FMO DATABASE

FMODB ID: 8595Y

Calculation Name: 1A9N-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A9N

Chain ID: A

ChEMBL ID:

UniProt ID: P09661

Base Structure: X-ray

Registration Date: 2023-06-22

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	162
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1701344.914429
FMO2-HF: Nuclear repulsion	1636748.739687
FMO2-HF: Total energy	-64596.174742
FMO2-MP2: Total energy	-64787.717805

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:2:VAL)

Summations of interaction energy for fragment #1(A:2: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.
-6.203	-5.632	14.481	-4.921	-10.131	-0.03

Interaction energy analysis for fragmet #1(A:2:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.050 / q_NPA : -0.024

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	LEU	0	0.056	0.040	3.686	-2.728	-0.792	0.003	-0.746	-1.194	0.005
4	A	5	THR	0	-0.041	-0.018	5.417	0.730	0.730	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.048	0.017	7.643	-0.243	-0.243	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.796	-0.922	8.244	0.456	0.456	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.104	-0.031	3.047	-0.617	-0.139	0.196	-0.112	-0.562	0.000
8	A	9	ILE	0	0.016	-0.004	6.871	-0.133	-0.133	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.950	-0.972	9.726	0.010	0.010	0.000	0.000	0.000	0.000
10	A	11	GLN	0	-0.114	-0.048	7.851	0.075	0.075	0.000	0.000	0.000	0.000
11	A	12	ALA	0	-0.036	-0.005	9.309	-0.048	-0.048	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.003	0.007	10.984	0.101	0.101	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.045	0.008	13.861	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	15	TYR	0	-0.057	-0.027	15.652	0.039	0.039	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.042	-0.026	19.738	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	17	ASN	0	0.020	-0.004	20.274	0.035	0.035	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.027	-0.004	22.459	0.024	0.024	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.037	-0.016	24.189	0.019	0.019	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.854	0.928	26.076	0.175	0.175	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.851	-0.908	22.871	-0.221	-0.221	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.834	0.909	20.091	0.225	0.225	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.814	-0.904	16.429	-0.469	-0.469	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.028	-0.004	11.511	0.023	0.023	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.879	-0.952	11.671	-0.898	-0.898	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.010	-0.015	6.980	-0.071	-0.071	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.912	0.973	7.810	0.393	0.393	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.010	0.001	7.596	-0.076	-0.076	0.000	0.000	0.000	0.000
28	A	29	TYR	0	0.008	0.012	2.734	-0.953	-0.084	0.393	-0.280	-0.981	0.001
29	A	30	LYS	1	0.875	0.935	2.057	0.114	-3.010	10.071	-2.545	-4.403	-0.024
30	A	31	ILE	0	0.036	0.033	2.430	-1.962	-2.015	3.803	-1.229	-2.521	-0.013
31	A	32	PRO	0	-0.008	0.003	3.454	1.105	1.570	0.015	-0.009	-0.470	0.001
32	A	33	VAL	0	-0.007	-0.029	6.228	0.464	0.464	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.010	0.012	8.019	-0.238	-0.238	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.826	-0.891	8.372	0.778	0.778	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.042	-0.025	9.283	-0.059	-0.059	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.076	0.030	11.175	-0.027	-0.027	0.000	0.000	0.000	0.000
37	A	38	GLY	0	-0.006	0.014	13.456	0.003	0.003	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.045	0.018	13.023	0.006	0.006	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.032	-0.020	13.356	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.012	-0.017	15.674	0.006	0.006	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.789	-0.874	18.578	-0.154	-0.154	0.000	0.000	0.000	0.000
42	A	43	GLN	0	-0.067	-0.021	19.271	0.030	0.030	0.000	0.000	0.000	0.000
43	A	44	PHE	0	-0.053	-0.037	15.981	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.738	-0.824	19.542	-0.199	-0.199	0.000	0.000	0.000	0.000
45	A	46	ALA	0	0.012	0.011	18.724	0.002	0.002	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.027	0.000	12.422	0.005	0.005	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.816	-0.869	13.492	-0.723	-0.723	0.000	0.000	0.000	0.000
