FMO DATABASE

FMODB ID: K9153

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

Total energy (hartree)

FMO2-HF: Electronic energy	-974980.105454
FMO2-HF: Nuclear repulsion	928396.04778
FMO2-HF: Total energy	-46584.057674
FMO2-MP2: Total energy	-46717.906031

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.
50.659	53.705	3.686	-2.548	-4.183	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	0.016	0.003	3.816	-4.579	-1.847	-0.023	-1.485	-1.223	0.005
4	A	1125	LYS	1	0.911	0.970	6.116	23.348	23.348	0.000	0.000	0.000	0.000
5	A	1126	PHE	0	0.022	0.009	7.779	1.678	1.678	0.000	0.000	0.000	0.000
6	A	1127	ILE	0	0.010	0.007	7.443	1.691	1.691	0.000	0.000	0.000	0.000
7	A	1128	ILE	0	0.013	0.008	10.200	1.890	1.890	0.000	0.000	0.000	0.000
8	A	1129	HIS	0	0.058	0.036	12.343	1.215	1.215	0.000	0.000	0.000	0.000
9	A	1130	ASN	0	0.008	0.004	13.888	2.118	2.118	0.000	0.000	0.000	0.000
10	A	1131	ALA	0	0.023	0.005	14.717	1.031	1.031	0.000	0.000	0.000	0.000
11	A	1132	LEU	0	-0.030	-0.029	16.344	1.043	1.043	0.000	0.000	0.000	0.000
12	A	1133	SER	0	-0.028	-0.012	18.221	1.049	1.049	0.000	0.000	0.000	0.000
13	A	1134	HIS	0	-0.054	-0.030	18.444	1.157	1.157	0.000	0.000	0.000	0.000
14	A	1135	CYS	0	-0.100	-0.042	19.513	0.330	0.330	0.000	0.000	0.000	0.000
15	A	1136	CYS	0	-0.011	0.002	19.555	0.265	0.265	0.000	0.000	0.000	0.000
16	A	1137	LEU	0	-0.015	-0.004	21.296	0.579	0.579	0.000	0.000	0.000	0.000
17	A	1138	ALA	0	0.024	0.019	23.817	-0.072	-0.072	0.000	0.000	0.000	0.000
18	A	1139	GLY	0	0.032	0.028	26.365	0.270	0.270	0.000	0.000	0.000	0.000
19	A	1140	LYS	1	0.998	0.978	28.954	8.047	8.047	0.000	0.000	0.000	0.000
20	A	1141	VAL	0	-0.014	-0.015	32.169	-0.024	-0.024	0.000	0.000	0.000	0.000
21	A	1142	ASN	0	0.011	0.006	26.341	-0.069	-0.069	0.000	0.000	0.000	0.000
22	A	1143	GLU	-1	-0.742	-0.849	26.756	-11.399	-11.399	0.000	0.000	0.000	0.000
23	A	1144	PRO	0	0.011	0.005	26.961	-0.301	-0.301	0.000	0.000	0.000	0.000
24	A	1145	GLN	0	-0.030	-0.016	25.255	0.004	0.004	0.000	0.000	0.000	0.000
25	A	1146	LYS	1	0.872	0.932	22.090	11.444	11.444	0.000	0.000	0.000	0.000
26	A	1147	ASN	0	0.003	-0.025	22.215	-0.880	-0.880	0.000	0.000	0.000	0.000
27	A	1148	ARG	1	1.000	1.020	23.025	10.295	10.295	0.000	0.000	0.000	0.000
28	A	1149	ILE	0	-0.034	-0.025	18.814	-0.275	-0.275	0.000	0.000	0.000	0.000
29	A	1150	LEU	0	-0.006	-0.007	17.592	-0.691	-0.691	0.000	0.000	0.000	0.000
30	A	1151	GLU	-1	-0.886	-0.945	18.241	-12.006	-12.006	0.000	0.000	0.000	0.000
31	A	1152	GLU	-1	-0.899	-0.945	19.259	-12.957	-12.957	0.000	0.000	0.000	0.000
32	A	1153	ILE	0	-0.080	-0.033	13.243	-0.659	-0.659	0.000	0.000	0.000	0.000
33	A	1154	GLU	-1	-0.878	-0.949	14.375	-18.027	-18.027	0.000	0.000	0.000	0.000
34	A	1155	LYS	1	0.819	0.913	15.608	12.289	12.289	0.000	0.000	0.000	0.000
35	A	1156	SER	0	-0.038	-0.002	13.896	-0.200	-0.200	0.000	0.000	0.000	0.000
36	A	1157	LYS	1	0.948	0.962	11.944	14.809	14.809	0.000	0.000	0.000	0.000
