FMO DATABASE

FMODB ID: 49MZN

Calculation Name: 5LZN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5LZN

Chain ID: A

ChEMBL ID:

UniProt ID: Q80VC9

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	OptAll
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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-978367.601552
FMO2-HF: Nuclear repulsion	931783.274156
FMO2-HF: Total energy	-46584.327396
FMO2-MP2: Total energy	-46718.188463

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:1122:LYS)

Summations of interaction energy for fragment #1(A:1122:LYS)

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.
47.78	51.157	2.899	-2.324	-3.952	0

Interaction energy analysis for fragmet #1(A:1122:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.978 / q_NPA : 0.986

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	1124	ASN	0	0.009	-0.006	3.869	-3.453	-0.938	-0.019	-1.404	-1.092	0.004
4	A	1125	LYS	1	0.881	0.961	6.324	23.148	23.148	0.000	0.000	0.000	0.000
5	A	1126	PHE	0	0.050	0.011	7.733	1.643	1.643	0.000	0.000	0.000	0.000
6	A	1127	ILE	0	-0.018	0.002	7.215	1.525	1.525	0.000	0.000	0.000	0.000
7	A	1128	ILE	0	0.011	0.004	10.383	1.726	1.726	0.000	0.000	0.000	0.000
8	A	1129	HIS	0	0.008	0.010	12.680	1.225	1.225	0.000	0.000	0.000	0.000
9	A	1130	ASN	0	0.022	0.014	14.045	1.981	1.981	0.000	0.000	0.000	0.000
10	A	1131	ALA	0	0.032	0.011	14.773	0.966	0.966	0.000	0.000	0.000	0.000
11	A	1132	LEU	0	-0.022	-0.024	16.508	0.973	0.973	0.000	0.000	0.000	0.000
12	A	1133	SER	0	-0.012	-0.013	18.346	0.996	0.996	0.000	0.000	0.000	0.000
13	A	1134	HIS	0	-0.075	-0.036	18.250	1.083	1.083	0.000	0.000	0.000	0.000
14	A	1135	CYS	0	-0.103	-0.039	19.353	0.222	0.222	0.000	0.000	0.000	0.000
15	A	1136	CYS	0	0.003	0.007	19.690	0.221	0.221	0.000	0.000	0.000	0.000
16	A	1137	LEU	0	-0.006	0.000	21.290	0.499	0.499	0.000	0.000	0.000	0.000
17	A	1138	ALA	0	0.029	0.015	23.724	0.066	0.066	0.000	0.000	0.000	0.000
18	A	1139	GLY	0	0.009	0.021	25.913	0.331	0.331	0.000	0.000	0.000	0.000
19	A	1140	LYS	1	0.998	0.979	28.778	8.002	8.002	0.000	0.000	0.000	0.000
20	A	1141	VAL	0	-0.007	-0.008	32.087	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	1142	ASN	0	0.061	0.035	26.086	-0.052	-0.052	0.000	0.000	0.000	0.000
22	A	1143	GLU	-1	-0.733	-0.829	26.619	-11.345	-11.345	0.000	0.000	0.000	0.000
23	A	1144	PRO	0	-0.009	-0.011	26.841	-0.323	-0.323	0.000	0.000	0.000	0.000
24	A	1145	GLN	0	-0.058	-0.033	25.502	0.131	0.131	0.000	0.000	0.000	0.000
25	A	1146	LYS	1	0.845	0.906	21.966	11.378	11.378	0.000	0.000	0.000	0.000
26	A	1147	ASN	0	-0.014	-0.020	22.155	-0.828	-0.828	0.000	0.000	0.000	0.000
27	A	1148	ARG	1	0.982	1.002	22.653	10.132	10.132	0.000	0.000	0.000	0.000
28	A	1149	ILE	0	-0.022	-0.010	19.023	-0.201	-0.201	0.000	0.000	0.000	0.000
29	A	1150	LEU	0	-0.013	-0.009	17.432	-0.687	-0.687	0.000	0.000	0.000	0.000
30	A	1151	GLU	-1	-0.888	-0.947	18.156	-11.973	-11.973	0.000	0.000	0.000	0.000
31	A	1152	GLU	-1	-0.872	-0.933	19.225	-12.814	-12.814	0.000	0.000	0.000	0.000
32	A	1153	ILE	0	-0.061	-0.026	13.148	-0.716	-0.716	0.000	0.000	0.000	0.000
