FMO DATABASE

FMODB ID: 39GKL

Calculation Name: 2AHD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2AHD

Chain ID: A

ChEMBL ID:

UniProt ID: Q58346

Base Structure: X-ray

Registration Date: 2023-06-26

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	165
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1800762.171999
FMO2-HF: Nuclear repulsion	1733921.703969
FMO2-HF: Total energy	-66840.46803
FMO2-MP2: Total energy	-67034.199661

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:MET)

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

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.
-42.664	-35.537	16.011	-9.923	-13.212	-0.106

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.136 / q_NPA : -0.076

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	ILE	0	0.021	0.021	3.867	1.408	2.561	-0.004	-0.517	-0.632	0.001
4	A	4	GLY	0	0.021	0.008	6.623	0.646	0.646	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.024	-0.011	10.070	-0.175	-0.175	0.000	0.000	0.000	0.000
6	A	6	MET	0	-0.014	-0.008	13.429	0.177	0.177	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.114	0.010	16.974	-0.081	-0.081	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.784	-0.857	20.469	-0.274	-0.274	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.035	0.008	21.135	0.023	0.023	0.000	0.000	0.000	0.000
10	A	10	HIS	0	-0.040	-0.037	24.005	0.019	0.019	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.740	-0.856	27.174	-0.120	-0.120	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.001	0.021	25.814	0.024	0.024	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.024	0.004	25.227	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.063	-0.034	24.602	0.014	0.014	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.016	0.000	23.075	0.049	0.049	0.000	0.000	0.000	0.000
16	A	16	ILE	0	0.065	0.030	20.437	0.003	0.003	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.803	0.893	19.596	0.002	0.002	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.909	0.948	19.263	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.010	-0.001	16.843	0.043	0.043	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.012	0.001	15.175	0.021	0.021	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.948	-0.979	14.697	0.244	0.244	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.012	-0.010	12.949	0.113	0.113	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.059	-0.046	10.792	0.091	0.091	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.002	0.006	10.554	0.016	0.016	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.942	-0.968	11.116	0.838	0.838	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.880	-0.907	7.471	1.178	1.178	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.091	-0.054	3.116	-3.335	-1.267	0.814	-1.172	-1.709	0.003
28	A	28	VAL	0	-0.001	0.009	4.964	-1.066	-0.983	-0.001	-0.011	-0.070	0.000
29	A	29	GLU	-1	-0.865	-0.920	2.747	-11.769	-9.185	0.521	-1.248	-1.856	-0.014
30	A	30	THR	0	-0.032	-0.016	5.347	0.357	0.413	-0.001	-0.002	-0.052	0.000
31	A	31	VAL	0	0.021	0.000	8.206	0.061	0.061	0.000	0.000	0.000	0.000
32	A	32	ILE	0	0.004	0.007	10.923	0.062	0.062	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.001	-0.015	13.636	0.084	0.084	0.000	0.000	0.000	0.000
34	A	34	CYS	0	-0.017	0.001	17.176	0.013	0.013	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.041	-0.024	19.693	0.037	0.037	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.860	-0.910	22.714	-0.263	-0.263	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.054	0.032	19.782	0.023	0.023	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.057	-0.026	24.777	0.027	0.027	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.054	-0.058	28.622	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.014	-0.013	27.637	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.013	-0.008	27.130	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.025	0.017	22.901	0.013	0.013	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.022	-0.012	22.079	0.000	0.000	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.804	0.885	22.400	0.106	0.106	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.818	-0.888	22.054	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	46	PHE	0	0.014	-0.015	16.485	0.022	0.022	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.851	-0.896	17.763	-0.087	-0.087	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.083	-0.048	18.431	0.024	0.024	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.015	0.000	12.237	0.061	0.061	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.020	-0.013	10.394	-0.141	-0.141	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.008	0.031	9.266	-0.050	-0.050	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.051	-0.022	9.950	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.021	-0.006	11.509	-0.081	-0.081	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.008	0.011	11.148	0.046	0.046	0.000	0.000	0.000	0.000
