FMO DATABASE

FMODB ID: R9GK8

Calculation Name: 2V14-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2V14

Chain ID: A

ChEMBL ID:

UniProt ID: Q96L93

Base Structure: X-ray

Registration Date: 2023-09-19

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1284420.400079
FMO2-HF: Nuclear repulsion	1229637.903648
FMO2-HF: Total energy	-54782.496431
FMO2-MP2: Total energy	-54944.10627

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:1179:ASP)

Summations of interaction energy for fragment #1(A:1179:ASP)

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.
-141.371	-135.687	0.192	-2.653	-3.222	0.018

Interaction energy analysis for fragmet #1(A:1179:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.912 / q_NPA : -0.965

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	1181	LYS	1	0.930	0.963	3.071	-65.555	-61.608	0.106	-1.993	-2.060	0.012
4	A	1182	ASP	-1	-0.908	-0.948	3.237	24.628	26.121	0.086	-0.625	-0.954	0.006
5	A	1183	PRO	0	0.020	0.023	4.363	-1.558	-1.314	0.000	-0.035	-0.208	0.000
6	A	1184	ILE	0	0.002	-0.002	5.703	-3.193	-3.193	0.000	0.000	0.000	0.000
7	A	1185	LYS	1	0.914	0.972	6.308	-30.873	-30.873	0.000	0.000	0.000	0.000
8	A	1186	ILE	0	0.014	-0.004	9.442	-1.478	-1.478	0.000	0.000	0.000	0.000
9	A	1187	SER	0	-0.046	-0.014	13.164	-0.090	-0.090	0.000	0.000	0.000	0.000
10	A	1188	ILE	0	-0.001	0.002	15.911	-0.364	-0.364	0.000	0.000	0.000	0.000
11	A	1189	PRO	0	-0.021	0.009	18.187	-0.409	-0.409	0.000	0.000	0.000	0.000
12	A	1190	ARG	1	0.911	0.954	20.594	-12.708	-12.708	0.000	0.000	0.000	0.000
13	A	1191	TYR	0	0.019	0.006	24.218	0.350	0.350	0.000	0.000	0.000	0.000
14	A	1192	VAL	0	0.036	0.016	27.042	-0.145	-0.145	0.000	0.000	0.000	0.000
15	A	1193	LEU	0	-0.008	-0.003	29.979	0.011	0.011	0.000	0.000	0.000	0.000
16	A	1194	CYS	0	0.013	0.011	31.832	0.049	0.049	0.000	0.000	0.000	0.000
17	A	1195	GLY	0	0.035	0.016	34.532	-0.102	-0.102	0.000	0.000	0.000	0.000
18	A	1196	GLN	0	0.070	0.019	37.944	0.116	0.116	0.000	0.000	0.000	0.000
19	A	1197	GLY	0	0.038	0.031	41.392	-0.074	-0.074	0.000	0.000	0.000	0.000
20	A	1198	LYS	1	0.869	0.901	42.301	-6.676	-6.676	0.000	0.000	0.000	0.000
21	A	1199	ASP	-1	-0.796	-0.871	39.892	7.258	7.258	0.000	0.000	0.000	0.000
22	A	1200	ALA	0	-0.116	-0.040	38.132	0.237	0.237	0.000	0.000	0.000	0.000
23	A	1201	HIS	1	0.696	0.819	32.480	-8.728	-8.728	0.000	0.000	0.000	0.000
24	A	1202	PHE	0	0.066	0.035	30.646	0.043	0.043	0.000	0.000	0.000	0.000
25	A	1203	GLU	-1	-0.891	-0.940	28.091	9.714	9.714	0.000	0.000	0.000	0.000
26	A	1204	PHE	0	-0.021	-0.027	24.003	-0.108	-0.108	0.000	0.000	0.000	0.000
27	A	1205	GLU	-1	-0.787	-0.889	21.283	12.626	12.626	0.000	0.000	0.000	0.000
