FMO DATABASE

FMODB ID: QY2KY

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	OptH
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	-1082015.475373
FMO2-HF: Nuclear repulsion	1031175.939343
FMO2-HF: Total energy	-50839.536031
FMO2-MP2: Total energy	-50990.538878

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.
-15.907	-20.082	17.289	-6.858	-6.257	0.059

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 : 0.086 / q_NPA : 0.036

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	0.009	0.005	3.866	-2.868	-0.489	-0.026	-1.098	-1.256	-0.002
4	A	4	LYS	1	0.860	0.918	2.151	-14.769	-21.411	17.316	-5.759	-4.915	0.061
5	A	5	GLU	-1	-0.950	-0.964	5.347	1.277	1.365	-0.001	-0.001	-0.086	0.000
6	A	6	ILE	0	-0.005	0.004	8.510	-0.087	-0.087	0.000	0.000	0.000	0.000
7	A	7	HIS	0	0.028	0.053	11.942	-0.048	-0.048	0.000	0.000	0.000	0.000
8	A	8	HIS	1	0.899	0.915	14.249	-0.590	-0.590	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.003	0.015	16.621	0.055	0.055	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.025	-0.020	19.030	-0.028	-0.028	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.001	0.006	22.237	0.006	0.006	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.032	-0.012	25.580	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.041	0.023	28.925	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.036	-0.052	31.934	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	15	ASN	0	0.010	0.000	35.668	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.032	-0.038	34.809	0.002	0.002	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.007	-0.011	36.169	0.006	0.006	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.048	0.021	36.784	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.018	0.005	31.094	0.007	0.007	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.891	0.953	32.840	-0.158	-0.158	0.000	0.000	0.000	0.000
21	A	21	ASN	0	-0.004	0.004	34.532	0.002	0.002	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.067	0.023	29.771	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	23	TYR	0	-0.022	-0.057	27.001	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.055	-0.023	29.877	0.009	0.009	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.970	-0.990	31.798	0.140	0.140	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.851	0.960	33.956	-0.136	-0.136	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.031	-0.029	27.659	0.001	0.001	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.019	0.034	28.905	0.009	0.009	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.071	-0.039	22.802	0.014	0.014	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.901	-0.946	27.179	0.189	0.189	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.034	-0.037	27.485	0.020	0.020	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.060	-0.011	22.599	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.841	0.902	22.675	-0.322	-0.322	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.767	-0.863	28.689	0.172	0.172	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.061	-0.033	30.041	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	HIS	0	-0.009	0.002	32.375	0.003	0.003	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.832	0.900	27.477	-0.231	-0.231	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.020	0.014	34.010	0.000	0.000	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.964	-1.009	34.378	0.131	0.131	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.858	0.923	28.564	-0.208	-0.208	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.033	0.069	34.002	0.009	0.009	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.796	-0.898	31.186	0.205	0.205	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.011	-0.005	32.535	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.805	0.924	23.773	-0.307	-0.307	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.006	-0.012	28.808	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.809	-0.894	24.107	0.337	0.337	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.006	-0.003	24.604	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.935	0.976	18.635	-0.413	-0.413	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.061	0.045	22.420	-0.025	-0.025	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.051	0.030	20.836	0.031	0.031	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.071	-0.056	15.218	-0.023	-0.023	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.025	0.003	17.016	0.072	0.072	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.928	-0.969	18.222	0.401	0.401	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.003	-0.005	19.558	0.040	0.040	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.883	-0.937	22.098	0.367	0.367	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.025	0.003	23.728	0.004	0.004	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.072	-0.029	24.155	-0.012	-0.012	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.016	-0.009	29.178	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	59	SER	0	0.024	-0.015	32.796	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.880	-0.936	35.423	0.134	0.134	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.032	-0.019	36.050	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	62	PHE	0	-0.090	-0.033	30.844	0.003	0.003	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.002	0.009	34.369	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.015	-0.001	34.558	0.009	0.009	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.860	0.931	27.334	-0.222	-0.222	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.026	-0.016	30.984	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.013	-0.006	32.222	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.046	0.007	34.333	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.000	-0.002	32.930	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.822	-0.932	28.527	0.221	0.221	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.015	0.000	29.271	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.019	-0.022	24.667	0.014	0.014	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.000	0.007	22.422	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.017	-0.016	18.367	0.009	0.009	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.966	1.003	22.290	-0.258	-0.258	0.000	0.000	0.000	0.000
76	A	76	HIS	0	0.023	0.005	22.659	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.012	0.027	19.522	0.044	0.044	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.031	0.016	20.709	-0.032	-0.032	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.020	-0.010	20.592	0.041	0.041	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.911	0.952	18.744	-0.214	-0.214	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.012	0.002	21.942	0.002	0.002	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-1.013	-1.010	23.881	0.127	0.127	0.000	0.000	0.000	0.000
83	A	83	HIS	0	0.040	0.017	25.834	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.001	-0.017	28.762	0.005	0.005	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.830	-0.909	30.489	0.093	0.093	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.941	-0.969	30.579	0.108	0.108	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.011	0.010	28.512	0.003	0.003	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.008	-0.006	31.934	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.036	-0.007	34.501	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.003	0.005	32.651	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.012	-0.002	31.107	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	ASN	0	0.032	0.007	35.441	0.002	0.002	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.994	-0.982	38.848	0.091	0.091	0.000	0.000	0.000	0.000
94	A	94	GLN	0	-0.046	-0.020	36.213	0.001	0.001	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.034	-0.024	39.088	0.003	0.003	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.097	-0.044	33.680	0.003	0.003	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.921	-0.959	37.080	0.105	0.105	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.043	-0.028	33.388	0.008	0.008	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.847	-0.929	33.364	0.138	0.138	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.011	0.004	35.648	0.000	0.000	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.019	0.001	32.419	0.006	0.006	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.855	0.937	31.328	-0.147	-0.147	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.024	-0.022	30.699	0.004	0.004	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.813	-0.912	24.594	0.178	0.178	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.905	-0.940	28.273	0.110	0.110	0.000	0.000	0.000	0.000
106	A	106	PHE	0	-0.046	-0.033	25.166	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.082	-0.047	22.682	-0.012	-0.012	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.012	0.015	25.732	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.900	0.954	21.684	-0.110	-0.110	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.896	0.942	27.503	-0.077	-0.077	0.000	0.000	0.000	0.000
111	A	111	MET	0	-0.018	0.000	26.162	0.008	0.008	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.014	-0.036	28.983	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.006	0.007	26.677	0.017	0.017	0.000	0.000	0.000	0.000
114	A	114	PHE	0	0.044	0.023	28.250	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	115	PHE	0	-0.024	-0.013	30.722	0.013	0.013	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.778	-0.860	29.943	0.207	0.207	0.000	0.000	0.000	0.000
117	A	117	PRO	0	-0.015	-0.021	32.092	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.814	-0.863	32.681	0.164	0.164	0.000	0.000	0.000	0.000
119	A	119	GLY	0	-0.030	-0.020	33.642	0.000	0.000	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.049	-0.024	25.591	0.005	0.005	0.000	0.000	0.000	0.000
121	A	121	PRO	0	-0.011	-0.008	27.755	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.024	-0.010	25.446	0.029	0.029	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.843	-0.939	24.223	0.232	0.232	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.007	0.009	25.242	0.018	0.018	0.000	0.000	0.000	0.000
125	A	125	HIS	1	0.861	0.898	23.095	-0.214	-0.214	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.920	-0.932	22.300	0.125	0.125	0.000	0.000	0.000	0.000

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