FMO DATABASE

FMODB ID: JLQL9

Calculation Name: 1A9N-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	162
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1706971.616227
FMO2-HF: Nuclear repulsion	1642373.482025
FMO2-HF: Total energy	-64598.134203
FMO2-MP2: Total energy	-64789.739485

3D Structure Molmil

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.
-8.03	-2.687	4.7	-3.332	-6.712	-0.024

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 : -0.022 / q_NPA : -0.017

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	0.025	0.033	3.848	-2.135	-0.547	-0.007	-0.658	-0.922	0.003
4	A	5	THR	0	-0.030	-0.047	5.643	0.637	0.637	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.020	0.010	8.092	-0.198	-0.198	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.754	-0.864	8.563	0.242	0.242	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.070	-0.027	3.641	-0.449	-0.118	0.017	-0.066	-0.283	0.000
8	A	9	ILE	0	-0.010	-0.012	7.244	-0.108	-0.108	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.959	-0.983	10.416	-0.057	-0.057	0.000	0.000	0.000	0.000
10	A	11	GLN	0	-0.094	-0.048	8.076	0.067	0.067	0.000	0.000	0.000	0.000
11	A	12	ALA	0	-0.028	0.009	9.620	-0.051	-0.051	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.006	0.009	11.147	0.107	0.107	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.061	0.027	14.100	0.003	0.003	0.000	0.000	0.000	0.000
14	A	15	TYR	0	-0.100	-0.068	15.902	0.039	0.039	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.010	-0.007	20.131	0.002	0.002	0.000	0.000	0.000	0.000
16	A	17	ASN	0	0.029	0.010	20.876	0.029	0.029	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.006	-0.010	22.637	0.022	0.022	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.028	-0.011	24.490	0.017	0.017	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.886	0.941	25.942	0.167	0.167	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.804	-0.887	22.512	-0.218	-0.218	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.792	0.879	20.645	0.228	0.228	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.829	-0.891	16.855	-0.401	-0.401	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.005	0.002	11.886	0.023	0.023	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.883	-0.940	11.780	-0.904	-0.904	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.008	-0.012	7.664	-0.056	-0.056	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.850	0.900	7.965	0.363	0.363	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.011	0.006	7.900	-0.120	-0.120	0.000	0.000	0.000	0.000
28	A	29	TYR	0	-0.020	-0.009	3.053	-0.759	-0.129	0.076	-0.132	-0.574	0.000
29	A	30	LYS	1	0.852	0.912	2.390	-2.880	-1.958	4.045	-1.697	-3.270	-0.020
30	A	31	ILE	0	0.056	0.040	2.861	-1.746	-0.459	0.540	-0.666	-1.161	-0.007
31	A	32	PRO	0	-0.040	-0.025	3.105	0.696	1.281	0.029	-0.113	-0.502	0.000
32	A	33	VAL	0	-0.026	-0.032	5.988	0.446	0.446	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.010	0.020	8.136	-0.278	-0.278	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.758	-0.869	8.310	0.790	0.790	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.053	-0.051	9.126	-0.081	-0.081	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.060	0.029	11.775	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	38	GLY	0	-0.004	0.020	13.253	0.001	0.001	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.031	0.020	13.108	0.012	0.012	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.011	-0.020	13.852	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.042	-0.018	16.140	0.010	0.010	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.780	-0.888	19.104	-0.152	-0.152	0.000	0.000	0.000	0.000
42	A	43	GLN	0	-0.081	-0.036	19.134	0.022	0.022	0.000	0.000	0.000	0.000
43	A	44	PHE	0	-0.039	-0.030	15.447	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.764	-0.826	20.053	-0.186	-0.186	0.000	0.000	0.000	0.000
45	A	46	ALA	0	0.026	0.007	19.320	0.006	0.006	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.001	-0.006	12.909	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.758	-0.833	13.950	-0.612	-0.612	0.000	0.000	0.000	0.000
