FMO DATABASE

FMODB ID: M38KZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1485093.691762
FMO2-HF: Nuclear repulsion	1424888.529919
FMO2-HF: Total energy	-60205.161843
FMO2-MP2: Total energy	-60383.044246

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.
-11.03	-5.658	2.097	-3.145	-4.323	-0.017

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 : 0.028 / q_NPA : 0.003

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	0.008	0.009	3.583	-2.251	-0.055	0.006	-0.868	-1.334	0.004
4	A	7	TYR	0	-0.033	-0.025	5.425	0.839	0.839	0.000	0.000	0.000	0.000
5	A	8	PRO	0	0.007	0.003	8.748	-0.022	-0.022	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.014	0.009	11.162	0.087	0.087	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.823	0.895	13.757	0.585	0.585	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.031	0.023	17.478	0.007	0.007	0.000	0.000	0.000	0.000
9	A	12	TYR	0	-0.041	-0.019	20.489	0.008	0.008	0.000	0.000	0.000	0.000
10	A	13	VAL	0	0.005	-0.009	23.517	0.008	0.008	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.023	-0.049	26.243	0.016	0.016	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.770	-0.851	30.079	-0.145	-0.145	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.024	-0.001	32.868	0.010	0.010	0.000	0.000	0.000	0.000
14	A	17	SER	0	-0.084	-0.054	35.383	0.011	0.011	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.863	0.911	33.302	0.157	0.157	0.000	0.000	0.000	0.000
16	A	19	GLY	0	-0.038	-0.026	37.741	0.006	0.006	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.026	-0.023	39.362	0.004	0.004	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.036	0.014	38.875	0.004	0.004	0.000	0.000	0.000	0.000
19	A	22	ARG	1	0.948	1.003	37.546	0.129	0.129	0.000	0.000	0.000	0.000
20	A	23	ARG	1	0.940	0.964	40.919	0.096	0.096	0.000	0.000	0.000	0.000
21	A	24	LEU	0	0.019	0.004	44.490	0.004	0.004	0.000	0.000	0.000	0.000
22	A	25	SER	0	0.057	0.043	41.841	0.002	0.002	0.000	0.000	0.000	0.000
23	A	26	PRO	0	-0.006	-0.008	44.095	0.003	0.003	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.050	-0.024	46.633	0.003	0.003	0.000	0.000	0.000	0.000
25	A	28	MET	0	-0.062	-0.011	45.859	0.003	0.003	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.008	-0.012	41.976	0.001	0.001	0.000	0.000	0.000	0.000
27	A	30	GLY	0	-0.026	0.012	46.193	0.000	0.000	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.786	0.866	40.147	0.125	0.125	0.000	0.000	0.000	0.000
29	A	32	GLN	0	-0.102	-0.058	40.547	0.006	0.006	0.000	0.000	0.000	0.000
30	A	33	LEU	0	0.025	0.017	37.564	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.841	-0.950	35.174	-0.131	-0.131	0.000	0.000	0.000	0.000
32	A	35	GLY	0	-0.033	-0.016	35.078	0.001	0.001	0.000	0.000	0.000	0.000
33	A	36	ILE	0	-0.045	-0.019	35.100	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	37	TRP	0	0.003	-0.009	29.655	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	38	HIS	0	0.060	0.046	28.104	0.004	0.004	0.000	0.000	0.000	0.000
36	A	39	THR	0	-0.043	-0.053	24.282	-0.011	-0.011	0.000	0.000	0.000	0.000
37	A	40	SER	0	-0.018	-0.033	23.339	0.006	0.006	0.000	0.000	0.000	0.000