28	A	1206	VAL	0	-0.008	-0.014	17.799	0.385	0.385	0.000	0.000	0.000	0.000
29	A	1207	LYS	1	0.984	0.993	14.375	-16.966	-16.966	0.000	0.000	0.000	0.000
30	A	1208	ILE	0	-0.019	-0.015	12.847	0.410	0.410	0.000	0.000	0.000	0.000
31	A	1209	THR	0	0.008	-0.012	8.159	-1.202	-1.202	0.000	0.000	0.000	0.000
32	A	1210	VAL	0	-0.020	-0.005	8.986	0.754	0.754	0.000	0.000	0.000	0.000
33	A	1211	LEU	0	0.006	-0.007	4.922	-1.175	-1.175	0.000	0.000	0.000	0.000
34	A	1212	ASP	-1	-0.825	-0.909	6.974	27.675	27.675	0.000	0.000	0.000	0.000
35	A	1213	GLU	-1	-0.930	-0.948	9.228	17.207	17.207	0.000	0.000	0.000	0.000
36	A	1214	THR	0	-0.020	-0.016	11.657	0.768	0.768	0.000	0.000	0.000	0.000
37	A	1215	TRP	0	-0.109	-0.070	13.508	-1.083	-1.083	0.000	0.000	0.000	0.000
38	A	1216	THR	0	0.008	0.006	16.740	0.780	0.780	0.000	0.000	0.000	0.000
39	A	1217	VAL	0	-0.037	-0.008	19.454	-0.552	-0.552	0.000	0.000	0.000	0.000
40	A	1218	PHE	0	0.026	0.028	22.239	0.193	0.193	0.000	0.000	0.000	0.000
41	A	1219	ARG	1	0.760	0.880	23.647	-12.078	-12.078	0.000	0.000	0.000	0.000
42	A	1220	ARG	1	1.022	1.026	26.293	-8.704	-8.704	0.000	0.000	0.000	0.000
43	A	1221	TYR	0	-0.046	-0.102	28.268	-0.046	-0.046	0.000	0.000	0.000	0.000
44	A	1222	SER	0	0.002	-0.022	29.022	0.105	0.105	0.000	0.000	0.000	0.000
45	A	1223	ARG	1	0.960	0.991	26.867	-10.605	-10.605	0.000	0.000	0.000	0.000
46	A	1224	PHE	0	0.056	0.035	21.811	0.079	0.079	0.000	0.000	0.000	0.000
47	A	1225	ARG	1	0.970	0.992	25.973	-8.886	-8.886	0.000	0.000	0.000	0.000
48	A	1226	GLU	-1	-0.850	-0.912	28.800	9.175	9.175	0.000	0.000	0.000	0.000
49	A	1227	MET	0	-0.013	0.022	20.682	0.038	0.038	0.000	0.000	0.000	0.000
50	A	1228	HIS	0	0.045	0.068	25.316	0.355	0.355	0.000	0.000	0.000	0.000
51	A	1229	LYS	1	0.825	0.879	26.256	-9.033	-9.033	0.000	0.000	0.000	0.000
52	A	1230	THR	0	0.008	0.003	27.669	-0.159	-0.159	0.000	0.000	0.000	0.000
53	A	1231	LEU	0	-0.002	-0.011	22.103	-0.044	-0.044	0.000	0.000	0.000	0.000
54	A	1232	LYS	1	0.930	0.974	26.037	-9.899	-9.899	0.000	0.000	0.000	0.000
55	A	1233	LEU	0	-0.017	-0.004	27.436	-0.114	-0.114	0.000	0.000	0.000	0.000
56	A	1234	LYS	1	0.899	0.968	25.615	-11.788	-11.788	0.000	0.000	0.000	0.000
57	A	1235	TYR	0	0.006	-0.007	23.437	0.166	0.166	0.000	0.000	0.000	0.000
58	A	1236	ALA	0	0.094	0.051	25.832	-0.100	-0.100	0.000	0.000	0.000	0.000
59	A	1237	GLU	-1	-0.765	-0.864	20.947	13.489	13.489	0.000	0.000	0.000	0.000
60	A	1238	LEU	0	-0.023	-0.020	21.006	0.265	0.265	0.000	0.000	0.000	0.000
61	A	1239	ALA	0	-0.059	-0.035	24.310	-0.275	-0.275	0.000	0.000	0.000	0.000
62	A	1240	ALA	0	-0.002	0.006	24.058	-0.290	-0.290	0.000	0.000	0.000	0.000
63	A	1241	LEU	0	-0.024	0.003	20.842	0.075	0.075	0.000	0.000	0.000	0.000
