FMO DATABASE

FMODB ID: 94J22

Calculation Name: 2A61-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2A61

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZG9

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	142
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1231102.980208
FMO2-HF: Nuclear repulsion	1174325.254023
FMO2-HF: Total energy	-56777.726185
FMO2-MP2: Total energy	-56945.700035

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:5:LYS)

Summations of interaction energy for fragment #1(A:5:LYS)

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.
97.234	101.937	1.303	-2.287	-3.719	0.002

Interaction energy analysis for fragmet #1(A:5:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.031 / q_NPA : 1.003

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	7	PRO	0	0.052	0.017	2.753	-1.380	1.399	0.494	-1.388	-1.885	0.006
4	A	8	PHE	0	0.029	0.013	2.474	-0.208	1.192	0.808	-0.721	-1.487	-0.004
5	A	9	GLU	-1	-0.799	-0.883	3.899	-28.380	-27.856	0.001	-0.178	-0.347	0.000
6	A	10	ARG	1	0.905	0.961	5.725	32.923	32.923	0.000	0.000	0.000	0.000
7	A	11	ILE	0	0.095	0.047	6.704	1.832	1.832	0.000	0.000	0.000	0.000
8	A	12	LEU	0	0.005	0.007	6.846	1.786	1.786	0.000	0.000	0.000	0.000
9	A	13	ARG	1	0.839	0.901	8.994	26.864	26.864	0.000	0.000	0.000	0.000
10	A	14	GLU	-1	-0.915	-0.962	11.704	-17.121	-17.121	0.000	0.000	0.000	0.000
11	A	15	ILE	0	0.014	0.008	11.752	1.272	1.272	0.000	0.000	0.000	0.000
12	A	16	CYS	0	-0.057	-0.039	12.869	1.059	1.059	0.000	0.000	0.000	0.000
13	A	17	PHE	0	-0.023	-0.013	15.607	0.983	0.983	0.000	0.000	0.000	0.000
14	A	18	MET	0	0.024	0.010	16.212	1.086	1.086	0.000	0.000	0.000	0.000
15	A	19	VAL	0	0.040	0.031	18.106	0.763	0.763	0.000	0.000	0.000	0.000
16	A	20	LYS	1	0.896	0.956	19.780	14.529	14.529	0.000	0.000	0.000	0.000
17	A	21	VAL	0	-0.017	-0.016	21.490	0.620	0.620	0.000	0.000	0.000	0.000
18	A	22	GLU	-1	-0.796	-0.880	23.358	-9.877	-9.877	0.000	0.000	0.000	0.000
19	A	23	GLY	0	0.045	0.014	24.416	0.414	0.414	0.000	0.000	0.000	0.000
20	A	24	ARG	1	0.800	0.867	25.180	12.261	12.261	0.000	0.000	0.000	0.000
21	A	25	LYS	1	0.835	0.910	26.728	10.853	10.853	0.000	0.000	0.000	0.000
22	A	26	VAL	0	0.014	0.018	30.004	0.265	0.265	0.000	0.000	0.000	0.000
23	A	27	LEU	0	-0.051	-0.024	29.310	0.194	0.194	0.000	0.000	0.000	0.000
24	A	28	ARG	1	0.928	0.969	33.048	8.742	8.742	0.000	0.000	0.000	0.000
25	A	29	ASP	-1	-0.868	-0.942	35.308	-8.313	-8.313	0.000	0.000	0.000	0.000
26	A	30	PHE	0	-0.004	0.005	35.266	0.197	0.197	0.000	0.000	0.000	0.000
27	A	31	GLY	0	0.023	0.024	37.717	0.122	0.122	0.000	0.000	0.000	0.000
28	A	32	ILE	0	-0.066	-0.020	33.203	-0.023	-0.023	0.000	0.000	0.000	0.000
29	A	33	THR	0	-0.003	-0.035	33.200	-0.276	-0.276	0.000	0.000	0.000	0.000
30	A	34	PRO	0	0.027	-0.013	27.711	-0.078	-0.078	0.000	0.000	0.000	0.000
