FMO DATABASE

FMODB ID: 5J9LZ

Calculation Name: 4UMS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4UMS

Chain ID: A

ChEMBL ID:

UniProt ID: Q6A564

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	154
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1336381.391391
FMO2-HF: Nuclear repulsion	1277478.777718
FMO2-HF: Total energy	-58902.613673
FMO2-MP2: Total energy	-59073.048814

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:1039:MET)

Summations of interaction energy for fragment #1(A:1039:MET)

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.
-7.674	-11.441	13.091	4.054	-13.378	-0.061

Interaction energy analysis for fragmet #1(A:1039:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : 0.020

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	1041	TRP	0	0.032	0.007	2.533	4.913	-2.631	1.392	9.644	-3.493	-0.026
4	A	1042	MET	0	0.003	0.025	4.983	0.022	0.077	-0.001	-0.010	-0.043	0.000
5	A	1043	ASN	0	-0.042	-0.029	8.283	0.158	0.158	0.000	0.000	0.000	0.000
6	A	1044	VAL	0	0.003	0.001	11.161	0.033	0.033	0.000	0.000	0.000	0.000
7	A	1045	VAL	0	-0.005	-0.001	13.437	0.050	0.050	0.000	0.000	0.000	0.000
8	A	1046	ILE	0	-0.037	-0.010	16.834	0.017	0.017	0.000	0.000	0.000	0.000
9	A	1047	GLY	0	0.038	0.015	19.510	0.017	0.017	0.000	0.000	0.000	0.000
10	A	1048	LYS	1	0.916	0.970	22.199	0.278	0.278	0.000	0.000	0.000	0.000
11	A	1049	MET	0	-0.018	0.002	25.585	0.000	0.000	0.000	0.000	0.000	0.000
12	A	1050	ASN	0	-0.016	-0.015	28.944	0.005	0.005	0.000	0.000	0.000	0.000
13	A	1051	ALA	0	0.024	0.010	32.596	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	1052	GLU	-1	-0.811	-0.869	35.088	-0.110	-0.110	0.000	0.000	0.000	0.000
15	A	1053	VAL	0	0.046	0.013	38.202	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	1054	GLY	0	-0.006	0.003	39.387	0.004	0.004	0.000	0.000	0.000	0.000
17	A	1055	GLY	0	-0.020	-0.003	38.714	0.001	0.001	0.000	0.000	0.000	0.000
18	A	1056	GLU	-1	-0.871	-0.937	35.278	-0.138	-0.138	0.000	0.000	0.000	0.000
19	A	1057	VAL	0	0.014	0.002	30.208	0.000	0.000	0.000	0.000	0.000	0.000
20	A	1058	VAL	0	0.015	0.008	28.093	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	1059	VAL	0	-0.007	-0.010	23.662	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	1060	PRO	0	-0.032	0.005	22.852	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	1061	ILE	0	-0.004	-0.015	17.439	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	1062	GLU	-1	-0.910	-0.965	18.205	-0.409	-0.409	0.000	0.000	0.000	0.000
25	A	1063	PHE	0	0.023	0.012	13.374	-0.080	-0.080	0.000	0.000	0.000	0.000
26	A	1064	ASN	0	-0.007	-0.021	13.591	0.037	0.037	0.000	0.000	0.000	0.000
27	A	1065	ASN	0	-0.005	-0.015	10.624	-0.109	-0.109	0.000	0.000	0.000	0.000
28	A	1066	VAL	0	-0.002	0.013	9.278	-0.306	-0.306	0.000	0.000	0.000	0.000
29	A	1067	PRO	0	0.048	0.025	4.843	0.096	0.096	0.000	0.000	0.000	0.000
30	A	1068	SER	0	-0.001	-0.005	7.019	0.263	0.263	0.000	0.000	0.000	0.000
31	A	1069	PHE	0	-0.043	-0.016	2.265	-0.249	0.837	1.292	-0.792	-1.586	-0.004
32	A	1070	GLY	0	0.043	0.037	7.677	0.283	0.283	0.000	0.000	0.000	0.000