38	A	41	ILE	0	0.016	0.013	16.735	-0.023	-0.023	0.000	0.000	0.000	0.000
39	A	42	VAL	0	-0.010	-0.002	17.961	0.027	0.027	0.000	0.000	0.000	0.000
40	A	43	VAL	0	-0.002	-0.006	12.327	-0.077	-0.077	0.000	0.000	0.000	0.000
41	A	44	HIS	1	0.831	0.931	9.577	0.765	0.765	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.896	0.943	14.427	0.336	0.336	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.814	-0.888	17.737	-0.175	-0.175	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.779	-0.841	18.973	-0.281	-0.281	0.000	0.000	0.000	0.000
45	A	48	PHE	0	0.026	0.006	17.886	0.023	0.023	0.000	0.000	0.000	0.000
46	A	49	PHE	0	-0.007	-0.024	21.874	-0.017	-0.017	0.000	0.000	0.000	0.000
47	A	50	PHE	0	-0.027	0.004	24.689	0.007	0.007	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.067	0.018	27.068	0.000	0.000	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.004	0.007	30.833	0.000	0.000	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.065	-0.037	32.060	0.009	0.009	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.015	0.008	29.654	0.004	0.004	0.000	0.000	0.000	0.000
52	A	55	ILE	0	-0.015	-0.006	22.708	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	56	SER	0	-0.044	-0.018	25.824	0.021	0.021	0.000	0.000	0.000	0.000
54	A	57	SER	0	-0.010	0.000	22.533	-0.022	-0.022	0.000	0.000	0.000	0.000
55	A	58	CYS	0	-0.010	-0.016	23.908	0.022	0.022	0.000	0.000	0.000	0.000
56	A	59	THR	0	0.070	0.050	23.610	-0.015	-0.015	0.000	0.000	0.000	0.000
57	A	60	PRO	0	-0.016	-0.030	21.133	0.005	0.005	0.000	0.000	0.000	0.000
58	A	61	GLY	0	-0.032	-0.014	23.901	0.013	0.013	0.000	0.000	0.000	0.000
59	A	62	GLY	0	-0.052	-0.010	26.975	0.015	0.015	0.000	0.000	0.000	0.000
60	A	63	THR	0	0.022	0.020	28.367	0.013	0.013	0.000	0.000	0.000	0.000
61	A	64	LEU	0	-0.032	-0.024	30.915	0.004	0.004	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.041	-0.021	30.502	0.006	0.006	0.000	0.000	0.000	0.000
63	A	66	GLY	0	-0.017	0.013	32.384	0.002	0.002	0.000	0.000	0.000	0.000
64	A	67	PRO	0	-0.007	-0.022	29.129	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	68	PRO	0	-0.022	0.012	25.352	0.006	0.006	0.000	0.000	0.000	0.000
66	A	69	ASP	-1	-0.827	-0.907	28.476	-0.157	-0.157	0.000	0.000	0.000	0.000
67	A	70	SER	0	-0.038	-0.024	26.544	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	71	VAL	0	0.009	0.019	20.920	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	72	VAL	0	0.001	-0.004	20.555	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	73	ASP	-1	-0.896	-0.932	15.309	-0.722	-0.722	0.000	0.000	0.000	0.000
71	A	74	VAL	0	0.008	0.018	15.142	0.020	0.020	0.000	0.000	0.000	0.000
72	A	75	GLY	0	0.047	0.020	12.565	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.052	-0.021	7.610	0.150	0.150	0.000	0.000	0.000	0.000
74	A	77	THR	0	0.013	-0.006	7.553	-0.020	-0.020	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.890	-0.960	2.476	-10.019	-6.899	2.092	-2.275	-2.936	-0.021
76	A	79	VAL	0	-0.031	0.001	4.874	0.430	0.486	-0.001	-0.002	-0.053	0.000