64	A	1242	GLU	-1	-0.932	-0.961	24.646	9.820	9.820	0.000	0.000	0.000	0.000
65	A	1243	PHE	0	-0.060	-0.032	25.331	0.223	0.223	0.000	0.000	0.000	0.000
66	A	1244	PRO	0	0.073	0.050	25.597	-0.379	-0.379	0.000	0.000	0.000	0.000
67	A	1245	PRO	0	0.075	0.083	28.584	-0.154	-0.154	0.000	0.000	0.000	0.000
68	A	1246	LYS	1	0.883	0.952	32.098	-8.654	-8.654	0.000	0.000	0.000	0.000
69	A	1247	LYS	1	1.000	0.997	34.208	-8.463	-8.463	0.000	0.000	0.000	0.000
70	A	1248	LEU	0	0.052	0.031	37.604	0.094	0.094	0.000	0.000	0.000	0.000
71	A	1249	PHE	0	0.032	0.009	40.629	0.004	0.004	0.000	0.000	0.000	0.000
72	A	1250	GLY	0	0.062	0.018	39.706	0.128	0.128	0.000	0.000	0.000	0.000
73	A	1251	ASN	0	-0.040	-0.014	35.290	0.378	0.378	0.000	0.000	0.000	0.000
74	A	1252	LYS	1	0.970	0.973	36.374	-6.935	-6.935	0.000	0.000	0.000	0.000
75	A	1253	ASP	-1	-0.758	-0.842	36.989	7.959	7.959	0.000	0.000	0.000	0.000
76	A	1254	GLU	-1	-0.853	-0.951	33.496	8.821	8.821	0.000	0.000	0.000	0.000
77	A	1255	ARG	1	0.883	0.935	32.347	-7.621	-7.621	0.000	0.000	0.000	0.000
78	A	1256	VAL	0	0.007	0.019	32.030	0.253	0.253	0.000	0.000	0.000	0.000
79	A	1257	ILE	0	-0.089	-0.036	29.800	0.306	0.306	0.000	0.000	0.000	0.000
80	A	1258	ALA	0	0.035	0.008	28.176	0.393	0.393	0.000	0.000	0.000	0.000
81	A	1259	GLU	-1	-0.887	-0.942	27.045	10.059	10.059	0.000	0.000	0.000	0.000
82	A	1260	ARG	1	0.840	0.904	26.947	-9.133	-9.133	0.000	0.000	0.000	0.000
83	A	1261	ARG	1	0.879	0.932	20.616	-12.452	-12.452	0.000	0.000	0.000	0.000
84	A	1262	SER	0	0.015	0.014	22.606	0.659	0.659	0.000	0.000	0.000	0.000
85	A	1263	HIS	0	-0.014	-0.007	22.220	0.890	0.890	0.000	0.000	0.000	0.000
86	A	1264	LEU	0	-0.053	-0.024	23.037	0.223	0.223	0.000	0.000	0.000	0.000
87	A	1265	GLU	-1	-0.855	-0.926	17.682	15.485	15.485	0.000	0.000	0.000	0.000
88	A	1266	LYS	1	0.882	0.944	18.072	-13.818	-13.818	0.000	0.000	0.000	0.000
89	A	1267	TYR	0	0.020	-0.035	18.915	0.583	0.583	0.000	0.000	0.000	0.000
90	A	1268	LEU	0	-0.006	-0.017	17.025	0.268	0.268	0.000	0.000	0.000	0.000
91	A	1269	ARG	1	0.872	0.930	13.389	-16.980	-16.980	0.000	0.000	0.000	0.000
92	A	1270	ASP	-1	-0.808	-0.910	15.027	16.374	16.374	0.000	0.000	0.000	0.000
93	A	1271	PHE	0	-0.062	-0.034	17.249	0.199	0.199	0.000	0.000	0.000	0.000
94	A	1272	PHE	0	0.008	-0.018	12.746	-0.073	-0.073	0.000	0.000	0.000	0.000
95	A	1273	SER	0	0.018	0.027	13.082	1.258	1.258	0.000	0.000	0.000	0.000
96	A	1274	VAL	0	0.001	0.003	14.130	0.381	0.381	0.000	0.000	0.000	0.000
97	A	1275	MET	0	-0.027	-0.001	16.527	-0.152	-0.152	0.000	0.000	0.000	0.000
98	A	1276	LEU	0	0.046	0.058	10.001	0.022	0.022	0.000	0.000	0.000	0.000
99	A	1277	GLN	0	0.011	0.000	11.010	2.937	2.937	0.000	0.000	0.000	0.000