33	A	1071	ILE	0	-0.070	-0.044	7.712	-0.217	-0.217	0.000	0.000	0.000	0.000
34	A	1072	ASN	0	0.030	0.008	9.571	0.181	0.181	0.000	0.000	0.000	0.000
35	A	1073	ASN	0	-0.006	-0.016	10.673	0.148	0.148	0.000	0.000	0.000	0.000
36	A	1074	CYS	0	-0.048	-0.019	10.693	-0.167	-0.167	0.000	0.000	0.000	0.000
37	A	1075	ASP	-1	-0.842	-0.897	12.711	-0.423	-0.423	0.000	0.000	0.000	0.000
38	A	1076	PHE	0	0.022	0.000	13.150	-0.098	-0.098	0.000	0.000	0.000	0.000
39	A	1077	LYS	1	0.853	0.928	15.252	0.315	0.315	0.000	0.000	0.000	0.000
40	A	1078	LEU	0	-0.025	0.001	17.299	-0.034	-0.034	0.000	0.000	0.000	0.000
41	A	1079	VAL	0	-0.001	0.000	20.058	0.029	0.029	0.000	0.000	0.000	0.000
42	A	1080	TYR	0	0.035	0.014	23.028	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	1081	ASP	-1	-0.792	-0.893	26.190	-0.137	-0.137	0.000	0.000	0.000	0.000
44	A	1082	ALA	0	0.030	0.007	29.617	0.003	0.003	0.000	0.000	0.000	0.000
45	A	1083	THR	0	-0.025	-0.011	31.804	0.010	0.010	0.000	0.000	0.000	0.000
46	A	1084	ALA	0	-0.032	0.005	32.717	0.007	0.007	0.000	0.000	0.000	0.000
47	A	1085	LEU	0	-0.030	-0.015	29.420	0.002	0.002	0.000	0.000	0.000	0.000
48	A	1086	GLU	-1	-0.805	-0.896	32.934	-0.126	-0.126	0.000	0.000	0.000	0.000
49	A	1087	LEU	0	-0.031	-0.016	27.812	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	1088	LYS	1	0.789	0.897	31.464	0.139	0.139	0.000	0.000	0.000	0.000
51	A	1089	ASN	0	-0.037	-0.023	30.584	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	1090	VAL	0	0.017	0.002	24.153	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	1091	GLU	-1	-0.957	-0.958	26.607	-0.201	-0.201	0.000	0.000	0.000	0.000
54	A	1092	ALA	0	-0.018	-0.014	22.766	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	1093	GLY	0	-0.017	-0.016	21.843	0.021	0.021	0.000	0.000	0.000	0.000
56	A	1094	ASP	-1	-0.903	-0.961	22.183	-0.335	-0.335	0.000	0.000	0.000	0.000
57	A	1095	ILE	0	-0.044	0.002	15.758	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	1096	ILE	0	-0.067	-0.019	17.962	-0.023	-0.023	0.000	0.000	0.000	0.000
59	A	1097	LYS	1	0.871	0.947	17.253	0.402	0.402	0.000	0.000	0.000	0.000
60	A	1098	THR	0	-0.010	-0.033	21.089	0.000	0.000	0.000	0.000	0.000	0.000
61	A	1099	PRO	0	0.080	0.030	22.420	0.005	0.005	0.000	0.000	0.000	0.000
62	A	1100	LEU	0	-0.024	-0.010	23.472	0.000	0.000	0.000	0.000	0.000	0.000
63	A	1101	ALA	0	-0.033	-0.009	23.772	0.009	0.009	0.000	0.000	0.000	0.000
64	A	1102	ASN	0	0.022	0.008	19.051	0.024	0.024	0.000	0.000	0.000	0.000
65	A	1103	PHE	0	0.007	0.000	19.470	-0.030	-0.030	0.000	0.000	0.000	0.000
66	A	1104	SER	0	-0.003	0.007	21.311	0.034	0.034	0.000	0.000	0.000	0.000
67	A	1105	ASN	0	0.015	0.002	21.912	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	1106	ASN	0	0.027	0.032	23.869	0.033	0.033	0.000	0.000	0.000	0.000
69	A	1107	LYS	1	0.926	0.945	25.035	0.184	0.184	0.000	0.000	0.000	0.000
70	A	1108	SER	0	-0.030	-0.024	27.614	0.009	0.009	0.000	0.000	0.000	0.000
71	A	1109	GLU	-1	-0.847	-0.898	24.576	-0.197	-0.197	0.000	0.000	0.000	0.000
72	A	1110	GLU	-1	-0.876	-0.951	27.696	-0.144	-0.144	0.000	0.000	0.000	0.000
73	A	1111	GLY	0	0.011	0.000	28.107	0.001	0.001	0.000	0.000	0.000	0.000
