FMO DATABASE

FMODB ID: 6N2YZ

Calculation Name: 4P0J-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4P0J

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UBH0

Base Structure: X-ray

Registration Date: 2023-09-19

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1356620.886525
FMO2-HF: Nuclear repulsion	1299075.101512
FMO2-HF: Total energy	-57545.785013
FMO2-MP2: Total energy	-57710.217904

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:4:SER)

Summations of interaction energy for fragment #1(A:4:SER)

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.
-10.465	-4.423	0.964	-3.285	-3.719	0.013

Interaction energy analysis for fragmet #1(A:4:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : -0.008

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	6	ALA	0	-0.008	0.002	2.638	-6.518	-1.621	0.955	-2.846	-3.006	0.015
4	A	7	LEU	0	-0.003	0.004	4.184	-0.653	-0.491	0.002	-0.053	-0.110	0.000
5	A	150	CYS	0	-0.060	-0.006	7.308	-0.383	-0.383	0.000	0.000	0.000	0.000
6	A	9	PHE	0	0.043	0.013	8.489	0.004	0.004	0.000	0.000	0.000	0.000
7	A	10	ARG	1	0.856	0.915	11.359	-0.237	-0.237	0.000	0.000	0.000	0.000
8	A	11	MET	0	0.013	0.010	14.112	0.026	0.026	0.000	0.000	0.000	0.000
9	A	12	LYS	1	0.915	0.969	16.676	-0.149	-0.149	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.665	-0.786	20.304	0.046	0.046	0.000	0.000	0.000	0.000
11	A	14	SER	0	0.039	0.008	22.938	0.003	0.003	0.000	0.000	0.000	0.000
12	A	15	ALA	0	-0.072	-0.033	25.853	0.000	0.000	0.000	0.000	0.000	0.000
13	A	16	LEU	0	-0.049	-0.029	24.280	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.812	0.913	24.232	-0.018	-0.018	0.000	0.000	0.000	0.000
15	A	18	VAL	0	-0.010	-0.006	18.751	0.008	0.008	0.000	0.000	0.000	0.000
16	A	19	LEU	0	0.022	0.020	16.451	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	20	TYR	0	-0.084	-0.084	16.362	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.027	0.025	12.914	0.001	0.001	0.000	0.000	0.000	0.000
19	A	22	HIS	0	-0.007	-0.007	17.199	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	23	ASN	0	-0.029	-0.021	20.529	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	24	ASN	0	-0.037	-0.023	14.626	0.014	0.014	0.000	0.000	0.000	0.000
22	A	25	GLN	0	0.057	0.047	18.058	0.007	0.007	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.026	0.009	14.984	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	27	LEU	0	-0.020	0.005	18.138	0.015	0.015	0.000	0.000	0.000	0.000
25	A	28	ALA	0	0.046	0.016	20.049	0.004	0.004	0.000	0.000	0.000	0.000
26	A	29	GLY	0	-0.021	-0.031	22.400	0.001	0.001	0.000	0.000	0.000	0.000
27	A	30	GLY	0	0.013	-0.004	23.396	0.007	0.007	0.000	0.000	0.000	0.000
28	A	31	LEU	0	-0.059	-0.025	24.437	0.005	0.005	0.000	0.000	0.000	0.000
29	A	32	HIS	0	-0.018	-0.002	27.249	0.003	0.003	0.000	0.000	0.000	0.000
30	A	33	ALA	0	0.017	0.017	26.442	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	34	GLY	0	0.006	0.006	28.533	0.005	0.005	0.000	0.000	0.000	0.000