33	A	1154	GLU	-1	-0.845	-0.941	14.541	-17.981	-17.981	0.000	0.000	0.000	0.000
34	A	1155	LYS	1	0.834	0.927	16.010	12.263	12.263	0.000	0.000	0.000	0.000
35	A	1156	SER	0	-0.054	-0.020	14.217	-0.224	-0.224	0.000	0.000	0.000	0.000
36	A	1157	LYS	1	0.935	0.953	11.881	14.989	14.989	0.000	0.000	0.000	0.000
37	A	1158	ALA	0	0.021	0.036	10.123	-1.109	-1.109	0.000	0.000	0.000	0.000
38	A	1159	ASN	0	0.047	0.014	4.745	-0.092	0.097	-0.001	-0.019	-0.168	0.000
39	A	1160	HIS	0	-0.059	-0.025	6.357	-3.954	-3.954	0.000	0.000	0.000	0.000
40	A	1161	PHE	0	0.037	0.015	7.902	2.549	2.549	0.000	0.000	0.000	0.000
41	A	1162	LEU	0	0.009	0.002	10.572	-0.806	-0.806	0.000	0.000	0.000	0.000
42	A	1163	ILE	0	-0.007	-0.011	13.151	1.023	1.023	0.000	0.000	0.000	0.000
43	A	1164	LEU	0	-0.026	0.010	16.493	-0.217	-0.217	0.000	0.000	0.000	0.000
44	A	1165	PHE	0	0.036	-0.003	18.167	0.368	0.368	0.000	0.000	0.000	0.000
45	A	1166	ARG	1	0.905	0.947	22.159	10.390	10.390	0.000	0.000	0.000	0.000
46	A	1167	ASP	-1	-0.791	-0.873	25.047	-10.617	-10.617	0.000	0.000	0.000	0.000
47	A	1168	SER	0	0.065	0.027	23.585	-0.244	-0.244	0.000	0.000	0.000	0.000
48	A	1169	SER	0	-0.063	-0.048	24.437	-0.263	-0.263	0.000	0.000	0.000	0.000
49	A	1170	CYS	0	-0.092	-0.055	21.268	-0.212	-0.212	0.000	0.000	0.000	0.000
50	A	1171	GLN	0	-0.032	-0.005	22.538	-0.047	-0.047	0.000	0.000	0.000	0.000
51	A	1172	PHE	0	0.030	-0.002	19.285	-0.096	-0.096	0.000	0.000	0.000	0.000
52	A	1173	ARG	1	0.868	0.963	22.373	11.037	11.037	0.000	0.000	0.000	0.000
53	A	1174	ALA	0	-0.004	-0.003	21.547	0.379	0.379	0.000	0.000	0.000	0.000
54	A	1175	LEU	0	0.011	0.018	14.610	-0.511	-0.511	0.000	0.000	0.000	0.000
55	A	1176	TYR	0	-0.010	-0.023	15.990	0.782	0.782	0.000	0.000	0.000	0.000
56	A	1177	THR	0	-0.027	-0.016	12.573	-0.788	-0.788	0.000	0.000	0.000	0.000
57	A	1178	LEU	0	-0.013	0.001	8.816	1.069	1.069	0.000	0.000	0.000	0.000
58	A	1179	SER	0	0.003	0.007	10.719	-1.658	-1.658	0.000	0.000	0.000	0.000
59	A	1180	GLY	0	-0.036	-0.033	9.759	-0.175	-0.175	0.000	0.000	0.000	0.000
60	A	1181	GLU	-1	-0.944	-0.966	10.645	-17.908	-17.908	0.000	0.000	0.000	0.000
61	A	1182	THR	0	-0.029	-0.033	13.996	0.494	0.494	0.000	0.000	0.000	0.000
62	A	1183	GLU	-1	-0.955	-0.971	13.798	-18.316	-18.316	0.000	0.000	0.000	0.000
63	A	1184	GLU	-1	-0.910	-0.933	14.887	-14.082	-14.082	0.000	0.000	0.000	0.000
64	A	1185	LEU	0	-0.014	-0.007	13.363	-1.017	-1.017	0.000	0.000	0.000	0.000
65	A	1186	SER	0	0.051	0.018	15.986	1.425	1.425	0.000	0.000	0.000	0.000
66	A	1187	ARG	1	0.825	0.911	17.193	11.095	11.095	0.000	0.000	0.000	0.000
67	A	1188	LEU	0	-0.036	-0.010	15.587	0.179	0.179	0.000	0.000	0.000	0.000
68	A	1189	ALA	0	0.015	-0.004	19.255	0.603	0.603	0.000	0.000	0.000	0.000
69	A	1190	GLY	0	0.011	0.005	21.603	-0.298	-0.298	0.000	0.000	0.000	0.000
70	A	1191	TYR	0	-0.003	-0.011	24.184	0.136	0.136	0.000	0.000	0.000	0.000
71	A	1192	GLY	0	0.079	0.028	24.123	-0.163	-0.163	0.000	0.000	0.000	0.000
72	A	1193	PRO	0	0.043	0.036	23.797	0.202	0.202	0.000	0.000	0.000	0.000
73	A	1194	ARG	1	0.880	0.945	20.965	12.319	12.319	0.000	0.000	0.000	0.000
74	A	1195	THR	0	0.056	0.019	19.932	-0.402	-0.402	0.000	0.000	0.000	0.000