55	A	55	ALA	0	0.003	-0.009	15.072	0.021	0.021	0.000	0.000	0.000	0.000
56	A	56	THR	0	-0.042	-0.030	18.298	-0.033	-0.033	0.000	0.000	0.000	0.000
57	A	57	TYR	0	-0.065	-0.021	21.549	0.021	0.021	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.032	0.007	25.098	-0.015	-0.015	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.028	-0.031	26.899	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.094	-0.067	29.723	0.034	0.034	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.739	-0.841	25.565	-0.275	-0.275	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.017	-0.020	29.101	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.858	-0.943	30.645	-0.174	-0.174	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.822	0.863	28.292	0.289	0.289	0.000	0.000	0.000	0.000
65	A	65	CYS	0	-0.100	-0.035	28.026	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.853	0.909	28.458	0.148	0.148	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.014	0.009	24.913	0.002	0.002	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.832	0.921	23.656	0.377	0.377	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.826	-0.902	24.324	-0.185	-0.185	0.000	0.000	0.000	0.000
70	A	70	TRP	0	0.027	0.000	25.112	0.005	0.005	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.016	0.008	18.954	0.010	0.010	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.785	0.892	18.955	0.488	0.488	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.933	-0.966	21.868	-0.158	-0.158	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.107	-0.035	18.047	0.028	0.028	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.001	-0.023	14.228	0.032	0.032	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.926	-0.951	17.888	-0.334	-0.334	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.837	-0.894	11.892	-0.829	-0.829	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.029	-0.004	15.563	-0.136	-0.136	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.054	-0.022	15.019	0.080	0.080	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.022	0.014	18.339	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.870	-0.945	21.010	-0.386	-0.386	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.789	-0.848	22.423	-0.374	-0.374	0.000	0.000	0.000	0.000
83	A	83	PHE	0	-0.018	-0.005	21.897	0.018	0.018	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.004	0.019	15.725	0.011	0.011	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.069	-0.033	16.249	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.004	-0.001	11.595	0.073	0.073	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.847	-0.924	9.031	-1.287	-1.287	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.004	0.002	4.309	0.078	0.197	-0.001	-0.009	-0.108	0.000
89	A	89	ASP	-1	-0.807	-0.893	2.393	-16.760	-14.455	3.612	-2.596	-3.322	-0.034
90	A	90	ASP	-1	-0.957	-0.972	4.884	-0.714	-0.645	-0.001	-0.007	-0.061	0.000
91	A	91	LEU	0	-0.025	0.022	7.888	0.547	0.547	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.761	0.844	9.960	1.052	1.052	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.007	0.001	8.584	0.181	0.181	0.000	0.000	0.000	0.000
94	A	94	PHE	0	-0.025	-0.018	13.864	0.134	0.134	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.029	0.016	13.575	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.005	-0.029	18.011	0.065	0.065	0.000	0.000	0.000	0.000
97	A	97	HIS	1	0.819	0.939	21.472	0.334	0.334	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.012	-0.018	23.875	0.014	0.014	0.000	0.000	0.000	0.000
99	A	99	HIS	0	-0.010	0.007	25.702	0.029	0.029	0.000	0.000	0.000	0.000
100	A	100	HIS	0	0.009	0.014	28.449	0.011	0.011	0.000	0.000	0.000	0.000
101	A	101	GLN	0	0.068	0.027	28.369	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.028	-0.024	28.670	-0.019	-0.019	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.010	0.004	25.314	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.048	0.039	22.258	-0.029	-0.029	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.854	-0.906	24.617	-0.325	-0.325	0.000	0.000	0.000	0.000
