FMO DATABASE

FMODB ID: K3Y33

Calculation Name: 4FFE-X-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4FFE

Chain ID: X

ChEMBL ID:

UniProt ID: Q8QN43

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1569640.189275
FMO2-HF: Nuclear repulsion	1506463.335774
FMO2-HF: Total energy	-63176.853502
FMO2-MP2: Total energy	-63360.394286

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(X:0:GLY)

Summations of interaction energy for fragment #1(X:0: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.
-6.369	-3.745	4.228	-3.657	-3.196	-0.021

Interaction energy analysis for fragmet #1(X:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.014 / q_NPA : -0.020

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	X	2	LYS	1	0.869	0.911	3.792	2.161	3.432	-0.020	-0.615	-0.637	0.000
4	X	3	LEU	0	-0.034	-0.016	6.964	0.233	0.233	0.000	0.000	0.000	0.000
5	X	4	ALA	0	0.003	0.013	10.636	0.091	0.091	0.000	0.000	0.000	0.000
6	X	5	PHE	0	-0.026	-0.029	13.112	0.056	0.056	0.000	0.000	0.000	0.000
7	X	6	ASN	0	0.028	0.012	16.878	0.012	0.012	0.000	0.000	0.000	0.000
8	X	7	PHE	0	-0.021	-0.019	19.425	0.028	0.028	0.000	0.000	0.000	0.000
9	X	8	ASN	0	0.037	0.021	22.782	0.005	0.005	0.000	0.000	0.000	0.000
10	X	9	LEU	0	-0.047	-0.023	25.870	0.013	0.013	0.000	0.000	0.000	0.000
11	X	10	GLU	-1	-0.799	-0.867	29.428	-0.152	-0.152	0.000	0.000	0.000	0.000
12	X	11	ILE	0	-0.064	-0.050	32.239	0.009	0.009	0.000	0.000	0.000	0.000
13	X	12	ASN	0	0.005	0.007	35.524	0.002	0.002	0.000	0.000	0.000	0.000
14	X	13	GLY	0	0.034	0.016	38.609	0.005	0.005	0.000	0.000	0.000	0.000
15	X	14	SER	0	-0.037	-0.020	40.895	0.000	0.000	0.000	0.000	0.000	0.000
16	X	15	ASP	-1	-0.884	-0.934	39.251	-0.079	-0.079	0.000	0.000	0.000	0.000
17	X	16	THR	0	-0.049	-0.042	34.088	-0.001	-0.001	0.000	0.000	0.000	0.000
18	X	17	HIS	0	-0.028	0.006	30.539	0.011	0.011	0.000	0.000	0.000	0.000
19	X	18	SER	0	0.000	-0.002	28.670	-0.003	-0.003	0.000	0.000	0.000	0.000
20	X	19	THR	0	0.012	-0.002	25.699	-0.002	-0.002	0.000	0.000	0.000	0.000
21	X	20	VAL	0	-0.024	-0.012	20.592	-0.006	-0.006	0.000	0.000	0.000	0.000
22	X	21	ASP	-1	-0.841	-0.889	19.554	-0.283	-0.283	0.000	0.000	0.000	0.000
23	X	22	VAL	0	-0.010	-0.018	15.150	-0.028	-0.028	0.000	0.000	0.000	0.000
24	X	23	TYR	0	0.008	-0.008	13.315	0.030	0.030	0.000	0.000	0.000	0.000
25	X	24	LEU	0	-0.018	-0.016	9.450	-0.023	-0.023	0.000	0.000	0.000	0.000
26	X	25	ASP	-1	-0.790	-0.888	6.332	-2.551	-2.551	0.000	0.000	0.000	0.000
27	X	26	ASP	-1	-0.901	-0.943	8.464	-1.336	-1.336	0.000	0.000	0.000	0.000
28	X	27	SER	0	-0.048	-0.015	11.498	0.234	0.234	0.000	0.000	0.000	0.000
29	X	28	GLN	0	-0.037	-0.017	13.645	-0.008	-0.008	0.000	0.000	0.000	0.000
30	X	29	ILE	0	-0.049	-0.030	14.395	0.058	0.058	0.000	0.000	0.000	0.000
31	X	30	ILE	0	-0.009	-0.011	17.422	0.061	0.061	0.000	0.000	0.000	0.000
32	X	31	THR	0	-0.006	0.009	20.096	-0.018	-0.018	0.000	0.000	0.000	0.000