75	A	1196	VAL	0	-0.032	-0.010	19.263	0.629	0.629	0.000	0.000	0.000	0.000
76	A	1197	THR	0	0.096	0.029	18.691	-0.786	-0.786	0.000	0.000	0.000	0.000
77	A	1198	PRO	0	0.071	0.017	16.714	0.310	0.310	0.000	0.000	0.000	0.000
78	A	1199	ALA	0	0.000	0.006	18.937	0.088	0.088	0.000	0.000	0.000	0.000
79	A	1200	MET	0	-0.037	0.016	21.973	0.435	0.435	0.000	0.000	0.000	0.000
80	A	1201	VAL	0	-0.015	-0.002	17.403	0.237	0.237	0.000	0.000	0.000	0.000
81	A	1202	GLU	-1	-0.884	-0.908	20.724	-11.464	-11.464	0.000	0.000	0.000	0.000
82	A	1203	GLY	0	0.011	0.015	20.408	-0.068	-0.068	0.000	0.000	0.000	0.000
83	A	1204	ILE	0	-0.022	-0.016	14.301	-0.436	-0.436	0.000	0.000	0.000	0.000
84	A	1205	TYR	0	-0.011	-0.039	15.361	0.469	0.469	0.000	0.000	0.000	0.000
85	A	1206	LYS	1	0.910	0.947	11.470	17.817	17.817	0.000	0.000	0.000	0.000
86	A	1207	TYR	0	0.006	-0.010	12.454	1.751	1.751	0.000	0.000	0.000	0.000
87	A	1208	ASN	0	-0.025	-0.020	13.403	-0.229	-0.229	0.000	0.000	0.000	0.000
88	A	1209	SER	0	0.078	0.035	14.940	0.773	0.773	0.000	0.000	0.000	0.000
89	A	1210	ASP	-1	-0.909	-0.941	16.759	-15.903	-15.903	0.000	0.000	0.000	0.000
90	A	1211	ARG	1	0.908	0.949	19.195	14.321	14.321	0.000	0.000	0.000	0.000
91	A	1212	LYS	1	0.902	0.963	19.735	12.997	12.997	0.000	0.000	0.000	0.000
92	A	1213	ARG	1	0.953	0.976	19.391	13.619	13.619	0.000	0.000	0.000	0.000
93	A	1214	PHE	0	0.078	0.032	14.342	-0.780	-0.780	0.000	0.000	0.000	0.000
94	A	1215	THR	0	-0.066	-0.021	16.037	0.710	0.710	0.000	0.000	0.000	0.000
95	A	1216	GLN	0	0.075	0.058	16.416	-0.588	-0.588	0.000	0.000	0.000	0.000
96	A	1217	ILE	0	-0.052	-0.029	12.143	-0.625	-0.625	0.000	0.000	0.000	0.000
97	A	1218	PRO	0	0.026	0.009	16.429	0.583	0.583	0.000	0.000	0.000	0.000
98	A	1219	ALA	0	0.033	0.018	16.656	-0.949	-0.949	0.000	0.000	0.000	0.000
99	A	1220	LYS	1	0.846	0.932	9.618	26.657	26.657	0.000	0.000	0.000	0.000
100	A	1221	THR	0	0.073	0.032	12.165	0.746	0.746	0.000	0.000	0.000	0.000
101	A	1222	MET	0	0.044	0.045	10.758	-1.998	-1.998	0.000	0.000	0.000	0.000
102	A	1223	SER	0	0.019	-0.013	7.318	-1.502	-1.502	0.000	0.000	0.000	0.000
103	A	1224	MET	0	-0.009	0.001	2.402	-2.824	-2.151	2.919	-0.901	-2.692	-0.004
104	A	1225	SER	0	-0.021	0.000	5.533	1.509	1.509	0.000	0.000	0.000	0.000
105	A	1226	VAL	0	0.017	0.004	7.280	2.702	2.702	0.000	0.000	0.000	0.000
106	A	1227	ASP	-1	-0.801	-0.876	9.457	-25.967	-25.967	0.000	0.000	0.000	0.000
107	A	1228	ALA	0	-0.013	-0.011	11.487	0.920	0.920	0.000	0.000	0.000	0.000
108	A	1229	PHE	0	-0.017	-0.015	15.080	-0.565	-0.565	0.000	0.000	0.000	0.000
109	A	1230	THR	0	0.001	-0.011	17.736	0.267	0.267	0.000	0.000	0.000	0.000
110	A	1231	ILE	0	0.007	-0.009	20.959	-0.524	-0.524	0.000	0.000	0.000	0.000
111	A	1232	GLN	0	0.023	0.006	23.398	0.775	0.775	0.000	0.000	0.000	0.000
112	A	1233	GLY	0	0.010	0.005	26.489	0.227	0.227	0.000	0.000	0.000	0.000
113	A	1234	HIS	0	0.003	-0.004	29.279	0.140	0.140	0.000	0.000	0.000	0.000
114	A	1235	LEU	0	-0.037	-0.014	25.481	0.179	0.179	0.000	0.000	0.000	0.000
115	A	1236	TRP	0	-0.057	-0.014	24.497	0.162	0.162	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1122:LYS)