FMO DATABASE

FMODB ID: 9G752

Calculation Name: 2WP7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2WP7

Chain ID: A

ChEMBL ID:

UniProt ID: Q9CQT7

Base Structure: X-ray

Registration Date: 2023-03-14

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	158
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1484138.729593
FMO2-HF: Nuclear repulsion	1423934.192192
FMO2-HF: Total energy	-60204.537401
FMO2-MP2: Total energy	-60382.467636

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:PRO)

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

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.
-9.199	-3.682	1.561	-2.906	-4.172	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.047 / q_NPA : 0.017

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	LEU	0	0.001	0.007	2.946	-2.585	0.179	0.088	-1.114	-1.738	0.005
4	A	7	TYR	0	-0.030	-0.025	5.495	0.807	0.807	0.000	0.000	0.000	0.000
5	A	8	PRO	0	0.005	0.006	8.787	0.002	0.002	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.026	0.012	11.242	0.089	0.089	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.801	0.889	13.810	0.611	0.611	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.034	0.025	17.537	0.010	0.010	0.000	0.000	0.000	0.000
9	A	12	TYR	0	-0.050	-0.025	20.542	0.019	0.019	0.000	0.000	0.000	0.000
10	A	13	VAL	0	0.012	-0.005	23.565	0.010	0.010	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.032	-0.053	26.321	0.012	0.012	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.743	-0.840	30.127	-0.147	-0.147	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.010	-0.005	32.939	0.009	0.009	0.000	0.000	0.000	0.000
14	A	17	SER	0	-0.089	-0.058	35.422	0.010	0.010	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.919	0.950	34.135	0.158	0.158	0.000	0.000	0.000	0.000
16	A	19	GLY	0	-0.036	-0.024	37.793	0.006	0.006	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.039	-0.037	39.391	0.005	0.005	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.038	0.013	38.926	0.005	0.005	0.000	0.000	0.000	0.000
19	A	22	ARG	1	0.993	1.014	37.989	0.130	0.130	0.000	0.000	0.000	0.000
20	A	23	ARG	1	0.917	0.960	40.851	0.102	0.102	0.000	0.000	0.000	0.000
21	A	24	LEU	0	0.021	0.002	44.531	0.004	0.004	0.000	0.000	0.000	0.000
22	A	25	SER	0	0.092	0.061	41.972	0.002	0.002	0.000	0.000	0.000	0.000
23	A	26	PRO	0	-0.041	-0.022	44.158	0.003	0.003	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.032	-0.009	46.578	0.003	0.003	0.000	0.000	0.000	0.000
25	A	28	MET	0	-0.065	-0.012	46.071	0.002	0.002	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.009	-0.014	42.038	0.002	0.002	0.000	0.000	0.000	0.000
27	A	30	GLY	0	-0.020	0.016	46.249	0.001	0.001	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.874	0.927	41.111	0.114	0.114	0.000	0.000	0.000	0.000
29	A	32	GLN	0	-0.091	-0.063	40.330	0.006	0.006	0.000	0.000	0.000	0.000
30	A	33	LEU	0	0.027	0.026	37.722	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.888	-0.975	34.924	-0.134	-0.134	0.000	0.000	0.000	0.000
32	A	35	GLY	0	-0.035	-0.015	35.143	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	36	ILE	0	-0.047	-0.017	35.099	0.000	0.000	0.000	0.000	0.000	0.000
