FMO DATABASE

FMODB ID: 49RNN

Calculation Name: 3EXZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EXZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q2RSA1

Base Structure: X-ray

Registration Date: 2023-06-21

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	146
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1217729.009646
FMO2-HF: Nuclear repulsion	1163174.769294
FMO2-HF: Total energy	-54554.240352
FMO2-MP2: Total energy	-54716.196248

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:15:GLY)

Summations of interaction energy for fragment #1(A:15:GLY)

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.
-2.775	0.896	1.915	-2.346	-3.239	-0.014

Interaction energy analysis for fragmet #1(A:15:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : 0.015

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	17	PHE	0	0.001	-0.013	3.783	0.547	2.222	-0.019	-0.851	-0.804	0.004
4	A	18	LEU	0	-0.021	-0.024	6.722	0.104	0.104	0.000	0.000	0.000	0.000
5	A	19	GLU	-1	-0.811	-0.908	10.275	-1.072	-1.072	0.000	0.000	0.000	0.000
6	A	20	ASP	-1	-0.809	-0.861	6.224	-3.571	-3.571	0.000	0.000	0.000	0.000
7	A	21	LEU	0	-0.025	0.010	8.080	0.114	0.114	0.000	0.000	0.000	0.000
8	A	22	ALA	0	0.000	-0.013	10.868	0.153	0.153	0.000	0.000	0.000	0.000
9	A	23	VAL	0	-0.045	-0.025	14.267	0.015	0.015	0.000	0.000	0.000	0.000
10	A	24	GLY	0	-0.011	-0.007	16.741	0.016	0.016	0.000	0.000	0.000	0.000
11	A	25	ASP	-1	-0.852	-0.919	11.354	-0.986	-0.986	0.000	0.000	0.000	0.000
12	A	26	ARG	1	0.895	0.940	13.098	0.372	0.372	0.000	0.000	0.000	0.000
13	A	27	PHE	0	-0.021	-0.016	7.285	-0.114	-0.114	0.000	0.000	0.000	0.000
14	A	28	ASP	-1	-0.800	-0.905	10.766	0.055	0.055	0.000	0.000	0.000	0.000
15	A	29	SER	0	0.008	0.019	11.059	0.040	0.040	0.000	0.000	0.000	0.000
16	A	30	ALA	0	-0.012	0.000	12.633	-0.032	-0.032	0.000	0.000	0.000	0.000
17	A	31	ARG	1	0.867	0.921	14.549	-0.128	-0.128	0.000	0.000	0.000	0.000
18	A	32	HIS	0	-0.018	-0.009	18.212	0.072	0.072	0.000	0.000	0.000	0.000
19	A	33	ARG	1	0.845	0.933	20.419	-0.143	-0.143	0.000	0.000	0.000	0.000
20	A	34	VAL	0	-0.029	-0.009	24.211	0.012	0.012	0.000	0.000	0.000	0.000
21	A	35	GLU	-1	-0.816	-0.904	26.372	0.102	0.102	0.000	0.000	0.000	0.000
22	A	36	ALA	0	0.041	0.010	29.609	0.000	0.000	0.000	0.000	0.000	0.000
23	A	37	ALA	0	0.013	0.000	32.271	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	38	ALA	0	0.006	0.006	27.301	0.002	0.002	0.000	0.000	0.000	0.000
25	A	39	ILE	0	-0.007	0.005	29.212	0.001	0.001	0.000	0.000	0.000	0.000
26	A	40	LYS	1	0.836	0.903	30.603	-0.071	-0.071	0.000	0.000	0.000	0.000
27	A	41	ALA	0	-0.033	0.000	30.175	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	42	PHE	0	0.035	0.014	24.959	0.000	0.000	0.000	0.000	0.000	0.000
29	A	43	ALA	0	0.011	0.002	29.388	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	44	GLY	0	-0.016	-0.018	32.274	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	45	GLU	-1	-0.989	-0.983	29.304	0.120	0.120	0.000	0.000	0.000	0.000