33	X	32	PHE	0	-0.008	-0.016	22.936	0.024	0.024	0.000	0.000	0.000	0.000
34	X	33	ASP	-1	-0.726	-0.840	25.613	-0.138	-0.138	0.000	0.000	0.000	0.000
35	X	34	GLY	0	0.075	0.041	28.809	0.008	0.008	0.000	0.000	0.000	0.000
36	X	35	LYS	1	0.819	0.914	30.673	0.095	0.095	0.000	0.000	0.000	0.000
37	X	36	ASP	-1	-0.906	-0.971	30.385	-0.086	-0.086	0.000	0.000	0.000	0.000
38	X	37	ILE	0	-0.040	-0.008	22.935	-0.010	-0.010	0.000	0.000	0.000	0.000
39	X	38	ARG	1	0.816	0.883	25.058	0.154	0.154	0.000	0.000	0.000	0.000
40	X	39	PRO	0	0.005	0.020	21.877	-0.021	-0.021	0.000	0.000	0.000	0.000
41	X	40	THR	0	-0.012	-0.023	19.508	0.017	0.017	0.000	0.000	0.000	0.000
42	X	41	ILE	0	0.014	0.009	15.484	-0.009	-0.009	0.000	0.000	0.000	0.000
43	X	42	PRO	0	0.027	-0.002	19.490	0.016	0.016	0.000	0.000	0.000	0.000
44	X	43	PHE	0	0.017	0.004	14.281	0.036	0.036	0.000	0.000	0.000	0.000
45	X	44	MET	0	0.007	0.018	17.794	0.023	0.023	0.000	0.000	0.000	0.000
46	X	45	ILE	0	-0.034	-0.018	20.471	0.007	0.007	0.000	0.000	0.000	0.000
47	X	46	GLY	0	-0.010	-0.005	24.162	0.013	0.013	0.000	0.000	0.000	0.000
48	X	47	ASP	-1	-0.834	-0.904	21.125	-0.073	-0.073	0.000	0.000	0.000	0.000
49	X	48	GLU	-1	-0.911	-0.955	23.732	-0.034	-0.034	0.000	0.000	0.000	0.000
50	X	49	ILE	0	-0.049	-0.024	21.121	0.006	0.006	0.000	0.000	0.000	0.000
51	X	50	PHE	0	-0.014	-0.027	16.484	-0.007	-0.007	0.000	0.000	0.000	0.000
52	X	51	LEU	0	0.000	0.009	21.018	-0.013	-0.013	0.000	0.000	0.000	0.000
53	X	52	PRO	0	0.029	0.012	23.591	-0.007	-0.007	0.000	0.000	0.000	0.000
54	X	53	PHE	0	0.013	0.018	20.630	0.000	0.000	0.000	0.000	0.000	0.000
55	X	54	TYR	0	0.050	0.005	16.059	0.001	0.001	0.000	0.000	0.000	0.000
56	X	55	LYS	1	0.905	0.980	22.913	0.095	0.095	0.000	0.000	0.000	0.000
57	X	56	ASN	0	-0.012	0.014	26.443	0.007	0.007	0.000	0.000	0.000	0.000
58	X	57	VAL	0	0.036	0.019	22.141	0.001	0.001	0.000	0.000	0.000	0.000
59	X	58	PHE	0	0.006	-0.014	20.146	-0.003	-0.003	0.000	0.000	0.000	0.000
60	X	59	SER	0	0.002	-0.014	25.739	0.002	0.002	0.000	0.000	0.000	0.000
61	X	60	GLU	-1	-0.885	-0.933	28.057	-0.072	-0.072	0.000	0.000	0.000	0.000
62	X	61	PHE	0	-0.035	-0.011	24.599	0.004	0.004	0.000	0.000	0.000	0.000
63	X	62	PHE	0	0.044	0.017	25.638	0.003	0.003	0.000	0.000	0.000	0.000
64	X	63	SER	0	-0.039	-0.017	30.052	0.008	0.008	0.000	0.000	0.000	0.000
65	X	64	LEU	0	-0.042	-0.029	31.687	0.009	0.009	0.000	0.000	0.000	0.000
66	X	65	PHE	0	-0.030	0.000	30.895	0.002	0.002	0.000	0.000	0.000	0.000
67	X	66	ARG	1	0.841	0.923	32.790	0.081	0.081	0.000	0.000	0.000	0.000
68	X	67	ARG	1	0.904	0.960	35.407	0.090	0.090	0.000	0.000	0.000	0.000
69	X	68	VAL	0	-0.015	-0.011	37.092	0.006	0.006	0.000	0.000	0.000	0.000
70	X	69	PRO	0	-0.016	-0.016	39.496	-0.004	-0.004	0.000	0.000	0.000	0.000
71	X	70	THR	0	-0.013	-0.016	38.585	0.000	0.000	0.000	0.000	0.000	0.000
