FMO DATABASE

FMODB ID: VQG31

Calculation Name: 2WWE-A-Xray372

Preferred Name: Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2WWE

Chain ID: A

ChEMBL ID: CHEMBL1163120

UniProt ID: O75747

Base Structure: X-ray

Registration Date: 2023-09-23

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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-952229.013358
FMO2-HF: Nuclear repulsion	906264.030461
FMO2-HF: Total energy	-45964.982897
FMO2-MP2: Total energy	-46100.054659

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:-6:ASN)

Summations of interaction energy for fragment #1(A:-6:ASN)

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.
-17.964	-11.617	2.973	-3.716	-5.603	-0.018

Interaction energy analysis for fragmet #1(A:-6:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.032 / q_NPA : -0.023

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	-4	TYR	0	0.009	0.004	2.498	-1.624	0.642	1.728	-1.308	-2.685	0.009
4	A	-3	PHE	0	-0.020	-0.010	6.091	0.652	0.652	0.000	0.000	0.000	0.000
5	A	-2	GLN	0	0.011	0.005	6.849	0.599	0.599	0.000	0.000	0.000	0.000
6	A	-1	SER	0	0.017	0.001	10.011	-0.053	-0.053	0.000	0.000	0.000	0.000
7	A	0	MET	0	0.034	0.002	12.116	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	1203	SER	0	0.008	0.029	9.031	0.021	0.021	0.000	0.000	0.000	0.000
9	A	1204	ILE	0	0.001	0.001	11.017	0.131	0.131	0.000	0.000	0.000	0.000
10	A	1205	GLU	-1	-0.939	-0.962	12.366	-1.088	-1.088	0.000	0.000	0.000	0.000
11	A	1206	ARG	1	0.919	0.955	14.929	0.465	0.465	0.000	0.000	0.000	0.000
12	A	1207	ALA	0	0.028	0.015	18.004	0.043	0.043	0.000	0.000	0.000	0.000
13	A	1208	THR	0	-0.014	-0.006	20.190	-0.016	-0.016	0.000	0.000	0.000	0.000
14	A	1209	ILE	0	-0.046	-0.030	23.896	0.027	0.027	0.000	0.000	0.000	0.000
15	A	1210	LEU	0	-0.024	-0.009	26.911	0.010	0.010	0.000	0.000	0.000	0.000
16	A	1211	GLY	0	0.002	0.002	29.530	0.017	0.017	0.000	0.000	0.000	0.000
17	A	1212	PHE	0	-0.054	-0.016	30.704	-0.013	-0.013	0.000	0.000	0.000	0.000
18	A	1213	SER	0	-0.020	-0.031	30.744	0.013	0.013	0.000	0.000	0.000	0.000
19	A	1214	LYS	1	0.877	0.919	30.589	0.140	0.140	0.000	0.000	0.000	0.000
20	A	1215	LYS	1	0.894	0.943	29.741	0.128	0.128	0.000	0.000	0.000	0.000
21	A	1216	SER	0	0.031	0.004	34.097	0.003	0.003	0.000	0.000	0.000	0.000
22	A	1217	SER	0	0.028	0.022	33.967	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	1218	ASN	0	-0.032	-0.011	33.586	-0.013	-0.013	0.000	0.000	0.000	0.000
24	A	1219	LEU	0	-0.050	-0.022	28.687	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	1220	TYR	0	0.013	-0.001	27.228	0.014	0.014	0.000	0.000	0.000	0.000
26	A	1221	LEU	0	-0.017	-0.008	27.297	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	1222	ILE	0	-0.016	-0.009	21.765	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	1223	GLN	0	0.025	0.008	23.433	0.007	0.007	0.000	0.000	0.000	0.000
29	A	1224	VAL	0	-0.006	-0.004	17.251	-0.048	-0.048	0.000	0.000	0.000	0.000
30	A	1225	THR	0	-0.031	-0.016	19.045	0.058	0.058	0.000	0.000	0.000	0.000
31	A	1226	HIS	0	0.017	-0.002	14.651	-0.068	-0.068	0.000	0.000	0.000	0.000