32	A	46	PHE	0	-0.065	-0.039	27.340	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	47	ASP	-1	-0.835	-0.877	31.139	0.034	0.034	0.000	0.000	0.000	0.000
34	A	48	PRO	0	0.026	0.013	33.076	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	49	GLN	0	-0.040	-0.032	35.129	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	50	PRO	0	0.068	0.009	37.736	0.003	0.003	0.000	0.000	0.000	0.000
37	A	51	PHE	0	0.002	-0.001	36.126	0.002	0.002	0.000	0.000	0.000	0.000
38	A	52	HIS	0	-0.050	-0.029	33.367	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	53	LEU	0	-0.023	-0.011	34.887	0.007	0.007	0.000	0.000	0.000	0.000
40	A	54	ASP	-1	-0.844	-0.940	37.547	0.049	0.049	0.000	0.000	0.000	0.000
41	A	55	GLU	-1	-0.825	-0.891	39.228	0.058	0.058	0.000	0.000	0.000	0.000
42	A	56	GLU	-1	-0.878	-0.909	40.612	0.030	0.030	0.000	0.000	0.000	0.000
43	A	57	ALA	0	0.019	-0.010	42.555	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	58	ALA	0	-0.019	0.001	38.775	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	59	ARG	1	0.851	0.940	40.837	-0.041	-0.041	0.000	0.000	0.000	0.000
46	A	60	HIS	0	-0.068	-0.029	43.004	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	61	SER	0	-0.037	-0.026	40.368	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	62	LEU	0	0.025	-0.004	39.666	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	63	PHE	0	0.002	0.003	33.631	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	64	GLY	0	0.008	0.032	38.084	0.001	0.001	0.000	0.000	0.000	0.000
51	A	65	GLY	0	-0.026	-0.024	38.714	0.001	0.001	0.000	0.000	0.000	0.000
52	A	66	LEU	0	-0.027	-0.027	34.428	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	67	ALA	0	0.000	0.014	32.817	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	68	ALA	0	0.010	0.010	28.432	0.003	0.003	0.000	0.000	0.000	0.000
55	A	69	SER	0	-0.023	-0.031	29.402	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	70	GLY	0	0.067	0.018	27.764	0.006	0.006	0.000	0.000	0.000	0.000
57	A	71	TRP	0	0.019	-0.011	25.390	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	72	HIS	0	0.017	0.021	24.564	0.002	0.002	0.000	0.000	0.000	0.000
59	A	73	THR	0	-0.017	-0.007	23.208	0.018	0.018	0.000	0.000	0.000	0.000
60	A	74	ALA	0	0.024	0.021	21.479	0.006	0.006	0.000	0.000	0.000	0.000
61	A	75	ALA	0	-0.016	-0.005	19.774	0.009	0.009	0.000	0.000	0.000	0.000
62	A	76	ILE	0	-0.012	-0.010	18.831	0.037	0.037	0.000	0.000	0.000	0.000
63	A	77	THR	0	-0.001	0.002	17.153	0.030	0.030	0.000	0.000	0.000	0.000
64	A	78	MET	0	0.013	0.011	13.165	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	79	ARG	1	0.961	0.985	13.903	-0.313	-0.313	0.000	0.000	0.000	0.000
66	A	80	LEU	0	-0.009	0.017	13.459	0.112	0.112	0.000	0.000	0.000	0.000
67	A	81	LEU	0	0.014	0.017	11.552	0.064	0.064	0.000	0.000	0.000	0.000
68	A	82	VAL	0	-0.029	-0.015	9.571	0.035	0.035	0.000	0.000	0.000	0.000