37	A	1158	ALA	0	-0.012	0.018	10.104	-1.339	-1.339	0.000	0.000	0.000	0.000
38	A	1159	ASN	0	0.049	0.017	4.844	0.257	0.257	0.000	0.000	0.000	0.000
39	A	1160	HIS	0	-0.034	-0.025	6.287	-3.495	-3.495	0.000	0.000	0.000	0.000
40	A	1161	PHE	0	0.021	0.000	7.646	2.740	2.740	0.000	0.000	0.000	0.000
41	A	1162	LEU	0	0.014	0.003	10.252	-0.923	-0.923	0.000	0.000	0.000	0.000
42	A	1163	ILE	0	-0.015	-0.010	12.891	1.097	1.097	0.000	0.000	0.000	0.000
43	A	1164	LEU	0	-0.021	0.017	16.214	-0.182	-0.182	0.000	0.000	0.000	0.000
44	A	1165	PHE	0	0.033	-0.003	18.167	0.440	0.440	0.000	0.000	0.000	0.000
45	A	1166	ARG	1	0.907	0.948	21.888	10.489	10.489	0.000	0.000	0.000	0.000
46	A	1167	ASP	-1	-0.791	-0.872	25.027	-10.623	-10.623	0.000	0.000	0.000	0.000
47	A	1168	SER	0	0.054	0.022	23.661	-0.306	-0.306	0.000	0.000	0.000	0.000
48	A	1169	SER	0	-0.063	-0.049	24.451	-0.221	-0.221	0.000	0.000	0.000	0.000
49	A	1170	CYS	0	-0.108	-0.051	21.188	-0.256	-0.256	0.000	0.000	0.000	0.000
50	A	1171	GLN	0	-0.014	0.002	22.812	0.021	0.021	0.000	0.000	0.000	0.000
51	A	1172	PHE	0	0.010	-0.015	18.845	-0.108	-0.108	0.000	0.000	0.000	0.000
52	A	1173	ARG	1	0.879	0.967	22.014	11.211	11.211	0.000	0.000	0.000	0.000
53	A	1174	ALA	0	0.008	0.001	21.083	0.392	0.392	0.000	0.000	0.000	0.000
54	A	1175	LEU	0	-0.003	0.013	14.318	-0.523	-0.523	0.000	0.000	0.000	0.000
55	A	1176	TYR	0	-0.003	-0.031	15.518	0.815	0.815	0.000	0.000	0.000	0.000
56	A	1177	THR	0	-0.014	-0.003	12.437	-0.945	-0.945	0.000	0.000	0.000	0.000
57	A	1178	LEU	0	-0.002	-0.001	8.957	1.157	1.157	0.000	0.000	0.000	0.000
58	A	1179	SER	0	0.006	0.019	10.486	-1.908	-1.908	0.000	0.000	0.000	0.000
59	A	1180	GLY	0	-0.017	-0.023	9.795	0.189	0.189	0.000	0.000	0.000	0.000
60	A	1181	GLU	-1	-0.946	-0.964	10.706	-17.233	-17.233	0.000	0.000	0.000	0.000
61	A	1182	THR	0	0.014	-0.008	13.686	0.352	0.352	0.000	0.000	0.000	0.000
62	A	1183	GLU	-1	-0.963	-0.971	13.608	-18.280	-18.280	0.000	0.000	0.000	0.000
63	A	1184	GLU	-1	-0.969	-0.978	14.683	-13.742	-13.742	0.000	0.000	0.000	0.000
64	A	1185	LEU	0	-0.036	-0.023	13.259	-1.012	-1.012	0.000	0.000	0.000	0.000
65	A	1186	SER	0	0.024	0.004	15.914	1.363	1.363	0.000	0.000	0.000	0.000
66	A	1187	ARG	1	0.830	0.907	17.302	11.151	11.151	0.000	0.000	0.000	0.000
67	A	1188	LEU	0	-0.049	-0.022	15.618	0.206	0.206	0.000	0.000	0.000	0.000
68	A	1189	ALA	0	0.016	0.002	19.121	0.589	0.589	0.000	0.000	0.000	0.000
69	A	1190	GLY	0	-0.003	0.000	21.271	-0.345	-0.345	0.000	0.000	0.000	0.000
70	A	1191	TYR	0	-0.010	-0.016	23.827	0.224	0.224	0.000	0.000	0.000	0.000
71	A	1192	GLY	0	0.079	0.025	23.640	-0.187	-0.187	0.000	0.000	0.000	0.000
72	A	1193	PRO	0	0.047	0.041	23.507	0.243	0.243	0.000	0.000	0.000	0.000
73	A	1194	ARG	1	0.911	0.972	21.381	12.161	12.161	0.000	0.000	0.000	0.000
74	A	1195	THR	0	0.066	0.023	20.090	-0.401	-0.401	0.000	0.000	0.000	0.000
75	A	1196	VAL	0	-0.042	-0.014	18.977	0.560	0.560	0.000	0.000	0.000	0.000
76	A	1197	THR	0	0.095	0.029	18.527	-0.749	-0.749	0.000	0.000	0.000	0.000