34	A	37	TRP	0	0.015	-0.007	29.689	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	38	HIS	0	0.062	0.032	28.332	0.003	0.003	0.000	0.000	0.000	0.000
36	A	39	THR	0	-0.041	-0.063	24.331	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	40	SER	0	-0.021	-0.032	23.359	0.004	0.004	0.000	0.000	0.000	0.000
38	A	41	ILE	0	0.029	0.018	16.647	-0.024	-0.024	0.000	0.000	0.000	0.000
39	A	42	VAL	0	-0.014	-0.004	17.879	0.025	0.025	0.000	0.000	0.000	0.000
40	A	43	VAL	0	-0.001	-0.007	12.294	-0.080	-0.080	0.000	0.000	0.000	0.000
41	A	44	HIS	1	0.818	0.910	9.626	0.789	0.789	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.898	0.944	14.411	0.434	0.434	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.823	-0.881	17.724	-0.218	-0.218	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.771	-0.845	18.970	-0.292	-0.292	0.000	0.000	0.000	0.000
45	A	48	PHE	0	0.021	0.003	17.516	0.026	0.026	0.000	0.000	0.000	0.000
46	A	49	PHE	0	-0.006	-0.026	21.860	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	50	PHE	0	-0.022	0.008	24.679	0.007	0.007	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.062	0.017	27.049	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	52	SER	0	0.004	0.015	30.814	0.001	0.001	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.072	-0.042	31.904	0.009	0.009	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.018	0.009	29.614	0.005	0.005	0.000	0.000	0.000	0.000
52	A	55	ILE	0	-0.010	-0.004	22.703	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	56	SER	0	-0.054	-0.024	25.790	0.020	0.020	0.000	0.000	0.000	0.000
54	A	57	SER	0	-0.014	0.002	22.476	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	58	CYS	0	0.002	-0.008	23.891	0.024	0.024	0.000	0.000	0.000	0.000
56	A	59	THR	0	0.050	0.033	23.597	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	60	PRO	0	-0.011	-0.022	21.128	0.008	0.008	0.000	0.000	0.000	0.000
58	A	61	GLY	0	-0.028	-0.012	23.916	0.011	0.011	0.000	0.000	0.000	0.000
59	A	62	GLY	0	-0.045	-0.008	26.982	0.016	0.016	0.000	0.000	0.000	0.000
60	A	63	THR	0	0.027	0.024	28.410	0.014	0.014	0.000	0.000	0.000	0.000
61	A	64	LEU	0	-0.031	-0.023	30.918	0.003	0.003	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.050	-0.030	30.558	0.006	0.006	0.000	0.000	0.000	0.000
63	A	66	GLY	0	-0.022	0.011	32.409	0.001	0.001	0.000	0.000	0.000	0.000
64	A	67	PRO	0	-0.010	-0.024	29.169	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	68	PRO	0	-0.021	0.005	25.401	0.008	0.008	0.000	0.000	0.000	0.000
66	A	69	ASP	-1	-0.848	-0.919	28.527	-0.168	-0.168	0.000	0.000	0.000	0.000
67	A	70	SER	0	-0.049	-0.030	26.309	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	71	VAL	0	0.009	0.017	20.810	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	72	VAL	0	0.009	0.001	20.162	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	73	ASP	-1	-0.896	-0.940	15.100	-0.754	-0.754	0.000	0.000	0.000	0.000
71	A	74	VAL	0	0.008	0.021	14.894	0.025	0.025	0.000	0.000	0.000	0.000
72	A	75	GLY	0	0.038	0.007	12.261	0.001	0.001	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.037	-0.012	7.332	0.164	0.164	0.000	0.000	0.000	0.000
74	A	77	THR	0	0.012	-0.004	7.596	0.008	0.008	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.911	-0.969	2.251	-8.059	-5.364	1.474	-1.790	-2.379	-0.014