48	A	49	PHE	0	0.074	0.021	8.692	-0.081	-0.081	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.057	-0.045	10.654	-0.073	-0.073	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.829	-0.903	10.773	-0.876	-0.876	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.072	-0.033	6.039	-0.903	-0.903	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.826	-0.889	5.787	-0.649	-0.649	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.060	0.049	7.661	0.245	0.245	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.885	0.923	7.305	0.559	0.559	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.797	0.898	12.466	0.146	0.146	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.027	0.024	13.885	-0.050	-0.050	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.795	-0.915	15.070	-0.045	-0.045	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.005	0.002	15.030	-0.050	-0.050	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.005	-0.003	15.317	-0.013	-0.013	0.000	0.000	0.000	0.000
60	A	61	PRO	0	-0.011	0.003	15.736	0.039	0.039	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.030	-0.028	18.831	-0.020	-0.020	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.042	-0.011	16.522	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.937	0.951	21.254	0.088	0.088	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.824	0.900	22.670	0.190	0.190	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.013	0.000	17.164	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.829	0.923	21.362	0.190	0.190	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.017	-0.013	20.627	0.011	0.011	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.008	0.000	15.667	-0.033	-0.033	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.004	0.010	16.403	0.028	0.028	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.037	0.005	12.925	-0.080	-0.080	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.021	0.008	14.854	0.072	0.072	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.045	-0.020	13.564	-0.036	-0.036	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.016	0.004	9.862	-0.233	-0.233	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.831	0.890	8.804	0.684	0.684	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.004	0.012	12.913	0.068	0.068	0.000	0.000	0.000	0.000
76	A	77	CYS	0	-0.024	-0.027	15.112	0.041	0.041	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.848	0.901	17.549	0.108	0.108	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.030	0.007	17.855	-0.042	-0.042	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.031	0.017	19.617	0.026	0.026	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.868	-0.950	20.779	-0.075	-0.075	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.009	0.009	23.496	0.005	0.005	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.008	0.000	19.004	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.807	-0.879	22.972	-0.091	-0.091	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.066	-0.043	25.623	0.010	0.010	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.026	0.000	20.743	0.008	0.008	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.019	0.006	18.655	-0.012	-0.012	0.000	0.000	0.000	0.000
87	A	88	PRO	0	-0.004	-0.005	22.950	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.903	-0.941	25.580	-0.134	-0.134	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.005	0.010	21.160	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.017	-0.007	24.413	0.014	0.014	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.954	-0.994	22.967	-0.240	-0.240	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.008	0.014	18.809	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.025	-0.018	19.927	0.025	0.025	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.052	0.019	16.727	-0.047	-0.047	0.000	0.000	0.000	0.000
95	A	96	THR	0	0.002	0.000	18.918	0.025	0.025	0.000	0.000	0.000	0.000
96	A	97	ASN	0	-0.065	-0.037	16.816	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.008	-0.003	14.840	-0.089	-0.089	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.011	-0.017	16.567	0.020	0.020	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.005	0.020	18.444	0.033	0.033	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.012	0.000	21.155	0.003	0.003	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.857	-0.923	24.143	-0.065	-0.065	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.006	-0.010	26.329	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.038	0.024	28.490	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.764	-0.865	22.665	-0.103	-0.103	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.025	-0.020	23.530	-0.016	-0.016	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.743	-0.839	25.658	-0.079	-0.079	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.023	0.014	23.671	0.002	0.002	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.001	0.010	22.670	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	110	ALA	0	0.009	0.014	26.102	0.000	0.000	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.051	-0.020	26.494	0.003	0.003	0.000	0.000	0.000	0.000
