FMO DATABASE

FMODB ID: 72RZK

Calculation Name: 3F6A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3F6A

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

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:

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	150
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1417742.131583
FMO2-HF: Nuclear repulsion	1358416.465873
FMO2-HF: Total energy	-59325.66571
FMO2-MP2: Total energy	-59499.036081

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:LEU)

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

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.
-0.9	2.186	0.192	-1.569	-1.708	0.007

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / q_NPA : 0.007

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	ARG	1	0.957	1.002	3.826	0.132	2.252	-0.029	-1.149	-0.941	0.001
4	A	4	HIS	0	-0.040	-0.033	5.571	-0.573	-0.573	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.009	-0.003	3.146	-1.394	-0.428	0.221	-0.420	-0.767	0.006
6	A	6	THR	0	-0.016	-0.023	8.613	-0.163	-0.163	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.027	-0.005	12.348	0.065	0.065	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.016	-0.017	15.180	-0.062	-0.062	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.029	-0.027	18.722	0.000	0.000	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.021	-0.001	21.801	-0.020	-0.020	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.008	-0.001	25.123	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.019	0.002	27.752	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	13	CYS	0	-0.053	-0.011	31.107	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.868	0.914	34.361	-0.079	-0.079	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.806	-0.882	36.302	0.080	0.080	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.829	0.898	35.266	-0.087	-0.087	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.027	0.017	28.883	0.003	0.003	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.029	-0.003	28.719	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.023	-0.007	26.926	0.013	0.013	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.045	0.005	23.529	-0.037	-0.037	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.063	-0.018	27.526	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.109	0.081	20.926	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.894	0.954	26.174	-0.149	-0.149	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.917	0.954	26.164	-0.102	-0.102	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.078	0.022	25.171	0.003	0.003	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.913	0.953	27.221	-0.089	-0.089	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.905	0.959	23.407	-0.207	-0.207	0.000	0.000	0.000	0.000
28	A	28	MET	0	-0.062	-0.013	27.797	0.002	0.002	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.003	-0.011	22.017	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.026	0.028	21.724	-0.022	-0.022	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.010	-0.004	22.962	0.004	0.004	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.002	-0.018	19.098	0.021	0.021	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.026	0.035	16.975	-0.038	-0.038	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.041	-0.030	12.520	0.098	0.098	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.003	0.010	9.769	-0.049	-0.049	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.915	-0.945	10.876	0.191	0.191	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.044	-0.038	7.183	0.056	0.056	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.105	-0.066	8.973	-0.115	-0.115	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.785	-0.886	10.781	0.272	0.272	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.025	-0.013	11.265	0.136	0.136	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.038	0.003	10.842	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.829	-0.931	13.557	0.205	0.205	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.851	-0.936	15.869	0.169	0.169	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.035	0.023	14.529	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	45	CYS	0	-0.078	-0.030	16.652	-0.022	-0.022	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.036	-0.023	19.293	-0.032	-0.032	0.000	0.000	0.000	0.000
47	A	47	ARG	1	0.741	0.864	16.259	-0.311	-0.311	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.763	-0.865	18.080	0.283	0.283	0.000	0.000	0.000	0.000
49	A	49	ALA	0	-0.042	-0.019	21.447	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.801	0.897	24.318	-0.123	-0.123	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.775	-0.877	21.165	0.173	0.173	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.804	-0.912	22.906	0.214	0.214	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.039	-0.041	26.139	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.043	0.044	28.462	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.074	-0.033	28.481	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	56	ASN	0	0.023	0.024	27.745	0.009	0.009	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.014	0.001	24.617	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.040	-0.017	27.047	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.014	0.005	20.324	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	60	TYR	0	0.000	0.001	24.200	-0.018	-0.018	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.027	-0.009	22.460	0.023	0.023	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.019	0.007	23.391	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.002	-0.007	24.189	0.003	0.003	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.812	-0.894	23.414	0.074	0.074	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.031	-0.041	25.117	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.014	-0.008	27.309	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.062	0.051	19.629	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.966	0.988	22.996	-0.078	-0.078	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.946	0.963	24.044	-0.041	-0.041	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.009	-0.015	24.805	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	71	CYS	0	-0.001	0.013	