76	A	79	VAL	0	-0.021	0.009	4.844	0.419	0.477	-0.001	-0.002	-0.055	0.000
77	A	80	THR	0	0.034	0.003	7.708	-0.051	-0.051	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.864	-0.959	9.526	-0.348	-0.348	0.000	0.000	0.000	0.000
79	A	82	GLU	-1	-0.935	-0.974	13.148	0.025	0.025	0.000	0.000	0.000	0.000
80	A	83	ILE	0	0.050	0.037	9.739	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	84	PHE	0	-0.034	-0.024	12.874	-0.023	-0.023	0.000	0.000	0.000	0.000
82	A	85	LEU	0	0.025	0.009	14.330	0.025	0.025	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.926	-0.953	16.621	-0.085	-0.085	0.000	0.000	0.000	0.000
84	A	87	TYR	0	-0.019	-0.013	15.644	0.002	0.002	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.012	-0.019	17.627	0.019	0.019	0.000	0.000	0.000	0.000
86	A	89	SER	0	0.000	0.008	20.040	0.022	0.022	0.000	0.000	0.000	0.000
87	A	90	SER	0	-0.016	-0.003	20.664	0.017	0.017	0.000	0.000	0.000	0.000
88	A	91	LEU	0	-0.014	0.000	20.047	0.012	0.012	0.000	0.000	0.000	0.000
89	A	92	GLY	0	-0.016	-0.002	23.317	0.011	0.011	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.953	-0.977	25.733	-0.088	-0.088	0.000	0.000	0.000	0.000
91	A	94	SER	0	-0.085	-0.058	25.078	0.008	0.008	0.000	0.000	0.000	0.000
92	A	95	LEU	0	-0.001	-0.005	25.428	0.009	0.009	0.000	0.000	0.000	0.000
93	A	96	PHE	0	0.008	0.014	24.082	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.953	0.996	27.612	0.100	0.100	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.022	-0.008	30.388	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-1.004	-1.015	32.580	-0.110	-0.110	0.000	0.000	0.000	0.000
97	A	100	ALA	0	0.041	0.046	31.103	0.003	0.003	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.043	-0.012	31.358	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	102	ASN	0	0.036	0.011	33.031	0.004	0.004	0.000	0.000	0.000	0.000
100	A	103	LEU	0	-0.015	-0.013	33.704	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	104	PHE	0	-0.060	-0.042	34.452	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.959	-0.988	32.746	-0.132	-0.132	0.000	0.000	0.000	0.000
103	A	106	HIS	0	-0.028	-0.010	28.431	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	107	ASN	0	0.039	0.019	29.480	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	108	CYS	0	0.014	0.009	27.410	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.005	0.001	25.626	-0.032	-0.032	0.000	0.000	0.000	0.000
107	A	110	THR	0	0.033	0.037	24.967	-0.021	-0.021	0.000	0.000	0.000	0.000
108	A	111	PHE	0	0.041	0.029	21.092	-0.020	-0.020	0.000	0.000	0.000	0.000
109	A	112	SER	0	0.011	-0.004	21.035	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	113	ASN	0	0.015	0.017	19.959	-0.070	-0.070	0.000	0.000	0.000	0.000
111	A	114	GLU	-1	-0.892	-0.949	19.829	-0.287	-0.287	0.000	0.000	0.000	0.000
112	A	115	VAL	0	0.019	0.015	16.521	-0.040	-0.040	0.000	0.000	0.000	0.000
113	A	116	ALA	0	-0.020	-0.013	15.708	-0.077	-0.077	0.000	0.000	0.000	0.000
114	A	117	GLN	0	-0.024	-0.017	14.856	-0.074	-0.074	0.000	0.000	0.000	0.000
115	A	118	PHE	0	-0.019	0.011	13.224	-0.069	-0.069	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.025	-0.002	11.186	-0.094	-0.094	0.000	0.000	0.000	0.000