31	A	35	ALA	0	0.045	0.022	29.190	-0.191	-0.191	0.000	0.000	0.000	0.000
32	A	36	GLN	0	0.078	0.060	30.336	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	37	PHE	0	0.083	0.035	26.802	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	38	ASP	-1	-0.823	-0.881	25.341	-12.504	-12.504	0.000	0.000	0.000	0.000
35	A	39	ILE	0	-0.014	0.001	28.246	-0.112	-0.112	0.000	0.000	0.000	0.000
36	A	40	LEU	0	0.016	0.015	31.115	0.031	0.031	0.000	0.000	0.000	0.000
37	A	41	GLN	0	0.018	-0.010	23.945	0.051	0.051	0.000	0.000	0.000	0.000
38	A	42	LYS	1	0.803	0.908	23.572	12.520	12.520	0.000	0.000	0.000	0.000
39	A	43	ILE	0	-0.009	-0.013	28.556	0.015	0.015	0.000	0.000	0.000	0.000
40	A	44	TYR	0	-0.044	-0.019	29.638	0.039	0.039	0.000	0.000	0.000	0.000
41	A	45	PHE	0	-0.024	-0.016	26.257	0.012	0.012	0.000	0.000	0.000	0.000
42	A	46	GLU	-1	-0.844	-0.900	25.326	-12.331	-12.331	0.000	0.000	0.000	0.000
43	A	47	GLY	0	0.034	0.029	29.703	0.150	0.150	0.000	0.000	0.000	0.000
44	A	48	PRO	0	-0.004	-0.018	33.289	-0.107	-0.107	0.000	0.000	0.000	0.000
45	A	49	LYS	1	0.866	0.944	28.875	10.423	10.423	0.000	0.000	0.000	0.000
46	A	50	ARG	1	0.841	0.910	34.293	8.835	8.835	0.000	0.000	0.000	0.000
47	A	51	PRO	0	0.027	-0.002	34.342	-0.297	-0.297	0.000	0.000	0.000	0.000
48	A	52	GLY	0	-0.037	-0.024	34.275	-0.146	-0.146	0.000	0.000	0.000	0.000
49	A	53	GLU	-1	-0.790	-0.897	30.637	-9.876	-9.876	0.000	0.000	0.000	0.000
50	A	54	LEU	0	0.036	0.010	29.579	-0.398	-0.398	0.000	0.000	0.000	0.000
51	A	55	SER	0	-0.090	-0.054	30.334	-0.137	-0.137	0.000	0.000	0.000	0.000
52	A	56	VAL	0	0.011	-0.006	26.227	-0.198	-0.198	0.000	0.000	0.000	0.000
53	A	57	LEU	0	-0.057	-0.017	25.086	-0.442	-0.442	0.000	0.000	0.000	0.000
54	A	58	LEU	0	-0.030	-0.019	25.224	-0.391	-0.391	0.000	0.000	0.000	0.000
55	A	59	GLY	0	0.034	0.040	26.357	-0.196	-0.196	0.000	0.000	0.000	0.000
56	A	60	VAL	0	-0.031	-0.008	27.238	0.221	0.221	0.000	0.000	0.000	0.000
57	A	61	ALA	0	0.049	0.034	30.845	0.103	0.103	0.000	0.000	0.000	0.000
58	A	62	LYS	1	0.998	0.981	34.243	9.178	9.178	0.000	0.000	0.000	0.000
59	A	63	SER	0	0.045	0.038	36.834	0.042	0.042	0.000	0.000	0.000	0.000
60	A	64	THR	0	0.043	0.017	33.302	0.136	0.136	0.000	0.000	0.000	0.000
61	A	65	VAL	0	0.015	0.014	33.204	0.037	0.037	0.000	0.000	0.000	0.000
62	A	66	THR	0	-0.021	-0.019	35.678	0.149	0.149	0.000	0.000	0.000	0.000
63	A	67	GLY	0	-0.009	-0.005	38.825	0.187	0.187	0.000	0.000	0.000	0.000
64	A	68	LEU	0	-0.059	-0.026	32.852	0.090	0.090	0.000	0.000	0.000	0.000
65	A	69	VAL	0	0.032	0.004	36.290	0.065	0.065	0.000	0.000	0.000	0.000
66	A	70	LYS	1	0.986	0.997	38.507	7.322	7.322	0.000	0.000	0.000	0.000
67	A	71	ARG	1	0.872	0.945	36.822	8.405	8.405	0.000	0.000	0.000	0.000
68	A	72	LEU	0	0.034	0.026	35.417	0.076	0.076	0.000	0.000	0.000	0.000
