FMO DATABASE

FMODB ID: YYQZ2

Calculation Name: 4HFF-A-Xray321

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4HFF

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZRL5

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	161
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1569886.255977
FMO2-HF: Nuclear repulsion	1507900.500667
FMO2-HF: Total energy	-61985.75531
FMO2-MP2: Total energy	-62166.463233

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:ACE )

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

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.
0.75	1.706	-0.001	-0.436	-0.52	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : -0.004

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].
3	A	3	ARG	1	0.834	0.909	3.817	1.788	2.554	-0.007	-0.369	-0.391
4	A	4	PRO	0	0.035	0.026	7.173	0.031	0.031	0.000	0.000	0.000
5	A	5	SER	0	0.032	-0.003	9.554	-0.040	-0.040	0.000	0.000	0.000
6	A	6	PHE	0	0.037	-0.005	12.289	0.066	0.066	0.000	0.000	0.000
7	A	7	ASN	0	-0.004	-0.016	15.456	0.044	0.044	0.000	0.000	0.000
8	A	8	GLU	-1	-0.873	-0.914	13.073	-0.105	-0.105	0.000	0.000	0.000
9	A	9	ALA	0	0.029	0.018	14.009	0.036	0.036	0.000	0.000	0.000
10	A	10	TRP	0	0.018	0.002	15.729	0.028	0.028	0.000	0.000	0.000
11	A	11	LEU	0	-0.042	-0.014	18.980	0.019	0.019	0.000	0.000	0.000
12	A	12	ALA	0	0.020	-0.003	17.010	0.016	0.016	0.000	0.000	0.000
13	A	13	PHE	0	0.035	0.008	19.013	0.013	0.013	0.000	0.000	0.000
14	A	14	ARG	1	0.956	0.979	20.598	0.060	0.060	0.000	0.000	0.000
15	A	15	LYS	1	0.895	0.956	22.121	0.007	0.007	0.000	0.000	0.000
16	A	16	VAL	0	0.016	0.017	21.471	0.007	0.007	0.000	0.000	0.000
17	A	17	ASN	0	-0.042	-0.014	24.363	0.004	0.004	0.000	0.000	0.000
18	A	18	HIS	0	0.024	0.016	26.243	-0.002	-0.002	0.000	0.000	0.000
19	A	19	SER	0	0.039	0.017	28.824	0.002	0.002	0.000	0.000	0.000
20	A	20	VAL	0	0.059	0.012	28.280	0.002	0.002	0.000	0.000	0.000
21	A	21	ALA	0	0.063	0.031	29.649	0.005	0.005	0.000	0.000	0.000
22	A	22	ASP	-1	-0.838	-0.921	30.603	0.012	0.012	0.000	0.000	0.000
23	A	23	VAL	0	-0.082	-0.043	24.773	0.004	0.004	0.000	0.000	0.000
24	A	24	GLY	0	0.007	-0.005	26.689	0.007	0.007	0.000	0.000	0.000
25	A	25	SER	0	-0.025	-0.022	28.643	0.006	0.006	0.000	0.000	0.000
26	A	26	ILE	0	-0.081	-0.021	24.493	0.003	0.003	0.000	0.000	0.000
27	A	27	ILE	0	-0.038	-0.012	21.940	0.006	0.006	0.000	0.000	0.000
28	A	28	GLY	0	0.086	0.048	24.710	0.009	0.009	0.000	0.000	0.000
29	A	29	GLY	0	0.032	0.001	26.230	0.005	0.005	0.000	0.000	0.000
30	A	30	ASN	0	-0.001	-0.008	25.574	-0.014	-0.014	0.000	0.000	0.000
31	A	31	VAL	0	0.034	0.036	22.757	-0.006	-0.006	0.000	0.000	0.000
32	A	32	GLY	0	0.036	0.023	25.984	-0.007	-0.007	0.000	0.000	0.000
33	A	33	LYS	1	0.905	0.964	29.059	-0.069	-0.069	0.000	0.000	0.000
34	A	34	ASN	0	-0.050	-0.056	27.927	-0.006	-0.006	0.000	0.000	0.000