111	A	112	LEU	0	0.053	0.021	23.486	0.006	0.006	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.827	0.892	27.801	0.079	0.079	0.000	0.000	0.000	0.000
113	A	114	SER	0	0.027	0.007	28.245	0.002	0.002	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.025	0.012	25.196	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.055	-0.040	28.299	0.017	0.017	0.000	0.000	0.000	0.000
116	A	117	TYR	0	-0.013	-0.011	26.768	0.014	0.014	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.051	0.032	23.765	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	119	CYS	0	-0.071	-0.023	22.906	0.020	0.020	0.000	0.000	0.000	0.000
119	A	120	ILE	0	0.079	0.028	22.350	-0.022	-0.022	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.015	0.014	23.480	0.004	0.004	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.861	0.916	20.038	0.269	0.269	0.000	0.000	0.000	0.000
122	A	123	ASN	0	0.047	0.046	19.988	-0.026	-0.026	0.000	0.000	0.000	0.000
123	A	124	PRO	0	0.012	-0.001	21.456	0.018	0.018	0.000	0.000	0.000	0.000
124	A	125	VAL	0	0.012	0.008	24.171	0.014	0.014	0.000	0.000	0.000	0.000
125	A	126	THR	0	-0.016	-0.006	25.835	0.006	0.006	0.000	0.000	0.000	0.000
126	A	127	ASN	0	-0.049	-0.030	26.880	0.009	0.009	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.789	0.899	27.921	0.099	0.099	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.974	0.971	31.662	0.058	0.058	0.000	0.000	0.000	0.000
129	A	130	HIS	0	0.017	-0.010	34.927	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	131	TYR	0	0.012	-0.005	27.471	0.001	0.001	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.805	0.873	32.158	0.122	0.122	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.023	-0.016	33.280	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	TYR	0	-0.010	-0.023	30.426	0.005	0.005	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.031	0.011	28.860	0.002	0.002	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.053	-0.025	31.672	0.001	0.001	0.000	0.000	0.000	0.000
136	A	137	TYR	0	-0.041	-0.031	34.735	0.002	0.002	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.804	0.898	31.557	0.074	0.074	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.020	-0.003	28.500	0.000	0.000	0.000	0.000	0.000	0.000
139	A	140	PRO	0	0.019	0.033	31.713	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	141	GLN	0	0.032	0.003	30.191	0.007	0.007	0.000	0.000	0.000	0.000
141	A	142	VAL	0	0.012	0.036	29.163	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.801	0.867	31.913	0.127	0.127	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.061	-0.029	30.532	0.007	0.007	0.000	0.000	0.000	0.000
144	A	145	LEU	0	0.067	0.042	28.047	-0.008	-0.008	0.000	0.000	0.000	0.000
145	A	146	ASP	-1	-0.756	-0.871	26.633	-0.175	-0.175	0.000	0.000	0.000	0.000
146	A	147	PHE	0	0.012	-0.008	24.483	0.008	0.008	0.000	0.000	0.000	0.000
147	A	148	GLN	0	-0.022	0.006	30.098	0.017	0.017	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.983	0.987	33.496	0.100	0.100	0.000	0.000	0.000	0.000
149	A	150	VAL	0	0.015	0.005	33.717	0.005	0.005	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.825	0.904	36.410	0.106	0.106	0.000	0.000	0.000	0.000
151	A	152	LEU	0	0.062	0.018	40.175	0.001	0.001	0.000	0.000	0.000	0.000
152	A	153	LYS	1	0.930	0.978	43.063	0.068	0.068	0.000	0.000	0.000	0.000
153	A	154	GLU	-1	-0.678	-0.807	37.513	-0.102	-0.102	0.000	0.000	0.000	0.000
154	A	155	ARG	1	0.888	0.940	35.979	0.094	0.094	0.000	0.000	0.000	0.000
155	A	156	GLN	0	0.021	0.010	40.722	0.005	0.005	0.000	0.000	0.000	0.000
156	A	157	GLU	-1	-0.896	-0.947	41.876	-0.062	-0.062	0.000	0.000	0.000	0.000
157	A	158	ALA	0	-0.024	-0.020	38.371	0.003	0.003	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.759	-0.842	40.294	-0.051	-0.051	0.000	0.000	0.000	0.000
159	A	160	LYS	1	0.743	0.867	43.122	0.061	0.061	0.000	0.000	0.000	0.000
160	A	161	MET	0	-0.018	-0.009	39.771	0.002	0.002	0.000	0.000	0.000	0.000
161	A	162	PHE	0	0.004	-0.007	36.636	-0.002	-0.002	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.828	0.921	40.746	0.049	0.049	0.000	0.000	0.000	0.000

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