72	X	71	SER	0	-0.009	-0.001	40.554	0.002	0.002	0.000	0.000	0.000	0.000
73	X	72	THR	0	0.003	0.007	38.665	0.002	0.002	0.000	0.000	0.000	0.000
74	X	73	PRO	0	-0.006	-0.003	40.550	0.000	0.000	0.000	0.000	0.000	0.000
75	X	74	TYR	0	-0.073	-0.065	32.418	0.000	0.000	0.000	0.000	0.000	0.000
76	X	75	GLU	-1	-0.835	-0.876	34.067	-0.109	-0.109	0.000	0.000	0.000	0.000
77	X	76	ASP	-1	-0.886	-0.938	28.546	-0.188	-0.188	0.000	0.000	0.000	0.000
78	X	77	LEU	0	-0.035	-0.017	28.648	-0.001	-0.001	0.000	0.000	0.000	0.000
79	X	78	THR	0	0.091	0.038	22.095	-0.002	-0.002	0.000	0.000	0.000	0.000
80	X	79	TYR	0	-0.108	-0.066	20.401	0.010	0.010	0.000	0.000	0.000	0.000
81	X	80	PHE	0	0.047	0.035	13.166	0.008	0.008	0.000	0.000	0.000	0.000
82	X	81	TYR	0	-0.003	-0.011	16.003	0.027	0.027	0.000	0.000	0.000	0.000
83	X	82	GLU	-1	-0.778	-0.875	9.413	-1.252	-1.252	0.000	0.000	0.000	0.000
84	X	83	CYS	0	-0.081	-0.016	10.562	0.056	0.056	0.000	0.000	0.000	0.000
85	X	84	ASP	-1	-0.809	-0.877	4.873	-2.061	-1.994	-0.001	-0.007	-0.059	0.000
86	X	85	TYR	0	-0.029	-0.018	5.025	0.657	0.657	0.000	0.000	0.000	0.000
87	X	86	THR	0	0.015	-0.030	2.466	-1.800	-0.131	4.214	-3.306	-2.577	-0.021
88	X	87	ASP	-1	-0.950	-0.975	3.376	0.608	0.225	0.035	0.271	0.077	0.000
89	X	88	ASN	0	-0.064	-0.037	6.002	-0.519	-0.519	0.000	0.000	0.000	0.000
90	X	89	LYS	1	0.930	0.974	6.748	-0.374	-0.374	0.000	0.000	0.000	0.000
91	X	90	SER	0	0.003	-0.009	7.155	0.008	0.008	0.000	0.000	0.000	0.000
92	X	91	THR	0	-0.035	-0.011	7.720	0.094	0.094	0.000	0.000	0.000	0.000
93	X	92	PHE	0	-0.027	-0.018	10.095	-0.084	-0.084	0.000	0.000	0.000	0.000
94	X	93	ASP	-1	-0.862	-0.923	12.359	-0.441	-0.441	0.000	0.000	0.000	0.000
95	X	94	GLN	0	-0.050	-0.031	14.011	-0.013	-0.013	0.000	0.000	0.000	0.000
96	X	95	PHE	0	0.038	0.029	16.158	0.031	0.031	0.000	0.000	0.000	0.000
97	X	96	TYR	0	-0.013	-0.020	20.169	0.004	0.004	0.000	0.000	0.000	0.000
98	X	97	LEU	0	0.018	0.013	22.151	0.001	0.001	0.000	0.000	0.000	0.000
99	X	98	TYR	0	-0.078	-0.091	25.529	0.010	0.010	0.000	0.000	0.000	0.000
100	X	99	ASN	0	0.028	0.008	29.274	0.001	0.001	0.000	0.000	0.000	0.000
101	X	100	GLY	0	0.055	0.033	26.418	0.003	0.003	0.000	0.000	0.000	0.000
102	X	101	GLU	-1	-0.992	-0.985	26.015	-0.163	-0.163	0.000	0.000	0.000	0.000
103	X	102	GLU	-1	-0.924	-0.965	21.417	-0.265	-0.265	0.000	0.000	0.000	0.000
104	X	103	TYR	0	-0.114	-0.079	25.287	0.018	0.018	0.000	0.000	0.000	0.000
105	X	104	THR	0	0.051	0.009	24.107	-0.002	-0.002	0.000	0.000	0.000	0.000
106	X	105	VAL	0	-0.032	-0.011	26.822	0.008	0.008	0.000	0.000	0.000	0.000
107	X	106	LYS	1	0.957	0.986	28.482	0.110	0.110	0.000	0.000	0.000	0.000
108	X	107	THR	0	0.008	0.011	32.514	0.006	0.006	0.000	0.000	0.000	0.000
109	X	108	GLN	0	-0.013	-0.010	36.182	-0.002	-0.002	0.000	0.000	0.000	0.000
110	X	109	GLU	-1	-0.925	-0.960	38.533	-0.079	-0.079	0.000	0.000	0.000	0.000
111	X	110	ALA	0	-0.014	-0.005	38.220	-0.004	-0.004	0.000	0.000	0.000	0.000