35	A	35	ILE	0	-0.027	-0.002	26.955	-0.004	-0.004	0.000	0.000	0.000
36	A	36	THR	0	-0.033	-0.006	30.952	-0.004	-0.004	0.000	0.000	0.000
37	A	37	GLY	0	-0.041	-0.021	33.703	-0.002	-0.002	0.000	0.000	0.000
38	A	38	GLY	0	0.024	0.021	34.128	-0.001	-0.001	0.000	0.000	0.000
39	A	39	TYR	0	-0.045	-0.017	31.114	-0.001	-0.001	0.000	0.000	0.000
40	A	40	PHE	0	-0.074	-0.038	25.548	0.001	0.001	0.000	0.000	0.000
41	A	41	GLN	0	0.082	0.028	29.610	0.000	0.000	0.000	0.000	0.000
42	A	42	ASN	0	0.004	-0.002	26.695	-0.006	-0.006	0.000	0.000	0.000
43	A	43	ALA	0	0.054	0.014	25.498	0.004	0.004	0.000	0.000	0.000
44	A	44	CYS	0	-0.021	0.028	22.225	0.004	0.004	0.000	0.000	0.000
45	A	45	PRO	0	0.001	0.007	19.801	-0.004	-0.004	0.000	0.000	0.000
46	A	46	ILE	0	0.050	0.023	19.090	0.010	0.010	0.000	0.000	0.000
47	A	47	ARG	1	0.914	0.955	19.897	0.017	0.017	0.000	0.000	0.000
48	A	48	MET	0	0.011	0.015	15.326	-0.006	-0.006	0.000	0.000	0.000
49	A	49	SER	0	0.001	-0.007	15.425	0.012	0.012	0.000	0.000	0.000
50	A	50	TYR	0	-0.003	-0.001	15.499	0.020	0.020	0.000	0.000	0.000
51	A	51	VAL	0	-0.021	-0.010	13.994	0.007	0.007	0.000	0.000	0.000
52	A	52	LEU	0	0.003	0.007	9.973	-0.012	-0.012	0.000	0.000	0.000
53	A	53	ASN	0	-0.012	-0.026	11.340	0.088	0.088	0.000	0.000	0.000
54	A	54	ALA	0	-0.076	-0.030	13.594	0.023	0.023	0.000	0.000	0.000
55	A	55	THR	0	-0.034	-0.017	11.355	-0.015	-0.015	0.000	0.000	0.000
56	A	56	GLY	0	0.026	0.024	9.029	-0.060	-0.060	0.000	0.000	0.000
57	A	57	PHE	0	-0.051	-0.018	3.746	0.019	0.209	0.006	-0.067	-0.129
58	A	58	PRO	0	0.024	0.011	8.007	-0.083	-0.083	0.000	0.000	0.000
59	A	59	ILE	0	-0.025	0.006	9.740	0.109	0.109	0.000	0.000	0.000
60	A	60	ALA	0	0.015	0.003	10.506	-0.017	-0.017	0.000	0.000	0.000
61	A	61	ARG	1	0.984	0.976	12.290	-0.264	-0.264	0.000	0.000	0.000
62	A	62	ASN	0	0.012	-0.005	12.740	-0.040	-0.040	0.000	0.000	0.000
63	A	63	SER	0	-0.012	0.022	12.524	-0.024	-0.024	0.000	0.000	0.000
64	A	64	PRO	0	0.032	0.034	14.261	-0.022	-0.022	0.000	0.000	0.000
65	A	65	TYR	0	0.058	0.012	13.776	-0.027	-0.027	0.000	0.000	0.000
66	A	66	ALA	0	-0.023	0.011	18.509	0.016	0.016	0.000	0.000	0.000
67	A	67	LYS	1	0.804	0.888	16.039	-0.196	-0.196	0.000	0.000	0.000
68	A	68	VAL	0	-0.022	-0.013	20.393	-0.004	-0.004	0.000	0.000	0.000
69	A	69	SER	0	0.011	0.003	21.094	0.002	0.002	0.000	0.000	0.000
70	A	70	GLY	0	0.078	0.034	21.396	-0.015	-0.015	0.000	0.000	0.000
71	A	71	ALA	0	-0.033	-0.018	23.056	0.009	0.009	0.000	0.000	0.000
72	A	72	ASP	-1	-0.796	-0.886	19.268	0.122	0.122	0.000	0.000	0.000
73	A	73	ASN	0	-0.082	-0.043	20.034	0.013	0.013	0.000	0.000	0.000
74	A	74	LYS	1	0.904	0.978	14.797	-0.147	-0.147	0.000	0.000	0.000
75	A	75	PHE	0	-0.007	-0.028	15.767	-0.031	-0.031	0.000	0.000	0.000
76	A	76	TYR	0	-0.046	-0.029	16.670	-0.001	-0.001	0.000	0.000	0.000
77	A	77	ILE	0	0.028	0.019	15.228	-0.004	-0.004	0.000	0.000	0.000
