FMO DATABASE

FMODB ID: V54L1

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	OptHSide
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	-1149546.335827
FMO2-HF: Nuclear repulsion	1098817.662568
FMO2-HF: Total energy	-50728.673259
FMO2-MP2: Total energy	-50880.117233

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.
-19.588	-7.137	10.712	-7.901	-15.258	-0.061

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 : -0.032 / q_NPA : -0.005

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	0.035	0.024	2.966	-1.608	0.594	0.067	-0.838	-1.430	0.003
4	A	4	GLU	-1	-0.839	-0.900	4.928	0.353	0.381	-0.001	-0.003	-0.024	0.000
5	A	5	ILE	0	0.005	0.020	8.585	0.000	0.000	0.000	0.000	0.000	0.000
6	A	6	GLY	0	0.011	-0.001	11.714	0.046	0.046	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.837	0.918	13.697	-0.113	-0.113	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.003	0.011	17.803	0.012	0.012	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.013	0.003	20.825	0.001	0.001	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.009	-0.006	24.576	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.007	0.014	27.200	0.002	0.002	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.018	0.011	30.491	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.013	0.001	31.770	0.002	0.002	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.081	-0.046	29.587	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.018	-0.019	25.782	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.017	-0.010	22.664	0.005	0.005	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.785	-0.896	19.757	-0.062	-0.062	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.043	-0.018	15.563	0.014	0.014	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.020	0.011	13.892	-0.020	-0.020	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.027	0.010	8.584	0.013	0.013	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.029	-0.026	8.695	0.002	0.002	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.051	0.029	4.322	-0.310	-0.081	-0.001	-0.016	-0.212	0.000
23	A	23	ARG	1	0.851	0.889	3.848	-0.688	-0.393	0.000	-0.073	-0.222	0.000
24	A	24	GLY	0	0.001	0.000	2.440	-2.154	-0.610	2.485	-2.022	-2.006	-0.019
25	A	25	VAL	0	-0.040	-0.009	2.559	-4.284	-1.553	1.906	-1.783	-2.854	-0.020
26	A	26	PRO	0	0.003	0.013	2.165	0.402	0.008	2.116	-0.320	-1.402	0.001
27	A	27	SER	0	0.001	-0.019	4.920	-0.004	0.016	-0.001	-0.004	-0.015	0.000
28	A	28	LYS	1	0.780	0.877	8.400	0.437	0.437	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.039	0.028	7.272	0.043	0.043	0.000	0.000	0.000	0.000
30	A	30	ILE	0	-0.048	-0.019	2.630	-0.819	-0.236	0.242	-0.163	-0.661	0.000
31	A	31	ALA	0	0.038	0.016	6.762	0.134	0.134	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.048	-0.030	8.911	0.067	0.067	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.009	-0.006	6.549	-0.157	-0.157	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.864	-0.906	8.663	-0.359	-0.359	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.020	0.004	7.198	-0.069	-0.069	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.010	0.006	11.548	0.055	0.055	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.004	-0.008	9.567	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.960	0.989	15.019	0.128	0.128	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.001	-0.001	18.197	0.006	0.006	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.745	-0.868	20.738	-0.053	-0.053	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.017	-0.003	24.493	0.005	0.005	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.096	-0.051	26.556	0.006	0.006	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.054	-0.016	25.817	0.004	0.004	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.017	-0.013	21.746	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.816	-0.894	25.530	-0.055	-0.055	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.012	-0.019	20.795	0.004	0.004	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.046	-0.022	23.830	0.000	0.000	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.008	0.003	22.850	0.000	0.000	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.015	-0.007	16.151	0.006	0.006	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.809	-0.859	18.523	-0.100	-0.100	0.000	0.000	0.000	0.000
51	A	51	PRO	0	0.027	0.017	15.108	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.009	-0.010	13.350	0.025	0.025	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.862	-0.944	14.068	-0.090	-0.090	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.093	-0.036	7.767	0.011	0.011	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.033	-0.002	11.184	-0.037	-0.037	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.004	-0.008	13.297	0.030	0.030	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.765	-0.844	15.775	-0.159	-0.159	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.016	-0.015	17.877	0.009	0.009	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.074	-0.030	20.844	0.010	0.010	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.052	0.014	17.193	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	61	THR	0	-0.017	-0.018	17.587	-0.016	-0.016	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.720	0.879	19.994	0.165	0.165	0.000	0.000	0.000	0.000
63	A	63	SER	0	0.044	-0.007	14.590	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	64	PHE	0	-0.093	-0.043	12.470	-0.037	-0.037	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.839	-0.914	15.407	-0.155	-0.155	0.000	0.000	0.000	0.000
