FMO DATABASE

FMODB ID: QY96Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-974596.622525
FMO2-HF: Nuclear repulsion	928013.028686
FMO2-HF: Total energy	-46583.593838
FMO2-MP2: Total energy	-46717.452551

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.
55.651	59.035	3.122	-2.569	-3.938	0.004

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 : 0.997 / q_NPA : 0.994

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

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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	0.015	0.002	3.784	-4.808	-2.027	-0.024	-1.507	-1.251	0.006
4	A	1125	LYS	1	0.968	0.995	6.076	23.592	23.592	0.000	0.000	0.000	0.000
5	A	1126	PHE	0	0.017	0.008	7.967	1.663	1.663	0.000	0.000	0.000	0.000
6	A	1127	ILE	0	0.010	0.010	6.968	1.675	1.675	0.000	0.000	0.000	0.000
7	A	1128	ILE	0	0.016	0.007	10.139	1.941	1.941	0.000	0.000	0.000	0.000
8	A	1129	HIS	0	0.060	0.039	12.304	1.054	1.054	0.000	0.000	0.000	0.000
9	A	1130	ASN	0	0.011	0.014	13.911	2.197	2.197	0.000	0.000	0.000	0.000
10	A	1131	ALA	0	0.016	0.000	14.728	1.072	1.072	0.000	0.000	0.000	0.000
11	A	1132	LEU	0	-0.026	-0.025	16.202	1.080	1.080	0.000	0.000	0.000	0.000
12	A	1133	SER	0	-0.032	-0.017	18.210	1.075	1.075	0.000	0.000	0.000	0.000
13	A	1134	HIS	0	-0.052	-0.031	18.605	1.230	1.230	0.000	0.000	0.000	0.000
14	A	1135	CYS	0	-0.105	-0.045	19.393	0.307	0.307	0.000	0.000	0.000	0.000
15	A	1136	CYS	0	-0.012	-0.002	19.480	0.269	0.269	0.000	0.000	0.000	0.000
16	A	1137	LEU	0	-0.002	0.007	21.364	0.577	0.577	0.000	0.000	0.000	0.000
17	A	1138	ALA	0	-0.012	-0.007	23.771	-0.057	-0.057	0.000	0.000	0.000	0.000
18	A	1139	GLY	0	0.077	0.050	26.660	0.095	0.095	0.000	0.000	0.000	0.000
19	A	1140	LYS	1	0.989	0.964	29.167	8.062	8.062	0.000	0.000	0.000	0.000
20	A	1141	VAL	0	-0.013	-0.016	32.150	-0.040	-0.040	0.000	0.000	0.000	0.000
21	A	1142	ASN	0	0.012	0.018	26.638	-0.118	-0.118	0.000	0.000	0.000	0.000
22	A	1143	GLU	-1	-0.825	-0.915	26.208	-11.529	-11.529	0.000	0.000	0.000	0.000
23	A	1144	PRO	0	0.029	0.016	26.896	-0.290	-0.290	0.000	0.000	0.000	0.000
24	A	1145	GLN	0	-0.020	-0.014	24.699	0.171	0.171	0.000	0.000	0.000	0.000
25	A	1146	LYS	1	0.882	0.948	21.975	11.550	11.550	0.000	0.000	0.000	0.000
26	A	1147	ASN	0	0.046	0.013	22.135	-0.830	-0.830	0.000	0.000	0.000	0.000
27	A	1148	ARG	1	0.984	1.012	22.956	10.366	10.366	0.000	0.000	0.000	0.000
28	A	1149	ILE	0	-0.042	-0.027	18.683	-0.256	-0.256	0.000	0.000	0.000	0.000
29	A	1150	LEU	0	-0.025	-0.017	17.613	-0.747	-0.747	0.000	0.000	0.000	0.000
30	A	1151	GLU	-1	-0.849	-0.922	18.242	-12.021	-12.021	0.000	0.000	0.000	0.000
31	A	1152	GLU	-1	-0.975	-1.000	19.152	-13.153	-13.153	0.000	0.000	0.000	0.000
32	A	1153	ILE	0	-0.075	-0.034	13.195	-0.719	-0.719	0.000	0.000	0.000	0.000
33	A	1154	GLU	-1	-0.941	-0.979	14.375	-17.013	-17.013	0.000	0.000	0.000	0.000
34	A	1155	LYS	1	0.890	0.961	15.656	12.280	12.280	0.000	0.000	0.000	0.000
35	A	1156	SER	0	-0.034	0.005	13.733	-0.192	-0.192	0.000	0.000	0.000	0.000