117	A	120	THR	0	-0.031	-0.027	10.033	-0.203	-0.203	0.000	0.000	0.000	0.000
118	A	121	GLY	0	0.007	0.016	11.867	-0.027	-0.027	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.806	0.897	12.368	0.877	0.877	0.000	0.000	0.000	0.000
120	A	123	LYS	1	0.990	1.010	16.796	0.291	0.291	0.000	0.000	0.000	0.000
121	A	124	ILE	0	-0.020	-0.016	20.219	-0.018	-0.018	0.000	0.000	0.000	0.000
122	A	125	PRO	0	-0.022	-0.034	21.960	0.018	0.018	0.000	0.000	0.000	0.000
123	A	126	SER	0	0.065	0.029	24.973	0.003	0.003	0.000	0.000	0.000	0.000
124	A	127	TYR	0	0.005	0.014	26.855	0.003	0.003	0.000	0.000	0.000	0.000
125	A	128	ILE	0	-0.048	-0.010	25.648	0.011	0.011	0.000	0.000	0.000	0.000
126	A	129	THR	0	-0.004	-0.024	25.883	0.005	0.005	0.000	0.000	0.000	0.000
127	A	130	ASP	-1	-0.870	-0.928	29.025	-0.182	-0.182	0.000	0.000	0.000	0.000
128	A	131	LEU	0	0.013	0.031	32.252	0.013	0.013	0.000	0.000	0.000	0.000
129	A	132	PRO	0	0.025	0.006	32.852	0.012	0.012	0.000	0.000	0.000	0.000
130	A	133	SER	0	-0.003	-0.009	35.320	0.011	0.011	0.000	0.000	0.000	0.000
131	A	134	GLU	-1	-0.927	-0.968	34.938	-0.146	-0.146	0.000	0.000	0.000	0.000
132	A	135	VAL	0	-0.005	-0.006	38.494	0.009	0.009	0.000	0.000	0.000	0.000
133	A	136	LEU	0	0.033	0.028	38.619	0.008	0.008	0.000	0.000	0.000	0.000
134	A	137	SER	0	-0.091	-0.007	40.794	0.008	0.008	0.000	0.000	0.000	0.000
135	A	138	THR	0	-0.016	-0.031	43.061	0.003	0.003	0.000	0.000	0.000	0.000
136	A	139	PRO	0	0.035	0.003	45.854	0.000	0.000	0.000	0.000	0.000	0.000
137	A	140	PHE	0	0.038	0.024	43.929	0.002	0.002	0.000	0.000	0.000	0.000
138	A	141	GLY	0	0.041	0.015	44.072	0.001	0.001	0.000	0.000	0.000	0.000
139	A	142	GLN	0	-0.090	-0.071	44.256	0.003	0.003	0.000	0.000	0.000	0.000
140	A	143	ALA	0	-0.036	-0.008	47.105	0.002	0.002	0.000	0.000	0.000	0.000
141	A	144	LEU	0	-0.019	-0.012	45.866	0.003	0.003	0.000	0.000	0.000	0.000
142	A	145	ARG	1	0.981	1.024	41.819	0.093	0.093	0.000	0.000	0.000	0.000
143	A	146	PRO	0	0.034	0.006	44.047	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	147	PHE	0	0.004	0.004	45.267	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	148	LEU	0	0.007	-0.013	41.032	-0.002	-0.002	0.000	0.000	0.000	0.000
146	A	149	ASP	-1	-0.850	-0.937	40.178	-0.108	-0.108	0.000	0.000	0.000	0.000
147	A	150	SER	0	-0.106	-0.048	40.879	0.001	0.001	0.000	0.000	0.000	0.000
148	A	151	ILE	0	-0.097	-0.037	38.297	0.001	0.001	0.000	0.000	0.000	0.000
149	A	152	GLN	0	0.005	0.001	36.721	-0.008	-0.008	0.000	0.000	0.000	0.000
150	A	153	ILE	0	-0.019	-0.014	33.297	0.004	0.004	0.000	0.000	0.000	0.000
151	A	154	GLN	0	0.051	0.025	30.466	-0.008	-0.008	0.000	0.000	0.000	0.000
152	A	155	PRO	0	-0.024	0.000	31.031	0.009	0.009	0.000	0.000	0.000	0.000
153	A	156	PRO	0	-0.003	-0.004	32.203	-0.003	-0.003	0.000	0.000	0.000	0.000
154	A	157	GLY	0	0.042	-0.001	31.941	-0.005	-0.005	0.000	0.000	0.000	0.000
155	A	158	GLY	0	0.004	0.024	28.716	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	159	ASN	0	-0.073	-0.037	26.944	0.006	0.006	0.000	0.000	0.000	0.000
157	A	160	SER	0	0.033	0.005	27.104	-0.010	-0.010	0.000	0.000	0.000	0.000
158	A	161	VAL	0	0.010	0.026	21.718	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:PRO)