48	A	49	PHE	0	0.043	0.000	9.041	-0.097	-0.097	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.063	-0.047	10.445	-0.097	-0.097	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.887	-0.933	10.234	-1.032	-1.032	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.021	-0.024	5.736	-1.022	-1.022	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.981	-1.008	5.971	-1.283	-1.283	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.043	0.027	7.752	0.261	0.261	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.904	0.939	7.947	0.765	0.765	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.898	0.970	12.622	0.209	0.209	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.038	0.029	13.751	-0.055	-0.055	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.903	-0.981	14.789	-0.073	-0.073	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.070	0.030	14.551	-0.061	-0.061	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.020	-0.007	15.075	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	61	PRO	0	-0.003	0.012	15.715	0.040	0.040	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.006	-0.006	18.782	-0.017	-0.017	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.051	-0.028	16.432	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.931	0.942	21.174	0.092	0.092	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.793	0.881	22.375	0.199	0.199	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.004	-0.006	17.435	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.867	0.943	21.158	0.206	0.206	0.000	0.000	0.000	0.000
67	A	68	THR	0	0.016	0.001	19.916	0.014	0.014	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.024	0.013	15.659	-0.033	-0.033	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.000	0.011	16.179	0.030	0.030	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.026	0.005	12.961	-0.088	-0.088	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.000	0.001	14.701	0.053	0.053	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.025	-0.011	13.185	-0.037	-0.037	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.010	0.018	9.592	-0.323	-0.323	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.873	0.934	10.054	0.849	0.849	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.016	0.008	13.114	0.064	0.064	0.000	0.000	0.000	0.000
76	A	77	CYS	0	-0.019	-0.021	15.249	0.053	0.053	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.968	0.968	17.422	0.161	0.161	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.011	0.013	17.832	-0.049	-0.049	0.000	0.000	0.000	0.000
79	A	80	GLY	0	-0.011	-0.004	19.196	0.030	0.030	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.897	-0.967	20.590	-0.107	-0.107	0.000	0.000	0.000	0.000
81	A	82	GLY	0	-0.027	-0.005	23.155	0.005	0.005	0.000	0.000	0.000	0.000
82	A	83	LEU	0	0.016	-0.003	19.090	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.816	-0.904	22.876	-0.110	-0.110	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.079	-0.047	25.539	0.012	0.012	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.018	-0.005	20.645	0.011	0.011	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.032	-0.004	18.937	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	88	PRO	0	-0.017	-0.010	22.979	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.922	-0.973	25.685	-0.145	-0.145	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.007	0.028	20.981	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.032	-0.017	24.357	0.018	0.018	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.942	-0.990	22.600	-0.276	-0.276	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.004	0.006	18.766	-0.023	-0.023	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.025	-0.015	19.403	0.023	0.023	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.080	0.017	17.140	-0.050	-0.050	0.000	0.000	0.000	0.000
95	A	96	THR	0	-0.030	0.002	18.779	0.008	0.008	0.000	0.000	0.000	0.000
96	A	97	ASN	0	-0.111	-0.085	16.678	-0.015	-0.015	0.000	0.000	0.000	0.000
97	A	98	ASN	0	0.011	0.004	14.850	-0.113	-0.113	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.044	-0.038	16.965	0.038	0.038	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.025	0.030	18.694	0.031	0.031	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.032	0.006	21.331	0.006	0.006	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-1.006	-1.009	24.335	-0.090	-0.090	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.017	0.005	26.534	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.061	0.030	28.446	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.884	-0.951	23.123	-0.148	-0.148	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.067	-0.041	23.868	-0.018	-0.018	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.826	-0.851	25.703	-0.110	-0.110	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.033	0.015	23.699	0.003	0.003	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.028	-0.016	22.426	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	110	ALA	0	0.005	0.008	26.168	0.003	0.003	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.038	0.002	26.954	0.006	0.006	0.000	0.000	0.000	0.000