36	A	1157	LYS	1	0.949	0.962	12.013	14.749	14.749	0.000	0.000	0.000	0.000
37	A	1158	ALA	0	-0.011	0.016	10.077	-1.288	-1.288	0.000	0.000	0.000	0.000
38	A	1159	ASN	0	0.044	0.017	4.803	1.011	1.011	0.000	0.000	0.000	0.000
39	A	1160	HIS	0	-0.022	-0.028	6.275	-3.748	-3.748	0.000	0.000	0.000	0.000
40	A	1161	PHE	0	0.024	0.006	7.429	2.769	2.769	0.000	0.000	0.000	0.000
41	A	1162	LEU	0	0.017	0.006	10.105	-1.097	-1.097	0.000	0.000	0.000	0.000
42	A	1163	ILE	0	-0.008	-0.006	12.736	1.170	1.170	0.000	0.000	0.000	0.000
43	A	1164	LEU	0	-0.021	0.014	16.086	-0.206	-0.206	0.000	0.000	0.000	0.000
44	A	1165	PHE	0	0.037	0.001	18.001	0.477	0.477	0.000	0.000	0.000	0.000
45	A	1166	ARG	1	0.909	0.948	21.773	10.652	10.652	0.000	0.000	0.000	0.000
46	A	1167	ASP	-1	-0.805	-0.885	24.915	-10.787	-10.787	0.000	0.000	0.000	0.000
47	A	1168	SER	0	0.009	0.002	23.333	-0.341	-0.341	0.000	0.000	0.000	0.000
48	A	1169	SER	0	-0.052	-0.039	24.106	-0.175	-0.175	0.000	0.000	0.000	0.000
49	A	1170	CYS	0	-0.092	-0.044	20.403	-0.125	-0.125	0.000	0.000	0.000	0.000
50	A	1171	GLN	0	0.000	0.012	22.628	0.019	0.019	0.000	0.000	0.000	0.000
51	A	1172	PHE	0	0.006	-0.014	18.802	-0.091	-0.091	0.000	0.000	0.000	0.000
52	A	1173	ARG	1	0.879	0.964	21.884	11.358	11.358	0.000	0.000	0.000	0.000
53	A	1174	ALA	0	0.003	-0.001	20.926	0.412	0.412	0.000	0.000	0.000	0.000
54	A	1175	LEU	0	-0.008	0.014	14.137	-0.561	-0.561	0.000	0.000	0.000	0.000
55	A	1176	TYR	0	-0.004	-0.032	15.342	0.836	0.836	0.000	0.000	0.000	0.000
56	A	1177	THR	0	-0.017	-0.003	12.220	-1.041	-1.041	0.000	0.000	0.000	0.000
57	A	1178	LEU	0	0.004	-0.001	8.988	1.124	1.124	0.000	0.000	0.000	0.000
58	A	1179	SER	0	0.004	0.020	10.487	-1.807	-1.807	0.000	0.000	0.000	0.000
59	A	1180	GLY	0	-0.017	-0.024	9.797	0.137	0.137	0.000	0.000	0.000	0.000
60	A	1181	GLU	-1	-0.936	-0.963	10.694	-17.057	-17.057	0.000	0.000	0.000	0.000
61	A	1182	THR	0	0.010	-0.004	13.684	0.333	0.333	0.000	0.000	0.000	0.000
62	A	1183	GLU	-1	-0.959	-0.971	13.535	-18.381	-18.381	0.000	0.000	0.000	0.000
63	A	1184	GLU	-1	-0.980	-0.983	14.667	-13.852	-13.852	0.000	0.000	0.000	0.000
64	A	1185	LEU	0	-0.035	-0.025	13.265	-1.018	-1.018	0.000	0.000	0.000	0.000
65	A	1186	SER	0	0.018	-0.002	15.941	1.373	1.373	0.000	0.000	0.000	0.000
66	A	1187	ARG	1	0.832	0.907	17.124	11.305	11.305	0.000	0.000	0.000	0.000
67	A	1188	LEU	0	-0.056	-0.026	15.367	0.159	0.159	0.000	0.000	0.000	0.000
68	A	1189	ALA	0	0.026	0.009	18.921	0.603	0.603	0.000	0.000	0.000	0.000
69	A	1190	GLY	0	-0.014	-0.007	21.097	-0.363	-0.363	0.000	0.000	0.000	0.000
70	A	1191	TYR	0	-0.011	-0.016	23.664	0.255	0.255	0.000	0.000	0.000	0.000
71	A	1192	GLY	0	0.085	0.025	23.452	-0.203	-0.203	0.000	0.000	0.000	0.000
72	A	1193	PRO	0	0.051	0.045	23.270	0.282	0.282	0.000	0.000	0.000	0.000
73	A	1194	ARG	1	0.936	0.985	22.085	12.000	12.000	0.000	0.000	0.000	0.000
74	A	1195	THR	0	0.060	0.022	20.150	-0.392	-0.392	0.000	0.000	0.000	0.000
75	A	1196	VAL	0	-0.039	-0.011	18.855	0.583	0.583	0.000	0.000	0.000	0.000
76	A	1197	THR	0	0.101	0.032	18.553	-0.775	-0.775	0.000	0.000	0.000	0.000