106	A	106	MET	0	-0.045	-0.025	26.203	0.013	0.013	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.008	0.004	21.645	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	108	ILE	0	0.057	0.039	21.253	-0.029	-0.029	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.816	0.885	22.593	0.331	0.331	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.084	-0.045	22.494	0.018	0.018	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.024	0.013	21.528	0.020	0.020	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.103	-0.050	19.935	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	113	TYR	0	-0.045	-0.034	16.004	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.768	-0.866	12.820	-1.056	-1.056	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.016	-0.009	11.184	0.046	0.046	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.035	-0.020	14.548	0.009	0.009	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.010	0.003	12.494	0.046	0.046	0.000	0.000	0.000	0.000
118	A	118	TYR	0	-0.018	-0.019	17.163	0.052	0.052	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.112	0.044	20.546	0.008	0.008	0.000	0.000	0.000	0.000
120	A	120	HIS	0	-0.114	-0.064	22.976	0.008	0.008	0.000	0.000	0.000	0.000
121	A	121	THR	0	-0.027	-0.031	25.760	0.021	0.021	0.000	0.000	0.000	0.000
122	A	122	HIS	1	0.742	0.878	25.914	0.241	0.241	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.894	-0.959	25.687	-0.179	-0.179	0.000	0.000	0.000	0.000
124	A	124	ARG	1	0.879	0.947	21.239	0.161	0.161	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.031	-0.019	21.425	0.031	0.031	0.000	0.000	0.000	0.000
126	A	126	PHE	0	0.002	-0.008	15.656	-0.050	-0.050	0.000	0.000	0.000	0.000
127	A	127	GLU	-1	-0.957	-0.969	19.613	-0.301	-0.301	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.844	-0.919	17.006	-0.711	-0.711	0.000	0.000	0.000	0.000
129	A	129	VAL	0	-0.053	-0.020	20.457	0.063	0.063	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.942	-0.980	22.143	-0.372	-0.372	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.963	-0.982	18.929	-0.453	-0.453	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.050	0.002	17.737	-0.090	-0.090	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.017	-0.004	13.830	0.064	0.064	0.000	0.000	0.000	0.000
134	A	134	VAL	0	-0.012	-0.014	16.620	-0.074	-0.074	0.000	0.000	0.000	0.000
135	A	135	ILE	0	-0.004	-0.007	13.389	0.041	0.041	0.000	0.000	0.000	0.000
136	A	136	ASN	0	0.000	-0.004	17.811	0.000	0.000	0.000	0.000	0.000	0.000
137	A	137	PRO	0	0.012	0.021	16.596	0.042	0.042	0.000	0.000	0.000	0.000
138	A	138	GLY	0	0.053	0.045	18.567	0.065	0.065	0.000	0.000	0.000	0.000
139	A	139	GLU	-1	-0.776	-0.850	21.693	-0.173	-0.173	0.000	0.000	0.000	0.000
140	A	140	CYS	0	0.021	0.037	20.348	0.037	0.037	0.000	0.000	0.000	0.000
141	A	141	CYS	0	-0.082	-0.037	22.327	0.038	0.038	0.000	0.000	0.000	0.000
142	A	142	GLY	0	0.015	-0.006	25.757	0.021	0.021	0.000	0.000	0.000	0.000
143	A	143	TYR	0	-0.079	-0.051	27.217	0.016	0.016	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.059	-0.038	29.966	0.010	0.010	0.000	0.000	0.000	0.000
145	A	145	THR	0	-0.013	-0.020	27.765	0.006	0.006	0.000	0.000	0.000	0.000
146	A	146	GLY	0	-0.042	-0.013	30.128	0.009	0.009	0.000	0.000	0.000	0.000
147	A	147	ILE	0	-0.091	-0.048	24.176	0.018	0.018	0.000	0.000	0.000	0.000
148	A	148	PRO	0	0.007	0.014	23.700	-0.019	-0.019	0.000	0.000	0.000	0.000
149	A	149	THR	0	-0.071	-0.063	19.664	0.040	0.040	0.000	0.000	0.000	0.000
150	A	150	ILE	0	-0.008	0.004	15.168	-0.020	-0.020	0.000	0.000	0.000	0.000
151	A	151	GLY	0	0.025	0.006	14.077	0.054	0.054	0.000	0.000	0.000	0.000
152	A	152	ILE	0	-0.048	-0.015	7.642	0.004	0.004	0.000	0.000	0.000	0.000
153	A	153	LEU	0	-0.002	-0.004	8.370	0.262	0.262	0.000	0.000	0.000	0.000
154	A	154	ASP	-1	-0.866	-0.947	5.506	-1.815	-1.815	0.000	0.000	0.000	0.000
155	A	155	THR	0	-0.023	-0.038	2.968	0.930	1.367	0.021	-0.122	-0.337	0.000
156	A	156	GLU	-1	-0.778	-0.892	1.903	-11.938	-13.790	11.052	-4.234	-4.966	-0.062
157	A	157	LYS	1	0.724	0.845	5.148	0.860	0.965	-0.001	-0.005	-0.099	0.000
158	A	158	LYS	1	0.877	0.942	8.526	1.141	1.141	0.000	0.000	0.000	0.000
159	A	159	GLU	-1	-0.847	-0.901	9.569	-0.025	-0.025	0.000	0.000	0.000	0.000
160	A	160	TYR	0	0.035	0.014	9.872	-0.088	-0.088	0.000	0.000	0.000	0.000
161	A	161	ARG	1	0.793	0.869	9.372	-0.153	-0.153	0.000	0.000	0.000	0.000
162	A	162	GLU	-1	-0.831	-0.899	13.490	-0.248	-0.248	0.000	0.000	0.000	0.000
163	A	163	ILE	0	-0.046	-0.029	12.227	0.079	0.079	0.000	0.000	0.000	0.000
164	A	164	VAL	0	-0.002	0.001	16.815	-0.033	-0.033	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.055	-0.021	18.727	0.050	0.050	0.000	0.000	0.000	0.000

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