100	A	1278	SER	0	-0.109	-0.061	14.808	-0.653	-0.653	0.000	0.000	0.000	0.000
101	A	1279	ALA	0	0.056	0.010	18.221	0.338	0.338	0.000	0.000	0.000	0.000
102	A	1280	THR	0	-0.043	-0.027	19.583	-0.347	-0.347	0.000	0.000	0.000	0.000
103	A	1281	SER	0	-0.016	-0.016	17.483	-0.761	-0.761	0.000	0.000	0.000	0.000
104	A	1282	PRO	0	-0.069	-0.035	18.938	0.564	0.564	0.000	0.000	0.000	0.000
105	A	1283	LEU	0	0.004	-0.017	14.606	0.303	0.303	0.000	0.000	0.000	0.000
106	A	1284	HIS	0	-0.006	0.010	13.930	1.364	1.364	0.000	0.000	0.000	0.000
107	A	1285	ILE	0	0.019	-0.011	8.762	-0.218	-0.218	0.000	0.000	0.000	0.000
108	A	1286	ASN	0	-0.028	-0.010	11.841	2.696	2.696	0.000	0.000	0.000	0.000
109	A	1287	LYS	1	0.862	0.949	14.110	-17.891	-17.891	0.000	0.000	0.000	0.000
110	A	1288	VAL	0	0.029	0.004	15.442	1.119	1.119	0.000	0.000	0.000	0.000
111	A	1289	GLY	0	0.006	0.000	16.031	-0.868	-0.868	0.000	0.000	0.000	0.000
112	A	1290	LEU	0	-0.051	-0.012	12.078	-0.888	-0.888	0.000	0.000	0.000	0.000
113	A	1291	THR	0	-0.015	0.007	13.477	1.164	1.164	0.000	0.000	0.000	0.000
114	A	1292	LEU	0	-0.008	-0.025	9.319	-1.311	-1.311	0.000	0.000	0.000	0.000
115	A	1293	SER	0	0.079	0.038	11.661	0.878	0.878	0.000	0.000	0.000	0.000
116	A	1294	LYS	1	0.946	0.980	13.686	-15.515	-15.515	0.000	0.000	0.000	0.000
117	A	1295	HIS	0	-0.004	0.001	15.631	-0.675	-0.675	0.000	0.000	0.000	0.000
118	A	1296	THR	0	0.034	0.019	15.349	-0.616	-0.616	0.000	0.000	0.000	0.000
119	A	1297	ILE	0	0.029	0.020	13.778	-0.715	-0.715	0.000	0.000	0.000	0.000
120	A	1298	CYS	0	-0.088	-0.053	17.042	-0.965	-0.965	0.000	0.000	0.000	0.000
121	A	1299	GLU	-1	-0.950	-0.971	20.213	11.621	11.621	0.000	0.000	0.000	0.000
122	A	1300	PHE	0	-0.023	0.004	18.962	-0.529	-0.529	0.000	0.000	0.000	0.000
123	A	1301	SER	0	0.009	-0.018	20.832	-0.793	-0.793	0.000	0.000	0.000	0.000
124	A	1302	PRO	0	0.029	0.000	21.724	0.313	0.313	0.000	0.000	0.000	0.000
125	A	1303	PHE	0	-0.070	-0.023	20.719	-0.478	-0.478	0.000	0.000	0.000	0.000
126	A	1304	PHE	0	0.092	0.023	17.819	-0.163	-0.163	0.000	0.000	0.000	0.000
127	A	1305	LYS	1	0.942	0.992	20.568	-11.711	-11.711	0.000	0.000	0.000	0.000
128	A	1306	LYS	1	0.886	0.950	20.571	-12.978	-12.978	0.000	0.000	0.000	0.000
129	A	1307	GLY	0	0.008	0.000	24.033	-0.266	-0.266	0.000	0.000	0.000	0.000
130	A	1308	VAL	0	0.000	-0.018	27.273	0.187	0.187	0.000	0.000	0.000	0.000
131	A	1309	PHE	0	0.016	0.009	28.421	-0.044	-0.044	0.000	0.000	0.000	0.000
132	A	1310	ASP	-1	-0.783	-0.866	23.210	11.644	11.644	0.000	0.000	0.000	0.000
133	A	1311	TYR	0	-0.032	-0.020	20.911	-0.048	-0.048	0.000	0.000	0.000	0.000
134	A	1312	SER	0	0.052	0.023	18.416	0.077	0.077	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1179:ASP)