77	A	1198	PRO	0	0.078	0.014	16.912	0.231	0.231	0.000	0.000	0.000	0.000
78	A	1199	ALA	0	0.010	0.014	19.121	0.099	0.099	0.000	0.000	0.000	0.000
79	A	1200	MET	0	-0.055	-0.003	22.121	0.364	0.364	0.000	0.000	0.000	0.000
80	A	1201	VAL	0	-0.025	-0.006	17.105	0.209	0.209	0.000	0.000	0.000	0.000
81	A	1202	GLU	-1	-0.958	-0.971	20.417	-11.807	-11.807	0.000	0.000	0.000	0.000
82	A	1203	GLY	0	-0.003	0.007	19.856	-0.312	-0.312	0.000	0.000	0.000	0.000
83	A	1204	ILE	0	-0.008	-0.014	13.324	-0.561	-0.561	0.000	0.000	0.000	0.000
84	A	1205	TYR	0	0.016	-0.010	14.808	0.487	0.487	0.000	0.000	0.000	0.000
85	A	1206	LYS	1	0.986	0.998	11.217	20.386	20.386	0.000	0.000	0.000	0.000
86	A	1207	TYR	0	0.013	0.002	11.856	2.176	2.176	0.000	0.000	0.000	0.000
87	A	1208	ASN	0	-0.038	-0.022	12.624	-1.105	-1.105	0.000	0.000	0.000	0.000
88	A	1209	SER	0	0.069	0.016	14.269	0.927	0.927	0.000	0.000	0.000	0.000
89	A	1210	ASP	-1	-0.880	-0.926	16.013	-15.833	-15.833	0.000	0.000	0.000	0.000
90	A	1211	ARG	1	0.877	0.928	18.588	15.174	15.174	0.000	0.000	0.000	0.000
91	A	1212	LYS	1	0.913	0.987	19.022	13.680	13.680	0.000	0.000	0.000	0.000
92	A	1213	ARG	1	0.945	0.971	18.548	14.420	14.420	0.000	0.000	0.000	0.000
93	A	1214	PHE	0	0.075	0.036	14.505	-0.853	-0.853	0.000	0.000	0.000	0.000
94	A	1215	THR	0	-0.128	-0.070	15.720	0.871	0.871	0.000	0.000	0.000	0.000
95	A	1216	GLN	0	0.060	0.028	16.126	-0.755	-0.755	0.000	0.000	0.000	0.000
96	A	1217	ILE	0	-0.089	-0.042	11.550	-0.435	-0.435	0.000	0.000	0.000	0.000
97	A	1218	PRO	0	0.003	-0.009	15.565	0.472	0.472	0.000	0.000	0.000	0.000
98	A	1219	ALA	0	0.044	0.025	16.007	-1.070	-1.070	0.000	0.000	0.000	0.000
99	A	1220	LYS	1	0.908	0.964	9.258	28.613	28.613	0.000	0.000	0.000	0.000
100	A	1221	THR	0	0.055	0.025	11.851	0.716	0.716	0.000	0.000	0.000	0.000
101	A	1222	MET	0	0.036	0.037	10.387	-2.241	-2.241	0.000	0.000	0.000	0.000
102	A	1223	SER	0	0.009	-0.013	6.569	-2.191	-2.191	0.000	0.000	0.000	0.000
103	A	1224	MET	0	0.012	0.011	2.045	-1.224	-0.702	3.147	-1.057	-2.612	-0.002
104	A	1225	SER	0	-0.038	-0.015	5.045	2.404	2.485	-0.001	-0.005	-0.075	0.000
105	A	1226	VAL	0	-0.039	-0.001	6.756	2.833	2.833	0.000	0.000	0.000	0.000
106	A	1227	ASP	-1	-0.778	-0.887	8.997	-28.391	-28.391	0.000	0.000	0.000	0.000
107	A	1228	ALA	0	-0.018	-0.014	11.253	1.037	1.037	0.000	0.000	0.000	0.000
108	A	1229	PHE	0	-0.005	-0.007	14.808	-0.616	-0.616	0.000	0.000	0.000	0.000
109	A	1230	THR	0	0.053	0.043	17.431	0.275	0.275	0.000	0.000	0.000	0.000
110	A	1231	ILE	0	0.006	0.001	20.761	-0.507	-0.507	0.000	0.000	0.000	0.000
111	A	1232	GLN	0	0.066	0.036	23.107	0.757	0.757	0.000	0.000	0.000	0.000
112	A	1233	GLY	0	0.012	-0.006	26.414	0.146	0.146	0.000	0.000	0.000	0.000
113	A	1234	HIS	0	-0.003	-0.010	29.267	0.140	0.140	0.000	0.000	0.000	0.000
114	A	1235	LEU	0	-0.032	-0.008	25.263	0.167	0.167	0.000	0.000	0.000	0.000
115	A	1236	TRP	0	-0.030	-0.001	24.219	0.186	0.186	0.000	0.000	0.000	0.000

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