66	A	66	THR	0	-0.082	-0.048	15.549	-0.022	-0.022	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.022	0.030	17.898	0.018	0.018	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.006	-0.012	19.668	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.006	0.001	21.313	0.008	0.008	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.033	0.005	24.123	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.907	-0.948	26.123	-0.074	-0.074	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.901	0.945	23.234	0.118	0.118	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.799	0.899	23.434	0.060	0.060	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.005	-0.002	18.881	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.024	-0.010	16.443	0.014	0.014	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.008	-0.002	15.732	-0.017	-0.017	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.020	-0.001	11.879	0.032	0.032	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.009	-0.001	12.637	-0.043	-0.043	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.026	-0.019	8.998	0.041	0.041	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.028	0.001	11.479	-0.061	-0.061	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.735	-0.822	12.537	-0.206	-0.206	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.811	-0.909	14.207	-0.163	-0.163	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.128	-0.077	17.614	0.022	0.022	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.021	0.010	17.825	0.017	0.017	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.136	-0.081	18.226	0.011	0.011	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.060	0.029	14.239	0.003	0.003	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.066	-0.033	14.309	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.059	-0.038	15.228	0.015	0.015	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.022	0.018	10.175	-0.026	-0.026	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.011	0.001	6.939	0.050	0.050	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.010	-0.014	7.884	-0.092	-0.092	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.844	0.931	8.975	0.158	0.158	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.792	-0.893	6.062	0.242	0.242	0.000	0.000	0.000	0.000
94	A	94	GLY	0	-0.016	-0.020	7.771	0.034	0.034	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.028	-0.014	8.904	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.045	0.024	8.124	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.023	0.012	10.225	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.819	0.893	13.392	0.092	0.092	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.024	0.022	14.866	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.831	0.890	18.248	0.096	0.096	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.012	0.001	21.984	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	102	THR	0	0.027	0.015	23.971	0.007	0.007	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.014	0.007	26.006	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.849	0.914	28.146	0.047	0.047	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.009	-0.014	29.781	0.004	0.004	0.000	0.000	0.000	0.000
106	A	106	SER	0	0.006	-0.003	29.443	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.058	-0.014	29.265	0.005	0.005	0.000	0.000	0.000	0.000
108	A	108	PRO	0	0.041	0.012	24.620	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.023	0.015	23.311	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	110	TYR	0	-0.025	-0.018	19.553	0.001	0.001	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.008	-0.010	15.043	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.016	-0.012	14.898	0.012	0.012	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.010	-0.012	10.207	-0.021	-0.021	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.972	-0.987	12.789	-0.141	-0.141	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.936	-0.971	13.416	-0.254	-0.254	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.065	-0.046	7.819	-0.030	-0.030	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.021	0.036	10.686	0.067	0.067	0.000	0.000	0.000	0.000
118	A	118	GLY	0	-0.015	-0.007	10.527	-0.036	-0.036	0.000	0.000	0.000	0.000
119	A	119	PHE	0	-0.027	-0.058	2.391	-1.391	-0.438	1.088	-0.564	-1.477	-0.006
120	A	120	ALA	0	0.033	0.039	6.355	-0.190	-0.190	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.780	-0.900	6.082	-0.618	-0.618	0.000	0.000	0.000	0.000
122	A	122	ASN	0	-0.022	-0.034	7.362	0.066	0.066	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.946	-0.938	10.555	-0.251	-0.251	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.049	-0.033	11.194	0.034	0.034	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.023	0.011	9.175	0.028	0.028	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.830	-0.918	7.920	-0.972	-0.972	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.081	-0.048	3.085	-0.825	-0.126	0.102	-0.122	-0.679	0.000
128	A	128	LYS	1	0.943	0.975	4.096	-0.178	0.167	-0.001	-0.054	-0.289	0.000
129	A	129	VAL	0	0.011	0.004	2.302	-6.635	-3.812	2.703	-1.916	-3.610	-0.020
130	A	130	SER	0	-0.077	-0.034	3.629	0.991	1.384	0.007	-0.023	-0.377	0.000
131	A	131	PHE	0	0.050	0.023	5.404	-0.227	-0.227	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.053	-0.021	7.759	0.162	0.162	0.000	0.000	0.000	0.000
133	A	133	ASP	-1	-0.768	-0.887	10.399	-0.149	-0.149	0.000	0.000	0.000	0.000
134	A	134	GLY	0	-0.026	-0.031	13.381	0.047	0.047	0.000	0.000	0.000	0.000
135	A	135	GLY	0	-0.011	0.002	15.647	-0.011	-0.011	0.000	0.000	0.000	0.000
136	A	136	VAL	0	-0.021	-0.013	18.519	0.013	0.013	0.000	0.000	0.000	0.000
137	A	137	ASN	0	-0.027	-0.025	21.940	0.003	0.003	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.004	0.015	19.274	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:1:VAL)