69	A	83	THR	0	-0.087	-0.061	8.609	0.252	0.252	0.000	0.000	0.000	0.000
70	A	84	SER	0	-0.024	-0.021	8.373	0.204	0.204	0.000	0.000	0.000	0.000
71	A	85	GLY	0	-0.006	-0.005	8.313	-0.092	-0.092	0.000	0.000	0.000	0.000
72	A	86	LEU	0	-0.001	-0.003	8.111	-0.213	-0.213	0.000	0.000	0.000	0.000
73	A	87	PRO	0	0.000	0.005	3.255	-0.212	0.134	0.026	-0.098	-0.274	-0.001
74	A	88	LEU	0	-0.004	0.004	2.899	-4.138	-2.451	0.473	-1.268	-0.892	-0.012
75	A	89	ALA	0	0.005	0.002	2.622	1.037	1.336	1.313	-0.496	-1.116	-0.005
76	A	90	GLN	0	-0.055	-0.036	3.158	0.817	0.481	0.122	0.367	-0.153	0.000
77	A	91	GLY	0	0.011	0.025	6.057	0.052	0.052	0.000	0.000	0.000	0.000
78	A	92	ILE	0	-0.013	-0.010	8.031	-0.265	-0.265	0.000	0.000	0.000	0.000
79	A	93	ILE	0	0.020	0.008	10.533	0.074	0.074	0.000	0.000	0.000	0.000
80	A	94	GLY	0	0.011	0.002	13.717	-0.066	-0.066	0.000	0.000	0.000	0.000
81	A	95	ALA	0	-0.035	-0.011	16.568	0.023	0.023	0.000	0.000	0.000	0.000
82	A	96	GLY	0	0.018	-0.008	19.639	0.024	0.024	0.000	0.000	0.000	0.000
83	A	97	THR	0	-0.061	-0.046	20.025	-0.034	-0.034	0.000	0.000	0.000	0.000
84	A	98	GLU	-1	-0.850	-0.884	21.888	-0.089	-0.089	0.000	0.000	0.000	0.000
85	A	99	LEU	0	-0.034	-0.016	22.487	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	100	SER	0	0.026	0.013	25.119	0.004	0.004	0.000	0.000	0.000	0.000
87	A	101	TRP	0	-0.014	-0.015	25.211	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	102	PRO	0	-0.056	-0.017	27.091	0.003	0.003	0.000	0.000	0.000	0.000
89	A	103	ASN	0	-0.019	-0.004	28.827	0.003	0.003	0.000	0.000	0.000	0.000
90	A	104	PRO	0	0.008	-0.008	29.202	0.003	0.003	0.000	0.000	0.000	0.000
91	A	105	THR	0	0.036	0.017	26.167	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	106	ARG	1	0.814	0.892	28.847	-0.030	-0.030	0.000	0.000	0.000	0.000
93	A	107	PRO	0	-0.005	-0.011	29.473	0.008	0.008	0.000	0.000	0.000	0.000
94	A	108	GLY	0	-0.013	-0.013	29.801	-0.007	-0.007	0.000	0.000	0.000	0.000
95	A	109	ASP	-1	-0.855	-0.927	26.398	0.054	0.054	0.000	0.000	0.000	0.000
96	A	110	GLU	-1	-0.911	-0.964	23.164	0.158	0.158	0.000	0.000	0.000	0.000
97	A	111	LEU	0	-0.021	-0.015	21.095	-0.017	-0.017	0.000	0.000	0.000	0.000
98	A	112	HIS	0	-0.075	-0.050	16.909	0.066	0.066	0.000	0.000	0.000	0.000
99	A	113	VAL	0	-0.039	-0.032	14.737	-0.027	-0.027	0.000	0.000	0.000	0.000
100	A	114	GLU	-1	-0.805	-0.875	14.742	-0.092	-0.092	0.000	0.000	0.000	0.000
101	A	115	THR	0	-0.045	-0.025	12.338	0.008	0.008	0.000	0.000	0.000	0.000
102	A	116	THR	0	0.017	0.011	13.743	-0.061	-0.061	0.000	0.000	0.000	0.000
103	A	117	VAL	0	-0.014	0.012	12.123	0.045	0.045	0.000	0.000	0.000	0.000
104	A	118	LEU	0	0.007	-0.004	15.138	0.020	0.020	0.000	0.000	0.000	0.000
105	A	119	ALA	0	-0.009	-0.015	17.827	0.026	0.026	0.000	0.000	0.000	0.000
106	A	120	ILE	0	0.036	0.036	14.284	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	121	THR	0	-0.045	-0.023	17.421	0.039	0.039	0.000	0.000	0.000	0.000