32	A	35	LYS	1	0.930	0.947	24.520	0.041	0.041	0.000	0.000	0.000	0.000
33	A	36	VAL	0	0.062	0.042	22.743	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	37	ILE	0	-0.020	0.000	20.352	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	38	LYS	1	0.836	0.926	13.415	0.009	0.009	0.000	0.000	0.000	0.000
36	A	39	GLY	0	0.043	0.014	16.608	0.021	0.021	0.000	0.000	0.000	0.000
37	A	40	GLU	-1	-0.885	-0.958	10.709	-0.355	-0.355	0.000	0.000	0.000	0.000
38	A	41	GLU	-1	-0.863	-0.922	8.693	0.135	0.135	0.000	0.000	0.000	0.000
39	A	42	ILE	0	0.001	-0.006	8.999	-0.162	-0.162	0.000	0.000	0.000	0.000
40	A	43	SER	0	-0.048	-0.024	5.175	-0.161	-0.134	-0.001	0.001	-0.026	0.000
41	A	44	VAL	0	0.018	0.003	7.142	-0.093	-0.093	0.000	0.000	0.000	0.000
42	A	45	VAL	0	0.002	0.003	5.818	0.185	0.185	0.000	0.000	0.000	0.000
43	A	46	PRO	0	0.026	0.015	9.154	-0.153	-0.153	0.000	0.000	0.000	0.000
44	A	47	ASN	0	-0.014	-0.034	11.592	0.047	0.047	0.000	0.000	0.000	0.000
45	A	48	ARG	1	0.892	0.936	12.508	-0.129	-0.129	0.000	0.000	0.000	0.000
46	A	49	TRP	0	-0.071	-0.025	14.061	-0.027	-0.027	0.000	0.000	0.000	0.000
47	A	50	LEU	0	-0.042	-0.014	17.870	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	51	ASP	-1	-0.839	-0.927	19.518	0.102	0.102	0.000	0.000	0.000	0.000
49	A	52	ALA	0	-0.029	-0.019	19.322	0.008	0.008	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.029	-0.001	20.385	0.011	0.011	0.000	0.000	0.000	0.000
51	A	54	LEU	0	-0.013	-0.012	22.598	0.002	0.002	0.000	0.000	0.000	0.000
52	A	55	SER	0	-0.006	-0.008	18.264	0.014	0.014	0.000	0.000	0.000	0.000
53	A	56	PRO	0	0.023	0.036	16.950	0.004	0.004	0.000	0.000	0.000	0.000
54	A	57	VAL	0	-0.036	-0.027	12.674	0.051	0.051	0.000	0.000	0.000	0.000
55	A	58	ILE	0	0.014	0.011	10.280	-0.065	-0.065	0.000	0.000	0.000	0.000
56	A	59	LEU	0	-0.019	-0.001	10.092	0.085	0.085	0.000	0.000	0.000	0.000
57	A	60	GLY	0	0.036	0.014	7.817	-0.057	-0.057	0.000	0.000	0.000	0.000
58	A	61	VAL	0	-0.015	-0.013	8.779	0.082	0.082	0.000	0.000	0.000	0.000
59	A	62	GLN	0	-0.006	-0.013	8.022	-0.150	-0.150	0.000	0.000	0.000	0.000
60	A	63	GLY	0	0.004	0.011	4.295	-0.074	-0.031	-0.001	-0.006	-0.036	0.000
61	A	64	GLY	0	-0.007	0.000	3.530	-2.782	-2.204	0.004	-0.309	-0.273	-0.002
62	A	65	SER	0	-0.058	-0.037	5.211	0.505	0.521	-0.001	0.000	-0.015	0.000
63	A	66	GLN	0	0.027	0.020	7.705	0.196	0.196	0.000	0.000	0.000	0.000
64	A	67	CYS	0	-0.039	-0.006	9.308	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	68	LEU	0	0.007	0.008	11.368	0.011	0.011	0.000	0.000	0.000	0.000
66	A	69	SER	0	0.017	0.010	14.580	0.036	0.036	0.000	0.000	0.000	0.000
67	A	70	CYS	0	-0.006	0.026	17.397	0.004	0.004	0.000	0.000	0.000	0.000
68	A	71	GLY	0	0.038	0.031	20.527	0.004	0.004	0.000	0.000	0.000	0.000
69	A	72	VAL	0	0.004	-0.024	22.473	0.005	0.005	0.000	0.000	0.000	0.000
70	A	73	GLY	0	-0.003	0.016	25.040	0.004	0.004	0.000	0.000	0.000	0.000
