FMO DATABASE

FMODB ID: K94K3

Calculation Name: 2P25-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2P25

Chain ID: A

ChEMBL ID:

UniProt ID: Q832L2

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:

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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1082096.474221
FMO2-HF: Nuclear repulsion	1031256.264735
FMO2-HF: Total energy	-50840.209486
FMO2-MP2: Total energy	-50991.19155

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:MET)

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

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.
-14.64	-17.673	15.131	-6.003	-6.095	0.047

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.076 / q_NPA : 0.030

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

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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	PHE	0	0.010	0.004	3.868	-2.804	-0.374	-0.025	-1.141	-1.264	-0.002
4	A	4	LYS	1	0.868	0.923	2.210	-13.692	-19.155	15.156	-4.862	-4.831	0.049
5	A	5	GLU	-1	-0.948	-0.963	5.427	1.412	1.412	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.007	0.008	8.603	-0.071	-0.071	0.000	0.000	0.000	0.000
7	A	7	HIS	0	0.034	0.045	12.023	-0.065	-0.065	0.000	0.000	0.000	0.000
8	A	8	HIS	1	0.812	0.862	14.330	-0.594	-0.594	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.005	0.017	16.687	0.060	0.060	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.022	-0.018	19.097	-0.031	-0.031	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.004	0.002	22.296	0.008	0.008	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.028	-0.009	25.638	0.005	0.005	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.047	0.024	28.977	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.041	-0.063	31.993	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	15	ASN	0	0.005	-0.003	35.726	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.027	-0.029	35.120	0.003	0.003	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.017	-0.005	36.247	0.007	0.007	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.033	0.015	36.927	0.000	0.000	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.016	0.002	31.187	0.007	0.007	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.844	0.916	32.923	-0.156	-0.156	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.006	0.005	34.621	0.001	0.001	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.056	0.022	29.950	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	23	TYR	0	-0.021	-0.067	26.978	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.056	-0.019	29.970	0.008	0.008	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.965	-0.989	31.892	0.135	0.135	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.838	0.945	34.171	-0.131	-0.131	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.044	-0.030	27.642	0.001	0.001	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.023	0.035	28.722	0.008	0.008	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.069	-0.043	22.886	0.014	0.014	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.897	-0.941	27.049	0.175	0.175	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.031	-0.040	27.484	0.020	0.020	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.064	-0.013	22.737	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.813	0.881	22.576	-0.323	-0.323	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.729	-0.840	28.890	0.170	0.170	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.068	-0.032	29.826	0.001	0.001	0.000	0.000	0.000	0.000
36	A	36	HIS	0	0.009	0.009	32.424	0.003	0.003	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.820	0.896	27.315	-0.232	-0.232	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.023	0.009	34.048	0.001	0.001	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.960	-1.000	34.382	0.133	0.133	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.880	0.930	28.924	-0.202	-0.202	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.021	0.066	34.031	0.008	0.008	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.800	-0.898	31.052	0.209	0.209	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.014	-0.006	32.660	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.757	0.871	23.586	-0.311	-0.311	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.007	-0.011	28.873	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.768	-0.852	23.982	0.331	0.331	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.005	0.003	24.702	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.857	0.913	18.182	-0.410	-0.410	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.059	0.051	22.367	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.047	0.025	20.430	0.029	0.029	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.039	-0.031	15.111	-0.013	-0.013	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.026	0.014	16.855	0.078	0.078	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.852	-0.937	18.319	0.386	0.386	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.003	0.005	19.643	0.044	0.044	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.835	-0.889	22.247	0.375	0.375	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.035	0.010	23.800	0.006	0.006	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.045	-0.017	24.216	-0.012	-0.012	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.025	-0.014	29.237	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	