69	A	73	GLU	-1	-0.821	-0.880	40.120	-7.468	-7.468	0.000	0.000	0.000	0.000
70	A	74	ALA	0	-0.023	-0.005	42.991	0.134	0.134	0.000	0.000	0.000	0.000
71	A	75	ASP	-1	-0.909	-0.951	41.712	-7.386	-7.386	0.000	0.000	0.000	0.000
72	A	76	GLY	0	0.019	0.018	43.904	0.027	0.027	0.000	0.000	0.000	0.000
73	A	77	TYR	0	-0.050	-0.023	38.124	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	78	LEU	0	-0.031	-0.027	35.948	-0.227	-0.227	0.000	0.000	0.000	0.000
75	A	79	THR	0	0.033	0.011	40.051	0.252	0.252	0.000	0.000	0.000	0.000
76	A	80	ARG	1	0.803	0.877	41.057	7.161	7.161	0.000	0.000	0.000	0.000
77	A	81	THR	0	0.041	0.028	41.355	0.210	0.210	0.000	0.000	0.000	0.000
78	A	82	PRO	0	0.008	0.003	42.974	-0.167	-0.167	0.000	0.000	0.000	0.000
79	A	83	ASP	-1	-0.776	-0.876	40.958	-7.927	-7.927	0.000	0.000	0.000	0.000
80	A	84	PRO	0	-0.003	0.000	42.669	0.170	0.170	0.000	0.000	0.000	0.000
81	A	85	ALA	0	0.011	0.009	43.218	0.190	0.190	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.805	-0.872	43.996	-7.001	-7.001	0.000	0.000	0.000	0.000
83	A	87	ARG	1	0.928	0.948	45.834	6.416	6.416	0.000	0.000	0.000	0.000
84	A	88	ARG	1	0.837	0.892	45.001	7.072	7.072	0.000	0.000	0.000	0.000
85	A	89	ALA	0	-0.043	-0.006	41.692	-0.113	-0.113	0.000	0.000	0.000	0.000
86	A	90	TYR	0	-0.015	-0.027	40.665	0.163	0.163	0.000	0.000	0.000	0.000
87	A	91	PHE	0	-0.035	-0.015	36.100	-0.217	-0.217	0.000	0.000	0.000	0.000
88	A	92	LEU	0	-0.032	-0.016	36.824	0.252	0.252	0.000	0.000	0.000	0.000
89	A	93	VAL	0	0.036	-0.002	36.958	-0.267	-0.267	0.000	0.000	0.000	0.000
90	A	94	ILE	0	-0.008	0.003	34.168	0.128	0.128	0.000	0.000	0.000	0.000
91	A	95	THR	0	-0.022	-0.023	37.836	0.075	0.075	0.000	0.000	0.000	0.000
92	A	96	ARG	1	0.830	0.842	36.628	8.014	8.014	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.905	0.967	39.262	7.295	7.295	0.000	0.000	0.000	0.000
94	A	98	GLY	0	0.015	-0.005	37.158	-0.120	-0.120	0.000	0.000	0.000	0.000
95	A	99	GLU	-1	-0.843	-0.916	34.813	-8.532	-8.532	0.000	0.000	0.000	0.000
96	A	100	GLU	-1	-0.851	-0.921	34.243	-7.905	-7.905	0.000	0.000	0.000	0.000
97	A	101	VAL	0	-0.061	-0.011	32.540	-0.122	-0.122	0.000	0.000	0.000	0.000
98	A	102	ILE	0	-0.042	-0.021	28.689	-0.295	-0.295	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.764	-0.844	29.972	-8.908	-8.908	0.000	0.000	0.000	0.000
100	A	104	LYS	1	0.944	0.973	31.473	7.921	7.921	0.000	0.000	0.000	0.000
101	A	105	VAL	0	-0.070	-0.031	26.650	-0.180	-0.180	0.000	0.000	0.000	0.000
102	A	106	ILE	0	-0.049	-0.026	26.519	-0.427	-0.427	0.000	0.000	0.000	0.000
103	A	107	GLU	-1	-0.840	-0.915	27.551	-8.855	-8.855	0.000	0.000	0.000	0.000
104	A	108	ARG	1	0.863	0.936	27.986	9.470	9.470	0.000	0.000	0.000	0.000
105	A	109	ARG	1	0.857	0.922	20.176	12.878	12.878	0.000	0.000	0.000	0.000