20.378	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.876	-0.945	21.828	0.040	0.040	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.103	-0.043	23.773	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.069	-0.038	21.071	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.025	-0.004	20.498	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.982	-0.983	15.831	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.923	0.938	17.630	-0.041	-0.041	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.016	0.003	17.398	0.014	0.014	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.008	0.003	13.685	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.052	-0.002	17.662	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.016	-0.019	15.968	0.053	0.053	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.023	-0.003	13.821	-0.025	-0.025	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.027	-0.011	17.097	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	84	HIS	1	0.778	0.851	18.376	-0.269	-0.269	0.000	0.000	0.000	0.000
85	A	85	THR	0	0.046	0.024	12.010	0.031	0.031	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.035	-0.016	14.988	-0.060	-0.060	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.006	0.017	11.198	0.098	0.098	0.000	0.000	0.000	0.000
88	A	88	GLY	0	-0.001	0.004	13.650	-0.093	-0.093	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.886	-0.955	14.131	0.367	0.367	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.095	-0.058	16.485	-0.037	-0.037	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.059	-0.015	18.423	0.011	0.011	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.134	0.065	14.150	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.048	-0.033	16.400	0.024	0.024	0.000	0.000	0.000	0.000
94	A	94	HIS	0	-0.002	-0.010	10.681	-0.137	-0.137	0.000	0.000	0.000	0.000
95	A	95	SER	0	0.014	0.011	10.902	0.056	0.056	0.000	0.000	0.000	0.000
96	A	96	HIS	0	-0.075	-0.031	9.635	0.112	0.112	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.000	0.008	6.997	-0.209	-0.209	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.769	-0.841	10.591	0.623	0.623	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.039	-0.025	8.565	-0.076	-0.076	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.030	0.009	14.268	-0.047	-0.047	0.000	0.000	0.000	0.000
101	A	101	TYR	0	0.058	0.023	14.947	0.001	0.001	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.033	-0.047	20.306	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.025	0.010	24.102	0.000	0.000	0.000	0.000	0.000	0.000
104	A	104	THR	0	0.036	0.034	26.244	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.018	-0.015	29.332	0.002	0.002	0.000	0.000	0.000	0.000
106	A	106	THR	0	0.020	0.009	31.702	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.024	-0.012	34.969	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	108	PHE	0	0.007	-0.017	34.864	0.003	0.003	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.977	-0.972	35.806	0.071	0.071	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.011	-0.010	31.970	0.005	0.005	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.036	-0.029	32.486	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.023	0.003	29.272	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.865	-0.918	27.307	0.094	0.094	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.022	-0.027	28.421	0.003	0.003	0.000	0.000	0.000	0.000
115	A	115	GLY	0	-0.023	-0.009	27.813	0.005	0.005	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.806	-0.890	24.063	0.174	0.174	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.137	-0.105	27.001	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.803	0.890	28.877	-0.100	-0.100	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.071	-0.027	31.613	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	120	LEU	0	0.076	0.044	29.735	0.008	0.008	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.877	0.939	32.152	-0.104	-0.104	0.000	0.000	0.000	0.000
122	A	122	TRP	0	0.028	0.015	31.724	0.008	0.008	0.000	0.000	0.000	0.000
123	A	123	TYR	0	-0.069	-0.049	32.558	-0.009	-0.009	0.000	0.000	0.000	0.000
124	A	124	SER	0	0.020	-0.015	34.883	0.002	0.002	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.934	0.933	34.953	-0.096	-0.096	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.911	-0.952	36.720	0.070	0.070	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.934	-0.905	36.975	0.084	0.084	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.058	0.010	33.604	0.005	0.005	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.903	0.943	35.438	-0.074	-0.074	0.000	0.000	0.000	0.000
130	A	130	ASN	0	-0.003	-0.009	37.156	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	131	ALA	0	-0.018	0.005	34.477	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	132	HIS	0	0.047	0.021	35.460	0.002	0.002	0.000	0.000	0.000	0.000
133	A	133	ASN	0	-0.078	-0.053	32.319	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.027	0.014	28.920	0.007	0.007	0.000	0.000	0.000	0.000
135	A	135	GLN	0	0.052	0.043	22.597	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.806	-0.918	27.847	0.129	0.129	0.000	0.000	0.000	0.000
137	A	137	ASN	0	0.034	0.010	21.789	-0.016	-0.016	0.000	0.000	0.000	0.000
138	A	138	ILE	0	-0.017	-0.001	22.525	0.008	0.008	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.017	0.010	25.915	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.006	0.010	26.961	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	141	MET	0	0.016	0.018	21.171	0.005	0.005	0.000	0.000	0.000	0.000
142	A	142	ALA	0	0.015	0.017	25.989	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	143	THR	0	-0.035	-0.037	28.466	-0.012	-0.012	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.815	-0.852	25.367	0.188	0.188	0.000	0.000	0.000	0.000
145	A	145	ALA	0	-0.007	-0.001	26.737	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	146	LEU	0	-0.030	-0.015	28.404	-0.008	-0.008	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.892	-0.934	31.859	0.099	0.099	0.000	0.000	0.000	0.000
148	A	148	LEU	0	-0.088	-0.029	26.916	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	149	LEU	0	-0.113	-0.064	27.533	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.970	-0.966	31.985	0.077	0.077	0.000	0.000	0.000	0.000

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