77	A	80	THR	0	0.040	-0.003	7.909	-0.025	-0.025	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.840	-0.952	9.617	-0.342	-0.342	0.000	0.000	0.000	0.000
79	A	82	GLU	-1	-0.944	-0.969	13.042	0.016	0.016	0.000	0.000	0.000	0.000
80	A	83	ILE	0	0.045	0.026	9.950	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	84	PHE	0	-0.037	-0.025	12.870	-0.030	-0.030	0.000	0.000	0.000	0.000
82	A	85	LEU	0	0.018	0.009	14.406	0.023	0.023	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.918	-0.950	16.732	-0.127	-0.127	0.000	0.000	0.000	0.000
84	A	87	TYR	0	-0.014	-0.012	15.812	0.000	0.000	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.021	-0.019	17.708	0.020	0.020	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.020	-0.012	20.106	0.022	0.022	0.000	0.000	0.000	0.000
87	A	90	SER	0	-0.010	0.005	20.794	0.010	0.010	0.000	0.000	0.000	0.000
88	A	91	LEU	0	-0.007	0.007	20.211	0.013	0.013	0.000	0.000	0.000	0.000
89	A	92	GLY	0	-0.018	-0.007	23.380	0.013	0.013	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.924	-0.954	25.629	-0.115	-0.115	0.000	0.000	0.000	0.000
91	A	94	SER	0	-0.088	-0.068	25.182	0.008	0.008	0.000	0.000	0.000	0.000
92	A	95	LEU	0	-0.007	-0.004	25.397	0.010	0.010	0.000	0.000	0.000	0.000
93	A	96	PHE	0	-0.016	-0.002	24.149	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.909	0.983	27.657	0.120	0.120	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.023	-0.005	30.443	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.944	-0.997	32.625	-0.120	-0.120	0.000	0.000	0.000	0.000
97	A	100	ALA	0	0.026	0.034	31.139	0.003	0.003	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.033	-0.004	31.131	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	102	ASN	0	0.019	-0.007	33.042	0.006	0.006	0.000	0.000	0.000	0.000
100	A	103	LEU	0	-0.002	-0.002	33.704	-0.010	-0.010	0.000	0.000	0.000	0.000
101	A	104	PHE	0	-0.055	-0.040	34.438	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.920	-0.975	32.745	-0.143	-0.143	0.000	0.000	0.000	0.000
103	A	106	HIS	0	-0.017	0.001	27.693	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	107	ASN	0	0.037	0.015	29.652	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	108	CYS	0	0.017	0.006	27.404	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.001	-0.010	25.616	-0.029	-0.029	0.000	0.000	0.000	0.000
107	A	110	THR	0	0.017	0.030	24.946	-0.022	-0.022	0.000	0.000	0.000	0.000
108	A	111	PHE	0	0.049	0.032	21.252	-0.023	-0.023	0.000	0.000	0.000	0.000
109	A	112	SER	0	0.017	0.001	21.021	-0.035	-0.035	0.000	0.000	0.000	0.000
110	A	113	ASN	0	-0.005	0.003	19.938	-0.064	-0.064	0.000	0.000	0.000	0.000
111	A	114	GLU	-1	-0.881	-0.951	19.807	-0.324	-0.324	0.000	0.000	0.000	0.000
112	A	115	VAL	0	0.014	0.012	16.622	-0.047	-0.047	0.000	0.000	0.000	0.000
113	A	116	ALA	0	-0.019	-0.012	15.705	-0.082	-0.082	0.000	0.000	0.000	0.000
114	A	117	GLN	0	-0.007	-0.003	14.826	-0.076	-0.076	0.000	0.000	0.000	0.000
115	A	118	PHE	0	-0.012	0.009	13.418	-0.084	-0.084	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.028	0.002	11.262	-0.109	-0.109	0.000	0.000	0.000	0.000
117	A	120	THR	0	-0.035	-0.032	10.009	-0.214	-0.214	0.000	0.000	0.000	0.000