74	A	1112	LYS	1	0.796	0.899	22.248	0.215	0.215	0.000	0.000	0.000	0.000
75	A	1113	ILE	0	-0.004	0.003	22.774	0.015	0.015	0.000	0.000	0.000	0.000
76	A	1114	SER	0	-0.019	-0.004	19.673	-0.030	-0.030	0.000	0.000	0.000	0.000
77	A	1115	PHE	0	-0.009	-0.020	17.795	0.037	0.037	0.000	0.000	0.000	0.000
78	A	1116	LEU	0	0.004	0.000	17.039	-0.036	-0.036	0.000	0.000	0.000	0.000
79	A	1117	PHE	0	-0.014	-0.015	13.327	0.034	0.034	0.000	0.000	0.000	0.000
80	A	1118	ASN	0	0.013	-0.012	15.451	-0.039	-0.039	0.000	0.000	0.000	0.000
81	A	1119	ASP	-1	-0.713	-0.806	15.455	-0.192	-0.192	0.000	0.000	0.000	0.000
82	A	1120	ALA	0	0.013	0.001	17.155	0.038	0.038	0.000	0.000	0.000	0.000
83	A	1121	SER	0	-0.088	-0.075	19.237	0.032	0.032	0.000	0.000	0.000	0.000
84	A	1122	GLN	0	-0.105	-0.050	16.404	0.052	0.052	0.000	0.000	0.000	0.000
85	A	1123	GLY	0	0.036	0.003	14.998	0.049	0.049	0.000	0.000	0.000	0.000
86	A	1124	SER	0	-0.048	-0.016	16.084	-0.023	-0.023	0.000	0.000	0.000	0.000
87	A	1125	MET	0	-0.129	-0.058	17.721	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	1126	GLN	0	0.033	0.013	11.777	-0.039	-0.039	0.000	0.000	0.000	0.000
89	A	1127	ILE	0	-0.002	0.014	12.878	0.026	0.026	0.000	0.000	0.000	0.000
90	A	1128	GLU	-1	-0.834	-0.933	12.092	-0.593	-0.593	0.000	0.000	0.000	0.000
91	A	1129	ASN	0	-0.067	-0.053	13.277	-0.042	-0.042	0.000	0.000	0.000	0.000
92	A	1130	GLY	0	0.021	0.020	14.770	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	1131	GLY	0	0.028	0.011	15.610	0.071	0.071	0.000	0.000	0.000	0.000
94	A	1132	VAL	0	-0.011	-0.012	18.333	-0.036	-0.036	0.000	0.000	0.000	0.000
95	A	1133	PHE	0	0.054	0.027	16.006	0.010	0.010	0.000	0.000	0.000	0.000
96	A	1134	ALA	0	-0.007	-0.013	18.952	0.032	0.032	0.000	0.000	0.000	0.000
97	A	1135	LYS	1	0.939	0.980	22.170	0.269	0.269	0.000	0.000	0.000	0.000
98	A	1136	ILE	0	0.026	0.017	22.386	0.010	0.010	0.000	0.000	0.000	0.000
99	A	1137	THR	0	0.001	0.012	26.562	0.004	0.004	0.000	0.000	0.000	0.000
100	A	1138	PHE	0	0.013	-0.015	26.233	0.002	0.002	0.000	0.000	0.000	0.000
101	A	1139	LYS	1	0.852	0.918	31.784	0.122	0.122	0.000	0.000	0.000	0.000
102	A	1140	VAL	0	-0.025	-0.010	34.192	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	1141	LYS	1	0.880	0.945	35.482	0.134	0.134	0.000	0.000	0.000	0.000
104	A	1142	SER	0	0.026	-0.006	38.619	0.000	0.000	0.000	0.000	0.000	0.000
105	A	1143	THR	0	0.001	-0.004	40.212	0.003	0.003	0.000	0.000	0.000	0.000
106	A	1144	THR	0	-0.079	-0.030	35.613	0.004	0.004	0.000	0.000	0.000	0.000
107	A	1145	ALA	0	0.035	0.028	38.398	0.003	0.003	0.000	0.000	0.000	0.000
108	A	1146	THR	0	0.033	0.023	37.342	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	1147	GLY	0	-0.023	-0.012	35.225	0.005	0.005	0.000	0.000	0.000	0.000
110	A	1148	VAL	0	-0.028	-0.015	28.672	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	1149	TYR	0	-0.018	-0.019	29.523	0.003	0.003	0.000	0.000	0.000	0.000
112	A	1150	ASP	-1	-0.816	-0.896	24.078	-0.226	-0.226	0.000	0.000	0.000	0.000
113	A	1151	LEU	0	-0.044	-0.019	23.057	0.004	0.004	0.000	0.000	0.000	0.000
114	A	1152	ARG	1	0.810	0.874	19.638	0.204	0.204	0.000	0.000	0.000	0.000
