.000	0.000
63	A	63	SER	0	0.044	0.000	14.609	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	64	PHE	0	-0.078	-0.037	12.398	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.853	-0.919	15.433	-0.154	-0.154	0.000	0.000	0.000	0.000
66	A	66	THR	0	-0.093	-0.055	15.609	-0.020	-0.020	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.022	0.024	17.996	0.017	0.017	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.001	-0.012	19.683	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.005	0.003	21.483	0.006	0.006	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.035	0.010	24.608	0.003	0.003	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.913	-0.956	26.575	-0.061	-0.061	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.880	0.941	23.595	0.090	0.090	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.796	0.881	23.878	0.042	0.042	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.007	0.008	19.328	0.001	0.001	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.017	-0.015	16.619	0.010	0.010	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.004	0.005	15.869	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.019	-0.003	12.103	0.023	0.023	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.022	0.008	13.056	-0.028	-0.028	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.022	-0.020	9.307	0.028	0.028	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.016	-0.004	11.801	-0.048	-0.048	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.728	-0.816	12.947	-0.245	-0.245	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.801	-0.896	14.583	-0.177	-0.177	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.109	-0.069	18.006	0.025	0.025	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.003	0.007	18.238	0.019	0.019	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.134	-0.088	17.896	0.014	0.014	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.052	0.016	14.090	0.001	0.001	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.069	-0.030	14.224	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.037	-0.034	15.135	0.010	0.010	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.001	0.013	10.228	-0.024	-0.024	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.014	0.004	6.575	0.036	0.036	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.008	-0.005	7.626	-0.148	-0.148	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.787	0.886	8.771	0.312	0.312	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.773	-0.877	5.699	-0.475	-0.475	0.000	0.000	0.000	0.000
94	A	94	GLY	0	-0.015	-0.018	7.560	0.077	0.077	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.053	-0.027	9.151	-0.035	-0.035	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.027	0.011	8.240	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.018	0.003	10.363	0.013	0.013	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.805	0.882	13.419	0.128	0.128	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.030	0.022	14.841	0.003	0.003	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.802	0.879	18.224	0.116	0.116	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.006	-0.005	21.921	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	102	THR	0	0.012	0.011	23.894	0.005	0.005	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.001	0.014	26.169	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.814	0.894	28.237	0.046	0.046	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.004	-0.012	29.832	0.004	0.004	0.000	0.000	0.000	0.000
106	A	106	SER	0	0.010	-0.002	29.481	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.043	-0.010	29.123	0.004	0.004	0.000	0.000	0.000	0.000
108	A	108	PRO	0	0.025	0.005	24.541	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.037	0.023	23.585	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	110	TYR	0	-0.040	-0.035	19.759	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.019	-0.012	15.416	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.031	-0.016	15.076	0.009	0.009	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.028	0.005	10.616	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.865	-0.928	13.330	-0.069	-0.069	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.955	-0.969	13.683	-0.165	-0.165	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.052	-0.039	7.950	-0.034	-0.034	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.025	0.030	11.238	0.052	0.052	0.000	0.000	0.000	0.000
118	A	118	GLY	0	-0.028	-0.009	10.700	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	119	PHE	0	-0.047	-0.074	2.321	-0.933	-0.158	0.822	-0.390	-1.207	-0.003
120	A	120	ALA	0	0.059	0.053	5.584	-0.314	-0.314	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.770	-0.886	6.152	-0.752	-0.752	0.000	0.000	0.000	0.000
122	A	122	ASN	0	-0.008	-0.026	7.627	0.115	0.115	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.931	-0.933	10.665	-0.301	-0.301	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.043	-0.028	11.208	0.047	0.047	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.034	-0.006	8.398	0.044	0.044	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.825	-0.902	7.677	-0.949	-0.949	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.078	-0.039	2.531	-1.035	-0.260	0.552	-0.241	-1.086	0.000
128	A	128	LYS	1	0.880	0.942	3.217	-1.736	-0.899	0.015	-0.291	-0.561	0.000
129	A	129	VAL	0	0.054	0.038	1.983	-7.788	-7.599	8.266	-3.814	-4.641	-0.040
130	A	130	SER	0	-0.053	-0.036	3.380	1.289	1.497	0.008	0.234	-0.449	0.000
131	A	131	PHE	0	0.053	0.031	5.373	-0.341	-0.341	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.043	-0.014	7.933	0.148	0.148	0.000	0.000	0.000	0.000
133	A	133	ASP	-1	-0.777	-0.886	10.479	-0.086	-0.086	0.000	0.000	0.000	0.000
134	A	134	GLY	0	-0.007	-0.021	13.610	0.030	0.030	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.016	0.009	15.707	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	136	VAL	0	-0.013	-0.006	18.755	0.006	0.006	0.000	0.000	0.000	0.000
137	A	137	ASN	0	-0.023	-0.028	22.154	0.003	0.003	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.037	0.011	19.112	0.008	0.008	0.000	0.000	0.000	0.000

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