77	A	1198	PRO	0	0.086	0.019	16.883	0.242	0.242	0.000	0.000	0.000	0.000
78	A	1199	ALA	0	0.004	0.010	19.095	0.123	0.123	0.000	0.000	0.000	0.000
79	A	1200	MET	0	-0.056	0.002	22.004	0.349	0.349	0.000	0.000	0.000	0.000
80	A	1201	VAL	0	-0.018	-0.003	17.331	0.223	0.223	0.000	0.000	0.000	0.000
81	A	1202	GLU	-1	-0.903	-0.924	20.622	-11.835	-11.835	0.000	0.000	0.000	0.000
82	A	1203	GLY	0	-0.006	0.008	20.133	-0.303	-0.303	0.000	0.000	0.000	0.000
83	A	1204	ILE	0	-0.010	-0.011	13.854	-0.525	-0.525	0.000	0.000	0.000	0.000
84	A	1205	TYR	0	-0.007	-0.040	15.091	0.503	0.503	0.000	0.000	0.000	0.000
85	A	1206	LYS	1	0.954	0.975	11.480	18.636	18.636	0.000	0.000	0.000	0.000
86	A	1207	TYR	0	0.002	-0.004	12.260	2.026	2.026	0.000	0.000	0.000	0.000
87	A	1208	ASN	0	-0.042	-0.022	13.009	-0.663	-0.663	0.000	0.000	0.000	0.000
88	A	1209	SER	0	0.083	0.028	14.658	0.821	0.821	0.000	0.000	0.000	0.000
89	A	1210	ASP	-1	-0.904	-0.941	16.428	-15.965	-15.965	0.000	0.000	0.000	0.000
90	A	1211	ARG	1	0.907	0.939	18.959	14.629	14.629	0.000	0.000	0.000	0.000
91	A	1212	LYS	1	0.901	0.980	19.417	13.399	13.399	0.000	0.000	0.000	0.000
92	A	1213	ARG	1	0.953	0.970	18.976	13.997	13.997	0.000	0.000	0.000	0.000
93	A	1214	PHE	0	0.081	0.042	14.557	-0.789	-0.789	0.000	0.000	0.000	0.000
94	A	1215	THR	0	-0.090	-0.041	16.120	0.722	0.722	0.000	0.000	0.000	0.000
95	A	1216	GLN	0	0.073	0.052	16.414	-0.668	-0.668	0.000	0.000	0.000	0.000
96	A	1217	ILE	0	-0.093	-0.045	11.889	-0.322	-0.322	0.000	0.000	0.000	0.000
97	A	1218	PRO	0	0.016	0.000	15.924	0.466	0.466	0.000	0.000	0.000	0.000
98	A	1219	ALA	0	0.033	0.018	16.352	-0.996	-0.996	0.000	0.000	0.000	0.000
99	A	1220	LYS	1	0.903	0.958	9.593	27.245	27.245	0.000	0.000	0.000	0.000
100	A	1221	THR	0	0.065	0.029	12.250	0.633	0.633	0.000	0.000	0.000	0.000
101	A	1222	MET	0	0.051	0.042	10.513	-2.064	-2.064	0.000	0.000	0.000	0.000
102	A	1223	SER	0	0.020	-0.005	6.847	-1.482	-1.482	0.000	0.000	0.000	0.000
103	A	1224	MET	0	0.008	0.004	2.227	-2.288	-1.974	3.709	-1.063	-2.960	-0.005
104	A	1225	SER	0	-0.026	-0.017	5.431	2.020	2.020	0.000	0.000	0.000	0.000
105	A	1226	VAL	0	-0.052	-0.007	6.989	2.597	2.597	0.000	0.000	0.000	0.000
106	A	1227	ASP	-1	-0.775	-0.877	9.500	-26.744	-26.744	0.000	0.000	0.000	0.000
107	A	1228	ALA	0	-0.024	-0.019	11.401	0.925	0.925	0.000	0.000	0.000	0.000
108	A	1229	PHE	0	-0.010	-0.010	14.910	-0.562	-0.562	0.000	0.000	0.000	0.000
109	A	1230	THR	0	0.020	0.005	17.557	0.205	0.205	0.000	0.000	0.000	0.000
110	A	1231	ILE	0	0.002	0.001	20.910	-0.487	-0.487	0.000	0.000	0.000	0.000
111	A	1232	GLN	0	0.051	0.026	23.270	0.760	0.760	0.000	0.000	0.000	0.000
112	A	1233	GLY	0	0.003	-0.009	26.599	0.130	0.130	0.000	0.000	0.000	0.000
113	A	1234	HIS	0	0.003	-0.009	29.423	0.115	0.115	0.000	0.000	0.000	0.000
114	A	1235	LEU	0	-0.030	-0.006	25.356	0.164	0.164	0.000	0.000	0.000	0.000
115	A	1236	TRP	0	-0.033	-0.004	24.417	0.130	0.130	0.000	0.000	0.000	0.000

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