115	A	1153	LYS	1	0.950	0.964	12.596	0.544	0.544	0.000	0.000	0.000	0.000
116	A	1154	ASP	-1	-0.849	-0.910	16.904	-0.255	-0.255	0.000	0.000	0.000	0.000
117	A	1155	LEU	0	-0.018	-0.014	15.040	-0.054	-0.054	0.000	0.000	0.000	0.000
118	A	1156	VAL	0	-0.039	-0.025	9.742	0.007	0.007	0.000	0.000	0.000	0.000
119	A	1157	GLY	0	0.026	0.028	12.079	0.052	0.052	0.000	0.000	0.000	0.000
120	A	1158	SER	0	-0.044	-0.023	8.849	-0.210	-0.210	0.000	0.000	0.000	0.000
121	A	1159	PHE	0	0.026	0.005	7.249	0.137	0.137	0.000	0.000	0.000	0.000
122	A	1160	SER	0	-0.045	-0.040	6.271	-0.279	-0.279	0.000	0.000	0.000	0.000
123	A	1161	GLY	0	0.081	0.052	6.112	-0.132	-0.132	0.000	0.000	0.000	0.000
124	A	1162	LEU	0	-0.007	0.011	7.150	0.613	0.613	0.000	0.000	0.000	0.000
125	A	1163	LYS	1	0.886	0.940	4.096	-6.603	-6.270	0.000	-0.137	-0.196	0.001
126	A	1164	ASP	-1	-0.788	-0.909	6.799	0.499	0.499	0.000	0.000	0.000	0.000
127	A	1165	ASN	0	-0.014	-0.008	10.219	0.018	0.018	0.000	0.000	0.000	0.000
128	A	1166	LYS	1	0.806	0.910	8.699	-0.854	-0.854	0.000	0.000	0.000	0.000
129	A	1167	MET	0	0.052	0.032	7.835	0.284	0.284	0.000	0.000	0.000	0.000
130	A	1168	THR	0	-0.046	-0.011	2.392	0.948	0.981	2.900	-1.082	-1.851	0.005
131	A	1169	SER	0	0.010	0.015	3.184	-2.153	-1.446	0.024	-0.186	-0.545	0.000
132	A	1170	ILE	0	-0.014	-0.023	2.413	-3.874	-3.160	7.151	-3.200	-4.665	-0.036
133	A	1171	GLY	0	0.014	0.018	2.597	-0.196	0.621	0.325	-0.210	-0.932	-0.001
134	A	1172	ALA	0	0.014	0.003	3.692	0.453	0.485	0.008	0.027	-0.067	0.000
135	A	1173	GLU	-1	-0.882	-0.946	7.157	-0.891	-0.891	0.000	0.000	0.000	0.000
136	A	1174	PHE	0	-0.023	-0.018	9.323	0.079	0.079	0.000	0.000	0.000	0.000
137	A	1175	THR	0	-0.011	0.007	12.856	0.043	0.043	0.000	0.000	0.000	0.000
138	A	1176	ASN	0	0.012	0.005	16.111	-0.022	-0.022	0.000	0.000	0.000	0.000
139	A	1177	GLY	0	0.061	0.015	18.998	0.009	0.009	0.000	0.000	0.000	0.000
140	A	1178	SER	0	-0.066	-0.037	22.261	0.008	0.008	0.000	0.000	0.000	0.000
141	A	1179	ILE	0	0.028	0.032	25.846	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	1180	THR	0	-0.032	-0.020	29.301	0.006	0.006	0.000	0.000	0.000	0.000
143	A	1181	VAL	0	-0.013	0.003	31.982	0.001	0.001	0.000	0.000	0.000	0.000
144	A	1182	ALA	0	-0.004	-0.013	35.346	0.005	0.005	0.000	0.000	0.000	0.000
145	A	1183	ALA	0	-0.002	-0.010	38.200	0.001	0.001	0.000	0.000	0.000	0.000
146	A	1184	THR	0	-0.013	-0.030	41.932	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	1185	ALA	0	-0.047	-0.017	43.566	0.004	0.004	0.000	0.000	0.000	0.000
148	A	1186	PRO	0	0.008	0.005	46.179	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	1187	LEU	0	0.013	-0.005	47.038	0.000	0.000	0.000	0.000	0.000	0.000
150	A	1188	GLU	-1	-0.899	-0.919	50.374	-0.059	-0.059	0.000	0.000	0.000	0.000
151	A	1189	HIS	0	-0.051	-0.034	51.771	0.001	0.001	0.000	0.000	0.000	0.000
152	A	1190	HIS	0	-0.034	-0.038	55.032	0.002	0.002	0.000	0.000	0.000	0.000
153	A	1191	HIS	0	-0.020	-0.008	56.151	0.001	0.001	0.000	0.000	0.000	0.000
154	A	1192	HIS	0	-0.006	0.009	59.262	0.002	0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1039:MET)