118	A	121	GLY	0	0.009	0.017	11.818	-0.033	-0.033	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.797	0.890	13.061	0.900	0.900	0.000	0.000	0.000	0.000
120	A	123	LYS	1	0.983	1.004	16.789	0.308	0.308	0.000	0.000	0.000	0.000
121	A	124	ILE	0	-0.012	-0.009	20.165	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	125	PRO	0	-0.022	-0.031	21.899	0.017	0.017	0.000	0.000	0.000	0.000
123	A	126	SER	0	0.058	0.028	25.090	0.002	0.002	0.000	0.000	0.000	0.000
124	A	127	TYR	0	-0.018	0.007	27.313	0.005	0.005	0.000	0.000	0.000	0.000
125	A	128	ILE	0	-0.051	-0.019	25.481	0.013	0.013	0.000	0.000	0.000	0.000
126	A	129	THR	0	0.007	-0.025	25.906	0.005	0.005	0.000	0.000	0.000	0.000
127	A	130	ASP	-1	-0.848	-0.921	28.981	-0.205	-0.205	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.005	0.020	32.193	0.014	0.014	0.000	0.000	0.000	0.000
129	A	132	PRO	0	0.049	0.020	32.816	0.012	0.012	0.000	0.000	0.000	0.000
130	A	133	SER	0	-0.005	-0.006	35.276	0.010	0.010	0.000	0.000	0.000	0.000
131	A	134	GLU	-1	-0.857	-0.899	35.882	-0.136	-0.136	0.000	0.000	0.000	0.000
132	A	135	VAL	0	0.006	-0.001	38.382	0.009	0.009	0.000	0.000	0.000	0.000
133	A	136	LEU	0	0.032	0.025	38.412	0.008	0.008	0.000	0.000	0.000	0.000
134	A	137	SER	0	-0.098	-0.037	40.452	0.007	0.007	0.000	0.000	0.000	0.000
135	A	138	THR	0	0.000	-0.018	43.017	0.004	0.004	0.000	0.000	0.000	0.000
136	A	139	PRO	0	0.031	0.001	45.807	0.000	0.000	0.000	0.000	0.000	0.000
137	A	140	PHE	0	0.034	0.019	43.721	0.001	0.001	0.000	0.000	0.000	0.000
138	A	141	GLY	0	0.040	0.016	44.038	0.001	0.001	0.000	0.000	0.000	0.000
139	A	142	GLN	0	-0.082	-0.058	44.372	0.003	0.003	0.000	0.000	0.000	0.000
140	A	143	ALA	0	-0.039	-0.008	47.077	0.002	0.002	0.000	0.000	0.000	0.000
141	A	144	LEU	0	-0.021	-0.013	45.876	0.003	0.003	0.000	0.000	0.000	0.000
142	A	145	ARG	1	0.877	0.966	39.657	0.111	0.111	0.000	0.000	0.000	0.000
143	A	146	PRO	0	0.029	0.004	44.040	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	147	PHE	0	0.002	0.005	45.280	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	148	LEU	0	0.009	-0.011	41.069	-0.002	-0.002	0.000	0.000	0.000	0.000
146	A	149	ASP	-1	-0.787	-0.896	39.979	-0.119	-0.119	0.000	0.000	0.000	0.000
147	A	150	SER	0	-0.098	-0.043	40.888	0.001	0.001	0.000	0.000	0.000	0.000
148	A	151	ILE	0	-0.097	-0.036	38.282	0.001	0.001	0.000	0.000	0.000	0.000
149	A	152	GLN	0	-0.013	-0.005	36.434	-0.009	-0.009	0.000	0.000	0.000	0.000
150	A	153	ILE	0	-0.015	-0.015	33.489	0.004	0.004	0.000	0.000	0.000	0.000
151	A	154	GLN	0	0.057	0.026	30.520	-0.010	-0.010	0.000	0.000	0.000	0.000
152	A	155	PRO	0	-0.016	0.006	30.703	0.010	0.010	0.000	0.000	0.000	0.000
153	A	156	PRO	0	-0.004	-0.005	32.215	-0.003	-0.003	0.000	0.000	0.000	0.000
154	A	157	GLY	0	0.036	-0.001	31.954	-0.004	-0.004	0.000	0.000	0.000	0.000
155	A	158	GLY	0	-0.001	0.021	28.744	-0.003	-0.003	0.000	0.000	0.000	0.000
156	A	159	ASN	0	-0.087	-0.040	27.048	0.009	0.009	0.000	0.000	0.000	0.000
157	A	160	SER	0	0.042	0.006	27.154	-0.010	-0.010	0.000	0.000	0.000	0.000
158	A	161	VAL	0	0.012	0.029	21.749	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)