106	A	110	GLU	-1	-0.899	-0.952	24.599	-10.517	-10.517	0.000	0.000	0.000	0.000
107	A	111	ASN	0	0.023	0.012	26.608	0.121	0.121	0.000	0.000	0.000	0.000
108	A	112	PHE	0	-0.033	-0.014	20.166	-0.019	-0.019	0.000	0.000	0.000	0.000
109	A	113	ILE	0	0.007	-0.006	19.890	-0.196	-0.196	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.854	-0.888	23.287	-9.384	-9.384	0.000	0.000	0.000	0.000
111	A	115	LYS	1	0.839	0.898	26.294	9.423	9.423	0.000	0.000	0.000	0.000
112	A	116	ILE	0	0.020	0.016	19.586	-0.058	-0.058	0.000	0.000	0.000	0.000
113	A	117	THR	0	-0.069	-0.065	21.150	-0.056	-0.056	0.000	0.000	0.000	0.000
114	A	118	SER	0	-0.002	0.013	23.164	0.182	0.182	0.000	0.000	0.000	0.000
115	A	119	ASP	-1	-0.925	-0.954	23.623	-10.107	-10.107	0.000	0.000	0.000	0.000
116	A	120	LEU	0	-0.074	-0.032	18.071	-0.127	-0.127	0.000	0.000	0.000	0.000
117	A	121	GLY	0	0.063	0.048	22.043	0.009	0.009	0.000	0.000	0.000	0.000
118	A	122	LYS	1	1.002	0.986	23.524	8.900	8.900	0.000	0.000	0.000	0.000
119	A	123	GLU	-1	-0.858	-0.900	23.372	-11.045	-11.045	0.000	0.000	0.000	0.000
120	A	124	LYS	1	0.918	0.951	18.493	11.262	11.262	0.000	0.000	0.000	0.000
121	A	125	SER	0	0.011	-0.014	19.200	-0.760	-0.760	0.000	0.000	0.000	0.000
122	A	126	SER	0	-0.050	-0.032	20.204	-0.258	-0.258	0.000	0.000	0.000	0.000
123	A	127	LYS	1	0.907	0.937	18.104	11.348	11.348	0.000	0.000	0.000	0.000
124	A	128	ILE	0	-0.003	0.003	14.801	-0.708	-0.708	0.000	0.000	0.000	0.000
125	A	129	LEU	0	0.002	0.000	15.953	-0.769	-0.769	0.000	0.000	0.000	0.000
126	A	130	ASP	-1	-0.839	-0.910	18.369	-12.950	-12.950	0.000	0.000	0.000	0.000
127	A	131	TYR	0	0.015	0.004	12.798	-0.374	-0.374	0.000	0.000	0.000	0.000
128	A	132	LEU	0	-0.027	-0.015	12.741	-1.304	-1.304	0.000	0.000	0.000	0.000
129	A	133	LYS	1	0.832	0.909	14.775	12.346	12.346	0.000	0.000	0.000	0.000
130	A	134	GLU	-1	-0.912	-0.952	14.198	-17.417	-17.417	0.000	0.000	0.000	0.000
131	A	135	LEU	0	-0.031	-0.016	8.200	-1.113	-1.113	0.000	0.000	0.000	0.000
132	A	136	LYS	1	0.837	0.900	11.975	14.295	14.295	0.000	0.000	0.000	0.000
133	A	137	GLY	0	0.075	0.045	14.612	-0.280	-0.280	0.000	0.000	0.000	0.000
134	A	138	VAL	0	-0.060	-0.020	10.272	0.065	0.065	0.000	0.000	0.000	0.000
135	A	139	MET	0	-0.026	-0.017	9.142	-0.644	-0.644	0.000	0.000	0.000	0.000
136	A	140	GLU	-1	-0.767	-0.879	12.301	-16.072	-16.072	0.000	0.000	0.000	0.000
137	A	141	ARG	1	0.858	0.926	14.199	19.675	19.675	0.000	0.000	0.000	0.000
138	A	142	ASN	0	-0.062	-0.044	10.742	-1.159	-1.159	0.000	0.000	0.000	0.000
139	A	143	PHE	0	-0.002	0.007	12.826	-0.687	-0.687	0.000	0.000	0.000	0.000
140	A	144	SER	0	0.018	0.021	14.478	0.137	0.137	0.000	0.000	0.000	0.000
141	A	145	LYS	1	0.918	0.968	8.439	32.691	32.691	0.000	0.000	0.000	0.000
142	A	146	GLN	0	-0.012	-0.001	13.102	-0.729	-0.729	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LYS)