111	A	112	LEU	0	0.069	0.039	23.307	0.005	0.005	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.846	0.922	27.738	0.100	0.100	0.000	0.000	0.000	0.000
113	A	114	SER	0	0.088	0.050	28.907	0.004	0.004	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.029	0.023	24.677	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.066	-0.061	28.053	0.018	0.018	0.000	0.000	0.000	0.000
116	A	117	TYR	0	-0.013	-0.012	26.490	0.013	0.013	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.054	0.045	23.760	-0.016	-0.016	0.000	0.000	0.000	0.000
118	A	119	CYS	0	-0.034	0.004	22.588	0.022	0.022	0.000	0.000	0.000	0.000
119	A	120	ILE	0	0.053	0.014	22.108	-0.028	-0.028	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.043	0.014	23.401	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.926	0.970	20.479	0.318	0.318	0.000	0.000	0.000	0.000
122	A	123	ASN	0	0.069	0.059	20.167	-0.035	-0.035	0.000	0.000	0.000	0.000
123	A	124	PRO	0	0.021	0.003	21.675	0.024	0.024	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.012	-0.010	24.449	0.017	0.017	0.000	0.000	0.000	0.000
125	A	126	THR	0	-0.022	-0.010	26.292	0.013	0.013	0.000	0.000	0.000	0.000
126	A	127	ASN	0	-0.033	-0.016	28.072	0.011	0.011	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.933	0.973	28.865	0.137	0.137	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.964	0.974	31.839	0.081	0.081	0.000	0.000	0.000	0.000
129	A	130	HIS	0	0.029	-0.003	34.921	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	131	TYR	0	0.018	0.006	27.355	0.002	0.002	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.826	0.903	31.975	0.144	0.144	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.002	-0.013	33.302	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	134	TYR	0	-0.065	-0.096	30.342	0.005	0.005	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.014	0.007	28.965	0.001	0.001	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.062	-0.030	31.608	0.002	0.002	0.000	0.000	0.000	0.000
136	A	137	TYR	0	-0.015	-0.003	34.520	0.001	0.001	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.974	0.995	31.141	0.098	0.098	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.021	-0.011	28.592	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	140	PRO	0	0.011	0.016	31.833	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	141	GLN	0	0.005	0.006	29.942	0.009	0.009	0.000	0.000	0.000	0.000
141	A	142	VAL	0	0.032	0.047	28.791	-0.005	-0.005	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.786	0.870	31.627	0.146	0.146	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.048	-0.011	30.382	0.007	0.007	0.000	0.000	0.000	0.000
144	A	145	LEU	0	0.038	0.017	28.069	-0.008	-0.008	0.000	0.000	0.000	0.000
145	A	146	ASP	-1	-0.772	-0.872	26.729	-0.213	-0.213	0.000	0.000	0.000	0.000
146	A	147	PHE	0	-0.002	-0.024	24.287	0.010	0.010	0.000	0.000	0.000	0.000
147	A	148	GLN	0	-0.001	0.007	29.981	0.021	0.021	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.961	0.969	33.269	0.114	0.114	0.000	0.000	0.000	0.000
149	A	150	VAL	0	0.015	0.018	33.589	0.006	0.006	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.873	0.942	36.284	0.121	0.121	0.000	0.000	0.000	0.000
151	A	152	LEU	0	0.033	0.013	40.115	0.000	0.000	0.000	0.000	0.000	0.000
152	A	153	LYS	1	0.951	0.968	42.896	0.081	0.081	0.000	0.000	0.000	0.000
153	A	154	GLU	-1	-0.724	-0.857	37.089	-0.120	-0.120	0.000	0.000	0.000	0.000
154	A	155	ARG	1	0.917	0.944	35.851	0.114	0.114	0.000	0.000	0.000	0.000
155	A	156	GLN	0	0.029	0.003	40.718	0.004	0.004	0.000	0.000	0.000	0.000
156	A	157	GLU	-1	-1.037	-1.031	41.995	-0.083	-0.083	0.000	0.000	0.000	0.000
157	A	158	ALA	0	-0.010	-0.008	38.375	0.002	0.002	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.886	-0.927	40.449	-0.069	-0.069	0.000	0.000	0.000	0.000
159	A	160	LYS	1	0.841	0.930	42.951	0.073	0.073	0.000	0.000	0.000	0.000
160	A	161	MET	0	0.009	0.015	40.290	0.001	0.001	0.000	0.000	0.000	0.000
161	A	162	PHE	0	-0.002	-0.016	36.526	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.933	0.992	41.084	0.056	0.056	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:VAL)