32	A	1227	SER	0	0.019	0.017	12.571	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	1228	ASN	0	-0.012	-0.015	14.855	-0.012	-0.012	0.000	0.000	0.000	0.000
34	A	1229	ASN	0	-0.046	-0.036	17.537	0.026	0.026	0.000	0.000	0.000	0.000
35	A	1230	GLU	-1	-0.894	-0.916	19.314	-0.100	-0.100	0.000	0.000	0.000	0.000
36	A	1231	THR	0	-0.068	-0.044	19.877	-0.054	-0.054	0.000	0.000	0.000	0.000
37	A	1232	SER	0	0.002	-0.004	19.012	0.033	0.033	0.000	0.000	0.000	0.000
38	A	1233	LEU	0	-0.028	-0.020	22.008	-0.031	-0.031	0.000	0.000	0.000	0.000
39	A	1234	THR	0	0.035	0.010	20.993	0.012	0.012	0.000	0.000	0.000	0.000
40	A	1235	GLU	-1	-0.793	-0.864	23.621	-0.152	-0.152	0.000	0.000	0.000	0.000
41	A	1236	LYS	1	0.821	0.925	21.132	0.286	0.286	0.000	0.000	0.000	0.000
42	A	1237	SER	0	0.030	-0.008	25.932	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	1238	PHE	0	0.038	0.009	26.588	-0.030	-0.030	0.000	0.000	0.000	0.000
44	A	1239	GLU	-1	-0.816	-0.891	26.928	-0.257	-0.257	0.000	0.000	0.000	0.000
45	A	1240	GLN	0	0.009	0.008	23.627	-0.022	-0.022	0.000	0.000	0.000	0.000
46	A	1241	PHE	0	0.050	0.021	21.656	-0.031	-0.031	0.000	0.000	0.000	0.000
47	A	1242	SER	0	-0.025	-0.016	22.349	-0.045	-0.045	0.000	0.000	0.000	0.000
48	A	1243	LYS	1	0.874	0.946	21.245	0.276	0.276	0.000	0.000	0.000	0.000
49	A	1244	LEU	0	0.037	0.024	15.806	-0.014	-0.014	0.000	0.000	0.000	0.000
50	A	1245	HIS	0	0.065	0.059	18.133	-0.093	-0.093	0.000	0.000	0.000	0.000
51	A	1246	SER	0	-0.058	-0.035	19.241	-0.037	-0.037	0.000	0.000	0.000	0.000
52	A	1247	GLN	0	-0.030	-0.032	16.557	0.037	0.037	0.000	0.000	0.000	0.000
53	A	1248	LEU	0	0.071	0.037	13.052	-0.042	-0.042	0.000	0.000	0.000	0.000
54	A	1249	GLN	0	0.003	-0.007	15.195	-0.073	-0.073	0.000	0.000	0.000	0.000
55	A	1250	LYS	1	0.869	0.944	17.429	0.395	0.395	0.000	0.000	0.000	0.000
56	A	1251	GLN	0	-0.017	0.000	9.454	0.154	0.154	0.000	0.000	0.000	0.000
57	A	1252	PHE	0	-0.009	-0.013	7.866	-0.106	-0.106	0.000	0.000	0.000	0.000
58	A	1253	ALA	0	0.033	0.018	12.964	0.015	0.015	0.000	0.000	0.000	0.000
59	A	1254	SER	0	-0.022	-0.006	12.962	0.077	0.077	0.000	0.000	0.000	0.000
60	A	1255	LEU	0	-0.033	-0.004	9.259	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	1256	THR	0	-0.008	-0.003	13.790	0.174	0.174	0.000	0.000	0.000	0.000
62	A	1257	LEU	0	-0.012	0.001	13.952	-0.073	-0.073	0.000	0.000	0.000	0.000
63	A	1258	PRO	0	0.021	0.017	16.872	0.079	0.079	0.000	0.000	0.000	0.000
64	A	1259	GLU	-1	-0.900	-0.960	19.799	-0.467	-0.467	0.000	0.000	0.000	0.000
65	A	1260	PHE	0	0.000	0.010	22.663	0.001	0.001	0.000	0.000	0.000	0.000
66	A	1261	PRO	0	0.009	-0.007	24.246	0.032	0.032	0.000	0.000	0.000	0.000
67	A	1262	HIS	1	0.828	0.927	27.484	0.388	0.388	0.000	0.000	0.000	0.000
68	A	1263	TRP	0	0.051	0.010	29.517	0.026	0.026	0.000	0.000	0.000	0.000
69	A	1264	TRP	0	0.057	0.030	30.122	0.015	0.015	0.000	0.000	0.000	0.000
70	A	1265	HIS	0	-0.048	-0.020	33.476	0.001	0.001	0.000	0.000	0.000	0.000