71	A	74	GLN	0	0.019	0.019	28.201	0.002	0.002	0.000	0.000	0.000	0.000
72	A	75	GLU	-1	-0.930	-0.966	29.565	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	76	PRO	0	-0.019	0.007	24.454	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	77	THR	0	-0.068	-0.055	24.010	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	78	LEU	0	-0.068	-0.014	18.166	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	79	THR	0	-0.007	-0.023	19.411	0.002	0.002	0.000	0.000	0.000	0.000
77	A	80	LEU	0	-0.026	-0.017	13.168	0.003	0.003	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.848	-0.909	14.694	-0.154	-0.154	0.000	0.000	0.000	0.000
79	A	82	PRO	0	-0.043	-0.011	13.129	-0.059	-0.059	0.000	0.000	0.000	0.000
80	A	83	VAL	0	-0.035	-0.017	11.924	0.006	0.006	0.000	0.000	0.000	0.000
81	A	84	ASN	0	0.041	0.016	6.192	0.133	0.133	0.000	0.000	0.000	0.000
82	A	85	ILE	0	0.066	0.008	3.975	0.108	0.212	-0.001	-0.011	-0.092	0.000
83	A	86	MET	0	-0.022	-0.014	4.564	0.213	0.428	0.007	-0.061	-0.161	0.000
84	A	87	GLU	-1	-0.839	-0.919	7.447	-0.355	-0.355	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.001	0.008	10.419	0.038	0.038	0.000	0.000	0.000	0.000
86	A	89	TYR	0	0.016	0.008	8.527	0.040	0.040	0.000	0.000	0.000	0.000
87	A	90	LEU	0	-0.040	-0.030	8.625	-0.023	-0.023	0.000	0.000	0.000	0.000
88	A	91	GLY	0	-0.011	0.000	11.723	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	92	ALA	0	-0.061	-0.015	13.694	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	93	LYS	1	0.936	0.971	14.945	0.095	0.095	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.864	-0.918	16.045	0.008	0.008	0.000	0.000	0.000	0.000
92	A	95	SER	0	0.083	0.019	14.599	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.964	0.993	16.220	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	97	SER	0	-0.009	-0.004	18.650	0.010	0.010	0.000	0.000	0.000	0.000
95	A	98	PHE	0	-0.008	-0.010	13.585	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	99	THR	0	-0.043	-0.023	14.527	0.035	0.035	0.000	0.000	0.000	0.000
97	A	100	PHE	0	-0.010	-0.009	15.472	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.003	-0.009	17.500	0.028	0.028	0.000	0.000	0.000	0.000
99	A	102	ARG	1	0.818	0.893	15.993	-0.248	-0.248	0.000	0.000	0.000	0.000
100	A	103	ARG	1	0.853	0.902	19.283	-0.081	-0.081	0.000	0.000	0.000	0.000
101	A	104	ASP	-1	-0.786	-0.842	19.853	0.203	0.203	0.000	0.000	0.000	0.000
102	A	105	MET	0	-0.024	-0.011	22.716	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	106	GLY	0	0.009	0.001	25.925	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.037	-0.020	24.219	0.012	0.012	0.000	0.000	0.000	0.000
105	A	108	THR	0	-0.064	-0.033	22.019	0.011	0.011	0.000	0.000	0.000	0.000
106	A	109	SER	0	-0.029	-0.033	18.897	0.007	0.007	0.000	0.000	0.000	0.000
107	A	110	SER	0	0.012	0.017	20.989	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	111	PHE	0	0.004	-0.020	15.601	0.015	0.015	0.000	0.000	0.000	0.000