78	A	78	TYR	0	0.028	0.005	19.220	-0.015	-0.015	0.000	0.000	0.000
79	A	79	ARG	1	0.939	0.973	21.721	-0.060	-0.060	0.000	0.000	0.000
80	A	80	VAL	0	0.034	0.009	21.053	0.004	0.004	0.000	0.000	0.000
81	A	81	ASN	0	0.019	-0.012	20.531	-0.011	-0.011	0.000	0.000	0.000
82	A	82	ASP	-1	-0.788	-0.888	18.822	0.062	0.062	0.000	0.000	0.000
83	A	83	MET	0	-0.057	-0.019	15.210	0.003	0.003	0.000	0.000	0.000
84	A	84	ILE	0	0.015	-0.002	15.618	-0.011	-0.011	0.000	0.000	0.000
85	A	85	ASP	-1	-0.879	-0.935	15.776	-0.009	-0.009	0.000	0.000	0.000
86	A	86	TYR	0	0.006	-0.007	9.251	0.033	0.033	0.000	0.000	0.000
87	A	87	LEU	0	0.015	-0.008	11.338	0.009	0.009	0.000	0.000	0.000
88	A	88	THR	0	-0.039	-0.021	11.112	-0.064	-0.064	0.000	0.000	0.000
89	A	89	HIS	0	-0.083	-0.044	10.953	0.010	0.010	0.000	0.000	0.000
90	A	90	THR	0	-0.096	-0.030	6.958	0.019	0.019	0.000	0.000	0.000
91	A	91	MET	0	-0.007	0.007	6.075	-0.134	-0.134	0.000	0.000	0.000
92	A	92	GLY	0	0.014	0.018	8.180	-0.133	-0.133	0.000	0.000	0.000
93	A	93	LYS	1	0.906	0.946	9.914	0.218	0.218	0.000	0.000	0.000
94	A	94	PRO	0	-0.004	0.001	12.772	-0.065	-0.065	0.000	0.000	0.000
95	A	95	ASP	-1	-0.806	-0.889	14.048	-0.462	-0.462	0.000	0.000	0.000
96	A	96	LEU	0	-0.046	-0.017	16.371	0.024	0.024	0.000	0.000	0.000
97	A	97	ILE	0	-0.012	-0.013	18.653	0.004	0.004	0.000	0.000	0.000
98	A	98	VAL	0	-0.010	0.003	21.674	0.003	0.003	0.000	0.000	0.000
99	A	99	ASN	0	0.018	-0.006	25.305	0.004	0.004	0.000	0.000	0.000
100	A	100	ASN	0	-0.050	-0.032	28.167	0.001	0.001	0.000	0.000	0.000
101	A	101	PRO	0	-0.055	0.009	26.210	-0.002	-0.002	0.000	0.000	0.000
102	A	102	LYS	1	1.036	1.006	28.330	0.077	0.077	0.000	0.000	0.000
103	A	103	GLN	0	0.010	-0.004	28.387	-0.007	-0.007	0.000	0.000	0.000
104	A	104	SER	0	-0.024	-0.021	28.163	-0.006	-0.006	0.000	0.000	0.000
105	A	105	ASP	-1	-0.860	-0.926	26.708	-0.093	-0.093	0.000	0.000	0.000
106	A	106	PHE	0	-0.046	-0.030	21.552	-0.013	-0.013	0.000	0.000	0.000
107	A	107	ILE	0	0.028	0.034	24.189	-0.009	-0.009	0.000	0.000	0.000
108	A	108	GLY	0	-0.035	-0.015	24.885	-0.007	-0.007	0.000	0.000	0.000
109	A	109	LYS	1	0.923	0.963	19.953	0.170	0.170	0.000	0.000	0.000
110	A	110	LYS	1	0.964	0.986	18.290	0.247	0.247	0.000	0.000	0.000
111	A	111	GLY	0	0.005	-0.003	15.855	-0.047	-0.047	0.000	0.000	0.000
112	A	112	ILE	0	-0.006	-0.004	12.183	0.044	0.044	0.000	0.000	0.000
113	A	113	ILE	0	0.009	0.011	16.083	-0.015	-0.015	0.000	0.000	0.000
114	A	114	VAL	0	-0.024	-0.017	17.564	0.021	0.021	0.000	0.000	0.000
115	A	115	VAL	0	0.034	0.022	20.250	-0.007	-0.007	0.000	0.000	0.000
116	A	116	LYS	1	0.905	0.954	21.875	0.042	0.042	0.000	0.000	0.000
117	A	117	GLY	0	0.098	0.044	25.673	-0.005	-0.005	0.000	0.000	0.000
118	A	118	HIS	0	-0.106	-0.062	29.475	0.007	0.007	0.000	0.000	0.000
119	A	119	GLY	0	0.088	0.038	32.754	-0.002	-0.002	0.000	0.000	0.000
120	A	120	TRP	0	-0.021	0.005	27.442	0.001	0.001	0.000	0.000	0.000