71	A	1266	LEU	0	0.076	0.025	36.740	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	1267	PRO	0	0.003	-0.013	37.067	0.002	0.002	0.000	0.000	0.000	0.000
73	A	1268	PHE	0	-0.009	0.005	30.009	0.001	0.001	0.000	0.000	0.000	0.000
74	A	1269	THR	0	0.004	-0.004	35.434	0.001	0.001	0.000	0.000	0.000	0.000
75	A	1270	ASN	0	-0.016	-0.006	37.904	0.007	0.007	0.000	0.000	0.000	0.000
76	A	1271	SER	0	-0.017	0.005	37.653	0.004	0.004	0.000	0.000	0.000	0.000
77	A	1272	ASP	-1	-0.751	-0.887	35.515	-0.197	-0.197	0.000	0.000	0.000	0.000
78	A	1273	HIS	0	0.011	0.001	33.911	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	1274	ARG	1	0.821	0.915	31.767	0.272	0.272	0.000	0.000	0.000	0.000
80	A	1275	ARG	1	0.869	0.937	31.387	0.195	0.195	0.000	0.000	0.000	0.000
81	A	1276	PHE	0	0.014	0.000	29.493	-0.023	-0.023	0.000	0.000	0.000	0.000
82	A	1277	ARG	1	0.893	0.942	28.310	0.307	0.307	0.000	0.000	0.000	0.000
83	A	1278	ASP	-1	-0.757	-0.869	27.677	-0.366	-0.366	0.000	0.000	0.000	0.000
84	A	1279	LEU	0	-0.011	0.002	25.081	-0.037	-0.037	0.000	0.000	0.000	0.000
85	A	1280	ASN	0	0.070	0.035	23.718	-0.050	-0.050	0.000	0.000	0.000	0.000
86	A	1281	HIS	0	-0.076	-0.042	23.073	-0.033	-0.033	0.000	0.000	0.000	0.000
87	A	1282	TYR	0	-0.015	-0.032	19.313	-0.057	-0.057	0.000	0.000	0.000	0.000
88	A	1283	MET	0	-0.029	-0.011	19.327	-0.069	-0.069	0.000	0.000	0.000	0.000
89	A	1284	GLU	-1	-0.827	-0.896	18.080	-0.639	-0.639	0.000	0.000	0.000	0.000
90	A	1285	GLN	0	-0.023	-0.018	17.573	-0.109	-0.109	0.000	0.000	0.000	0.000
91	A	1286	ILE	0	-0.062	-0.029	15.106	-0.134	-0.134	0.000	0.000	0.000	0.000
92	A	1287	LEU	0	-0.044	-0.010	13.352	-0.165	-0.165	0.000	0.000	0.000	0.000
93	A	1288	ASN	0	-0.056	-0.037	12.967	-0.163	-0.163	0.000	0.000	0.000	0.000
94	A	1289	VAL	0	-0.021	0.014	11.580	0.028	0.028	0.000	0.000	0.000	0.000
95	A	1290	SER	0	-0.003	-0.040	6.467	0.203	0.203	0.000	0.000	0.000	0.000
96	A	1291	HIS	0	-0.012	0.000	2.383	-3.915	-2.504	0.886	-0.920	-1.377	-0.009
97	A	1292	GLU	-1	-0.787	-0.905	2.674	-16.518	-13.897	0.360	-1.487	-1.494	-0.018
98	A	1293	VAL	0	0.004	0.013	5.354	1.129	1.178	-0.001	-0.001	-0.047	0.000
99	A	1294	THR	0	0.013	0.007	8.698	0.412	0.412	0.000	0.000	0.000	0.000
100	A	1295	ASN	0	-0.080	-0.041	5.129	1.285	1.285	0.000	0.000	0.000	0.000
101	A	1296	SER	0	-0.026	-0.016	6.923	0.480	0.480	0.000	0.000	0.000	0.000
102	A	1297	ASP	-1	-0.858	-0.941	8.585	-0.043	-0.043	0.000	0.000	0.000	0.000
103	A	1298	CYS	0	-0.057	-0.023	10.939	0.053	0.053	0.000	0.000	0.000	0.000
104	A	1299	VAL	0	0.035	0.015	11.593	0.141	0.141	0.000	0.000	0.000	0.000
105	A	1300	LEU	0	0.012	0.011	8.263	0.139	0.139	0.000	0.000	0.000	0.000
106	A	1301	SER	0	0.008	0.003	12.812	0.132	0.132	0.000	0.000	0.000	0.000
107	A	1302	PHE	0	-0.080	-0.032	15.543	0.077	0.077	0.000	0.000	0.000	0.000
108	A	1303	PHE	0	0.001	-0.031	15.269	0.062	0.062	0.000	0.000	0.000	0.000
109	A	1304	LEU	0	0.029	0.026	13.467	0.038	0.038	0.000	0.000	0.000	0.000
110	A	1305	SER	0	-0.037	-0.008	17.444	0.069	0.069	0.000	0.000	0.000	0.000
111	A	1306	GLU	-1	-0.952	-0.956	20.010	-0.144	-0.144	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-6:ASN)