109	A	112	GLU	-1	-0.770	-0.846	20.122	0.038	0.038	0.000	0.000	0.000	0.000
110	A	113	SER	0	0.013	-0.014	20.592	0.010	0.010	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.002	-0.008	20.306	0.000	0.000	0.000	0.000	0.000	0.000
112	A	115	ALA	0	-0.082	-0.040	21.788	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	116	TYR	0	-0.046	-0.032	23.519	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	117	PRO	0	0.037	0.010	25.749	0.003	0.003	0.000	0.000	0.000	0.000
115	A	118	GLY	0	-0.011	-0.012	27.214	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	119	TRP	0	-0.011	-0.001	25.461	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	120	PHE	0	-0.014	-0.023	23.471	0.006	0.006	0.000	0.000	0.000	0.000
118	A	121	LEU	0	-0.023	-0.008	17.383	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	122	CYS	0	-0.054	-0.026	21.543	0.007	0.007	0.000	0.000	0.000	0.000
120	A	123	THR	0	-0.042	-0.043	22.278	-0.011	-0.011	0.000	0.000	0.000	0.000
121	A	124	VAL	0	0.040	0.021	24.888	0.004	0.004	0.000	0.000	0.000	0.000
122	A	125	PRO	0	-0.010	-0.022	28.061	0.001	0.001	0.000	0.000	0.000	0.000
123	A	126	GLU	-1	-0.923	-0.936	30.586	-0.014	-0.014	0.000	0.000	0.000	0.000
124	A	127	ALA	0	0.000	-0.007	28.381	0.000	0.000	0.000	0.000	0.000	0.000
125	A	128	ASP	-1	-0.801	-0.880	25.039	-0.019	-0.019	0.000	0.000	0.000	0.000
126	A	129	GLN	0	0.026	0.013	26.067	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	130	PRO	0	-0.019	-0.016	22.715	0.003	0.003	0.000	0.000	0.000	0.000
128	A	131	VAL	0	0.001	0.004	18.987	0.011	0.011	0.000	0.000	0.000	0.000
129	A	132	ARG	1	0.841	0.911	21.846	0.013	0.013	0.000	0.000	0.000	0.000
130	A	133	LEU	0	0.035	0.020	21.182	0.008	0.008	0.000	0.000	0.000	0.000
131	A	134	THR	0	0.014	0.000	24.713	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	135	GLN	0	0.053	0.034	27.552	0.003	0.003	0.000	0.000	0.000	0.000
133	A	136	GLU	-1	-0.861	-0.910	30.219	0.013	0.013	0.000	0.000	0.000	0.000
134	A	137	LEU	0	0.011	0.006	27.843	0.000	0.000	0.000	0.000	0.000	0.000
135	A	138	GLY	0	0.003	0.011	31.087	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	139	LYS	1	0.782	0.863	32.207	-0.012	-0.012	0.000	0.000	0.000	0.000
137	A	140	SER	0	0.019	0.002	32.928	0.002	0.002	0.000	0.000	0.000	0.000
138	A	141	TYR	0	-0.023	-0.006	28.313	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	142	ASN	0	0.008	0.006	25.865	0.010	0.010	0.000	0.000	0.000	0.000
140	A	143	THR	0	0.053	0.013	24.186	-0.006	-0.006	0.000	0.000	0.000	0.000
141	A	144	ASP	-1	-0.878	-0.917	23.457	0.089	0.089	0.000	0.000	0.000	0.000
142	A	145	PHE	0	-0.026	-0.032	18.957	-0.009	-0.009	0.000	0.000	0.000	0.000
143	A	146	TYR	0	-0.009	0.002	20.363	0.017	0.017	0.000	0.000	0.000	0.000
144	A	147	PHE	0	0.034	-0.004	13.753	0.000	0.000	0.000	0.000	0.000	0.000
145	A	148	GLN	0	-0.031	-0.015	15.670	-0.019	-0.019	0.000	0.000	0.000	0.000
146	A	149	GLN	0	0.037	0.028	11.685	0.008	0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:SER)