108	A	122	PRO	0	0.056	0.021	18.278	0.016	0.016	0.000	0.000	0.000	0.000
109	A	123	SER	0	0.025	0.028	19.123	0.053	0.053	0.000	0.000	0.000	0.000
110	A	124	LYS	1	0.849	0.907	21.062	0.276	0.276	0.000	0.000	0.000	0.000
111	A	125	SER	0	0.031	0.019	24.381	0.002	0.002	0.000	0.000	0.000	0.000
112	A	126	ARG	1	0.833	0.890	19.414	0.233	0.233	0.000	0.000	0.000	0.000
113	A	127	PRO	0	0.062	0.018	19.428	-0.027	-0.027	0.000	0.000	0.000	0.000
114	A	128	ASP	-1	-0.795	-0.854	15.989	-0.338	-0.338	0.000	0.000	0.000	0.000
115	A	129	ARG	1	0.900	0.951	14.465	0.207	0.207	0.000	0.000	0.000	0.000
116	A	130	ALA	0	-0.010	-0.006	14.610	0.055	0.055	0.000	0.000	0.000	0.000
117	A	131	ILE	0	-0.013	0.008	15.034	-0.016	-0.016	0.000	0.000	0.000	0.000
118	A	132	VAL	0	0.018	0.000	12.335	0.011	0.011	0.000	0.000	0.000	0.000
119	A	133	THR	0	-0.034	-0.014	15.271	0.061	0.061	0.000	0.000	0.000	0.000
120	A	134	CYS	0	-0.011	0.000	13.323	-0.074	-0.074	0.000	0.000	0.000	0.000
121	A	135	GLN	0	0.002	-0.017	15.842	0.047	0.047	0.000	0.000	0.000	0.000
122	A	136	SER	0	-0.008	-0.018	14.751	-0.023	-0.023	0.000	0.000	0.000	0.000
123	A	137	ASP	-1	-0.738	-0.825	17.296	-0.091	-0.091	0.000	0.000	0.000	0.000
124	A	138	THR	0	-0.033	-0.026	18.960	0.004	0.004	0.000	0.000	0.000	0.000
125	A	139	LEU	0	0.016	0.014	20.477	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	140	ASN	0	0.047	0.012	22.190	0.014	0.014	0.000	0.000	0.000	0.000
127	A	141	GLN	0	0.053	0.018	24.718	-0.012	-0.012	0.000	0.000	0.000	0.000
128	A	142	ARG	1	0.750	0.846	26.004	-0.022	-0.022	0.000	0.000	0.000	0.000
129	A	143	GLY	0	-0.003	0.009	25.094	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	144	GLU	-1	-0.820	-0.852	26.172	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	145	VAL	0	0.034	0.009	23.581	0.007	0.007	0.000	0.000	0.000	0.000
132	A	146	VAL	0	0.008	0.005	23.999	0.000	0.000	0.000	0.000	0.000	0.000
133	A	147	GLN	0	-0.001	-0.021	20.653	0.015	0.015	0.000	0.000	0.000	0.000
134	A	148	ARG	1	0.832	0.906	21.891	0.117	0.117	0.000	0.000	0.000	0.000
135	A	149	SER	0	0.018	0.007	18.877	0.017	0.017	0.000	0.000	0.000	0.000
136	A	150	THR	0	-0.055	-0.026	19.234	-0.035	-0.035	0.000	0.000	0.000	0.000
137	A	151	ALA	0	0.013	0.008	16.644	0.016	0.016	0.000	0.000	0.000	0.000
138	A	152	LYS	1	0.890	0.946	17.522	0.191	0.191	0.000	0.000	0.000	0.000
139	A	153	VAL	0	0.028	0.010	11.281	0.046	0.046	0.000	0.000	0.000	0.000
140	A	154	VAL	0	-0.043	-0.017	14.060	-0.052	-0.052	0.000	0.000	0.000	0.000
141	A	155	VAL	0	0.023	0.012	8.733	0.003	0.003	0.000	0.000	0.000	0.000
142	A	156	PHE	0	0.020	-0.006	10.542	0.078	0.078	0.000	0.000	0.000	0.000
143	A	157	ARG	1	0.865	0.917	9.795	0.464	0.464	0.000	0.000	0.000	0.000
144	A	158	ARG	1	0.808	0.878	6.018	2.663	2.663	0.000	0.000	0.000	0.000
145	A	159	PRO	0	-0.029	-0.019	9.326	0.120	0.120	0.000	0.000	0.000	0.000
146	A	160	LEU	0	0.008	0.017	11.932	-0.031	-0.031	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:15:GLY)