59	SER	0	0.018	-0.016	32.857	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.867	-0.913	35.475	0.136	0.136	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.039	-0.034	35.991	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	62	PHE	0	-0.088	-0.036	30.891	0.004	0.004	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.002	0.007	34.360	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.011	-0.001	34.595	0.009	0.009	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.836	0.900	27.462	-0.229	-0.229	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.022	-0.016	31.022	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.010	-0.007	32.250	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.049	0.006	34.359	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.003	0.001	32.846	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.802	-0.911	28.899	0.227	0.227	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.014	0.002	29.264	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.015	-0.021	24.829	0.014	0.014	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.003	0.009	22.367	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.018	-0.014	18.430	0.011	0.011	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.965	1.000	22.318	-0.272	-0.272	0.000	0.000	0.000	0.000
76	A	76	HIS	0	-0.015	-0.002	22.373	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.017	0.022	19.528	0.046	0.046	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.022	0.017	20.774	-0.033	-0.033	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.014	-0.011	20.667	0.039	0.039	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.928	0.962	18.881	-0.197	-0.197	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.010	-0.001	21.899	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-1.017	-1.011	23.466	0.114	0.114	0.000	0.000	0.000	0.000
83	A	83	HIS	0	0.029	0.010	25.813	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.002	-0.013	28.666	0.004	0.004	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.817	-0.897	30.481	0.094	0.094	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.948	-0.971	30.808	0.099	0.099	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.015	0.011	28.398	0.003	0.003	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.008	-0.006	31.818	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.037	-0.009	34.417	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.001	0.004	32.127	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.022	0.005	31.147	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	ASN	0	0.019	0.002	35.481	0.001	0.001	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.970	-0.965	38.764	0.090	0.090	0.000	0.000	0.000	0.000
94	A	94	GLN	0	-0.062	-0.031	36.324	0.000	0.000	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.040	-0.020	39.168	0.003	0.003	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.090	-0.041	33.801	0.003	0.003	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.919	-0.957	37.160	0.106	0.106	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.036	-0.029	33.456	0.008	0.008	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.817	-0.891	33.317	0.143	0.143	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.016	-0.002	35.712	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.020	0.002	32.338	0.006	0.006	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.821	0.894	31.729	-0.151	-0.151	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.010	-0.014	30.744	0.004	0.004	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.796	-0.892	24.643	0.180	0.180	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.911	-0.956	28.314	0.121	0.121	0.000	0.000	0.000	0.000
106	A	106	PHE	0	-0.047	-0.027	25.188	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.105	-0.064	22.684	-0.014	-0.014	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.011	0.014	25.821	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.888	0.949	21.721	-0.117	-0.117	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.807	0.882	27.660	-0.084	-0.084	0.000	0.000	0.000	0.000
111	A	111	MET	0	-0.021	-0.003	26.423	0.010	0.010	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.010	-0.029	29.047	-0.012	-0.012	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.004	0.008	26.725	0.019	0.019	0.000	0.000	0.000	0.000
114	A	114	PHE	0	0.043	0.022	28.123	-0.015	-0.015	0.000	0.000	0.000	0.000
115	A	115	PHE	0	-0.020	-0.015	30.786	0.014	0.014	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.774	-0.859	30.017	0.208	0.208	0.000	0.000	0.000	0.000
117	A	117	PRO	0	-0.017	-0.017	32.162	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.817	-0.855	32.765	0.164	0.164	0.000	0.000	0.000	0.000
119	A	119	GLY	0	-0.024	-0.014	33.697	0.001	0.001	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.040	-0.021	25.671	0.006	0.006	0.000	0.000	0.000	0.000
121	A	121	PRO	0	-0.012	-0.008	27.835	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.025	-0.008	25.472	0.029	0.029	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.832	-0.934	24.210	0.239	0.239	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.002	0.011	25.315	0.017	0.017	0.000	0.000	0.000	0.000
125	A	125	HIS	1	0.873	0.905	23.207	-0.217	-0.217	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.824	-0.877	23.441	0.127	0.127	0.000	0.000	0.000	0.000

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