112	X	111	THR	0	0.062	0.029	36.495	-0.001	-0.001	0.000	0.000	0.000	0.000
113	X	112	ASN	0	0.018	-0.006	34.268	0.001	0.001	0.000	0.000	0.000	0.000
114	X	113	LYS	1	0.984	1.025	30.910	0.130	0.130	0.000	0.000	0.000	0.000
115	X	114	ASN	0	0.035	0.016	31.209	-0.014	-0.014	0.000	0.000	0.000	0.000
116	X	115	MET	0	-0.003	0.014	32.064	-0.002	-0.002	0.000	0.000	0.000	0.000
117	X	116	TRP	0	-0.011	-0.009	25.563	0.009	0.009	0.000	0.000	0.000	0.000
118	X	117	LEU	0	-0.005	0.021	26.248	-0.006	-0.006	0.000	0.000	0.000	0.000
119	X	118	THR	0	-0.094	-0.058	27.460	0.000	0.000	0.000	0.000	0.000	0.000
120	X	119	THR	0	-0.058	-0.057	29.243	0.003	0.003	0.000	0.000	0.000	0.000
121	X	120	SER	0	-0.001	-0.006	24.914	0.005	0.005	0.000	0.000	0.000	0.000
122	X	121	GLU	-1	-0.749	-0.826	20.814	-0.171	-0.171	0.000	0.000	0.000	0.000
123	X	122	PHE	0	-0.043	-0.034	23.603	0.006	0.006	0.000	0.000	0.000	0.000
124	X	123	ARG	1	0.793	0.903	26.247	0.144	0.144	0.000	0.000	0.000	0.000
125	X	124	LEU	0	0.025	0.019	19.610	0.008	0.008	0.000	0.000	0.000	0.000
126	X	125	LYS	1	0.865	0.904	18.469	0.188	0.188	0.000	0.000	0.000	0.000
127	X	126	LYS	1	0.869	0.967	22.992	0.091	0.091	0.000	0.000	0.000	0.000
128	X	127	TRP	0	-0.069	-0.045	24.669	0.009	0.009	0.000	0.000	0.000	0.000
129	X	128	PHE	0	-0.001	-0.008	15.609	-0.002	-0.002	0.000	0.000	0.000	0.000
130	X	129	ASP	-1	-0.818	-0.896	19.189	-0.096	-0.096	0.000	0.000	0.000	0.000
131	X	130	GLY	0	0.003	-0.009	15.490	-0.026	-0.026	0.000	0.000	0.000	0.000
132	X	131	GLU	-1	-0.898	-0.967	14.350	-0.061	-0.061	0.000	0.000	0.000	0.000
133	X	132	ASP	-1	-0.798	-0.890	15.214	-0.073	-0.073	0.000	0.000	0.000	0.000
134	X	134	ILE	0	0.031	0.010	9.035	-0.043	-0.043	0.000	0.000	0.000	0.000
135	X	135	MET	0	-0.015	0.000	10.924	0.041	0.041	0.000	0.000	0.000	0.000
136	X	136	HIS	1	0.809	0.891	13.259	0.165	0.165	0.000	0.000	0.000	0.000
137	X	137	LEU	0	0.015	0.026	6.470	0.063	0.063	0.000	0.000	0.000	0.000
138	X	138	ARG	1	0.947	0.971	7.821	-0.616	-0.616	0.000	0.000	0.000	0.000
139	X	139	SER	0	-0.043	-0.033	9.768	0.104	0.104	0.000	0.000	0.000	0.000
140	X	140	LEU	0	-0.039	-0.023	12.022	0.036	0.036	0.000	0.000	0.000	0.000
141	X	141	VAL	0	-0.017	-0.002	6.898	-0.014	-0.014	0.000	0.000	0.000	0.000
142	X	142	ARG	1	0.895	0.939	10.146	-0.302	-0.302	0.000	0.000	0.000	0.000
143	X	143	LYS	1	0.853	0.932	12.563	0.058	0.058	0.000	0.000	0.000	0.000
144	X	144	MET	0	-0.036	-0.016	9.811	0.010	0.010	0.000	0.000	0.000	0.000
145	X	145	GLU	-1	-0.962	-0.995	9.135	0.775	0.775	0.000	0.000	0.000	0.000
146	X	146	ASP	-1	-0.847	-0.909	13.792	0.271	0.271	0.000	0.000	0.000	0.000
147	X	147	SER	0	-0.035	0.009	17.007	-0.021	-0.021	0.000	0.000	0.000	0.000
148	X	148	LYS	1	0.932	0.956	19.014	-0.016	-0.016	0.000	0.000	0.000	0.000
149	X	149	ARG	1	0.882	0.947	14.506	-0.077	-0.077	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(X:0:GLY)