121	A	121	SER	0	-0.019	-0.018	33.352	0.001	0.001	0.000	0.000	0.000
122	A	122	ASN	0	-0.009	-0.006	30.042	0.001	0.001	0.000	0.000	0.000
123	A	123	ALA	0	-0.034	-0.023	26.871	0.004	0.004	0.000	0.000	0.000
124	A	124	ARG	1	0.946	0.974	26.090	0.012	0.012	0.000	0.000	0.000
125	A	125	GLY	0	0.050	0.026	25.391	-0.006	-0.006	0.000	0.000	0.000
126	A	126	HIS	0	-0.031	-0.020	23.966	0.012	0.012	0.000	0.000	0.000
127	A	127	VAL	0	0.002	-0.008	17.311	-0.008	-0.008	0.000	0.000	0.000
128	A	128	THR	0	-0.026	-0.032	19.995	0.012	0.012	0.000	0.000	0.000
129	A	129	LEU	0	0.015	0.016	16.335	-0.021	-0.021	0.000	0.000	0.000
130	A	130	TRP	0	0.012	0.000	19.476	0.021	0.021	0.000	0.000	0.000
131	A	131	ASN	0	0.049	0.012	20.293	-0.023	-0.023	0.000	0.000	0.000
132	A	132	GLY	0	0.008	0.019	22.591	-0.003	-0.003	0.000	0.000	0.000
133	A	133	SER	0	-0.057	-0.040	24.417	0.009	0.009	0.000	0.000	0.000
134	A	134	ILE	0	0.037	0.025	26.338	0.007	0.007	0.000	0.000	0.000
135	A	135	CYS	0	-0.024	-0.007	24.040	-0.011	-0.011	0.000	0.000	0.000
136	A	136	SER	0	-0.017	-0.015	22.137	0.001	0.001	0.000	0.000	0.000
137	A	137	ASP	-1	-0.840	-0.887	24.214	-0.036	-0.036	0.000	0.000	0.000
138	A	138	GLN	0	-0.028	-0.036	26.287	0.002	0.002	0.000	0.000	0.000
139	A	139	CYS	0	-0.022	-0.036	27.954	0.000	0.000	0.000	0.000	0.000
140	A	140	HIS	0	0.049	0.022	28.722	-0.006	-0.006	0.000	0.000	0.000
141	A	141	LEU	0	-0.012	0.000	26.112	0.002	0.002	0.000	0.000	0.000
142	A	142	LEU	0	-0.012	0.012	25.445	-0.001	-0.001	0.000	0.000	0.000
143	A	143	ASN	0	-0.101	-0.055	30.085	0.001	0.001	0.000	0.000	0.000
144	A	144	ASP	-1	-0.860	-0.936	33.431	-0.053	-0.053	0.000	0.000	0.000
145	A	145	PRO	0	-0.029	0.004	36.016	0.002	0.002	0.000	0.000	0.000
146	A	146	ASP	-1	-0.864	-0.945	38.946	-0.030	-0.030	0.000	0.000	0.000
147	A	147	ASN	0	-0.061	-0.029	40.748	0.000	0.000	0.000	0.000	0.000
148	A	148	GLY	0	-0.017	-0.003	36.996	0.002	0.002	0.000	0.000	0.000
149	A	149	PRO	0	-0.016	-0.011	36.050	0.000	0.000	0.000	0.000	0.000
150	A	150	PHE	0	-0.065	-0.031	27.784	0.000	0.000	0.000	0.000	0.000
151	A	151	VAL	0	0.079	0.037	33.418	-0.003	-0.003	0.000	0.000	0.000
152	A	152	PRO	0	-0.032	-0.017	28.420	0.001	0.001	0.000	0.000	0.000
153	A	153	GLU	-1	-0.836	-0.900	28.849	-0.034	-0.034	0.000	0.000	0.000
154	A	154	VAL	0	-0.015	-0.007	23.309	-0.005	-0.005	0.000	0.000	0.000
155	A	155	GLY	0	0.012	0.009	23.451	0.004	0.004	0.000	0.000	0.000
156	A	156	THR	0	-0.044	-0.030	17.361	-0.007	-0.007	0.000	0.000	0.000
157	A	157	LEU	0	0.003	-0.002	17.100	0.008	0.008	0.000	0.000	0.000
158	A	158	TRP	0	-0.005	0.005	11.395	0.007	0.007	0.000	0.000	0.000
159	A	159	ILE	0	-0.014	-0.016	14.122	0.031	0.031	0.000	0.000	0.000
160	A	160	LEU	0	-0.074	-0.038	11.266	-0.089	-0.089	0.000	0.000	0.000
161	A	161	PRO	-1	-0.892	-0.928	10.271	-0.297	-0.297	0.000	0.000	0.000

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