FMO DATABASE

FMODB ID: YVQK2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1337406.155918
FMO2-HF: Nuclear repulsion	1278503.148367
FMO2-HF: Total energy	-58903.007551
FMO2-MP2: Total energy	-59073.457957

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.
-15.047	-12.377	7.388	1.566	-11.622	-0.043

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 : -0.004 / q_NPA : 0.029

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	0.012	-0.004	2.537	2.405	-2.465	1.238	6.655	-3.023	-0.024
4	A	1042	MET	0	-0.004	0.029	5.232	-0.066	-0.028	-0.001	-0.008	-0.028	0.000
5	A	1043	ASN	0	-0.061	-0.036	8.501	0.150	0.150	0.000	0.000	0.000	0.000
6	A	1044	VAL	0	0.003	0.006	11.321	0.027	0.027	0.000	0.000	0.000	0.000
7	A	1045	VAL	0	-0.021	-0.014	13.739	0.049	0.049	0.000	0.000	0.000	0.000
8	A	1046	ILE	0	-0.025	0.000	17.320	0.015	0.015	0.000	0.000	0.000	0.000
9	A	1047	GLY	0	0.038	0.015	19.974	0.016	0.016	0.000	0.000	0.000	0.000
10	A	1048	LYS	1	0.878	0.950	22.581	0.312	0.312	0.000	0.000	0.000	0.000
11	A	1049	MET	0	-0.007	0.014	26.002	0.000	0.000	0.000	0.000	0.000	0.000
12	A	1050	ASN	0	-0.012	-0.011	29.435	0.004	0.004	0.000	0.000	0.000	0.000
13	A	1051	ALA	0	0.023	0.012	33.093	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	1052	GLU	-1	-0.811	-0.878	35.527	-0.121	-0.121	0.000	0.000	0.000	0.000
15	A	1053	VAL	0	0.036	0.008	38.678	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	1054	GLY	0	0.004	0.015	39.895	0.005	0.005	0.000	0.000	0.000	0.000
17	A	1055	GLY	0	-0.009	0.000	39.077	0.001	0.001	0.000	0.000	0.000	0.000
18	A	1056	GLU	-1	-0.853	-0.928	35.789	-0.148	-0.148	0.000	0.000	0.000	0.000
19	A	1057	VAL	0	0.004	-0.001	30.698	0.000	0.000	0.000	0.000	0.000	0.000
20	A	1058	VAL	0	0.020	0.012	28.500	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	1059	VAL	0	-0.016	-0.009	24.100	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	1060	PRO	0	-0.002	0.008	23.213	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	1061	ILE	0	-0.008	-0.009	17.848	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	1062	GLU	-1	-0.902	-0.953	18.585	-0.427	-0.427	0.000	0.000	0.000	0.000
25	A	1063	PHE	0	0.010	0.001	13.770	-0.081	-0.081	0.000	0.000	0.000	0.000
26	A	1064	ASN	0	0.001	-0.015	13.770	0.041	0.041	0.000	0.000	0.000	0.000
27	A	1065	ASN	0	-0.020	-0.027	10.765	-0.105	-0.105	0.000	0.000	0.000	0.000
28	A	1066	VAL	0	0.019	0.026	9.480	-0.327	-0.327	0.000	0.000	0.000	0.000
29	A	1067	PRO	0	0.036	0.018	5.117	0.176	0.176	0.000	0.000	0.000	0.000
30	A	1068	SER	0	-0.016	-0.012	7.291	0.254	0.254	0.000	0.000	0.000	0.000
31	A	1069	PHE	0	-0.033	-0.007	2.801	-0.273	0.842	0.269	-0.423	-0.961	-0.004
32	A	1070	GLY	0	0.044	0.032	8.085	0.236	0.236	0.000	0.000	0.000	0.000
33	A	1071	ILE	0	-0.063	-0.031	8.033	-0.319	-0.319	0.000	0.000	0.000	0.000
34	A	1072	ASN	0	0.054	0.021	9.694	0.207	0.207	0.000	0.000	0.000	0.000
35	A	1073	ASN	0	0.002	0.000	10.778	0.195	0.195	0.000	0.000	0.000	0.000
36	A	1074	CYS	0	-0.036	-0.009	10.807	-0.194	-0.194	0.000	0.000	0.000	0.000
37	A	1075	ASP	-1	-0.835	-0.895	12.560	-0.484	-0.484	0.000	0.000	0.000	0.000
38	A	1076	PHE	0	0.020	-0.004	13.159	-0.104	-0.104	0.000	0.000	0.000	0.000
39	A	1077	LYS	1	0.790	0.896	15.484	0.348	0.348	0.000	0.000	0.000	0.000
40	A	1078	LEU	0	-0.016	0.009	17.605	-0.041	-0.041	0.000	0.000	0.000	0.000
41	A	1079	VAL	0	-0.001	-0.016	20.240	0.031	0.031	0.000	0.000	0.000	0.000
42	A	1080	TYR	0	0.012	0.005	23.299	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	1081	ASP	-1	-0.769	-0.872	26.515	-0.149	-0.149	0.000	0.000	0.000	0.000
44	A	1082	ALA	0	0.029	0.007	29.955	0.002	0.002	0.000	0.000	0.000	0.000
45	A	1083	THR	0	-0.071	-0.042	32.100	0.011	0.011	0.000	0.000	0.000	0.000
46	A	1084	ALA	0	0.004	0.011	32.918	0.006	0.006	0.000	0.000	0.000	0.000
47	A	1085	LEU	0	-0.031	-0.006	29.669	0.002	0.002	0.000	0.000	0.000	0.000
48	A	1086	GLU	-1	-0.801	-0.897	33.490	-0.135	-0.135	0.000	0.000	0.000	0.000
49	A	1087	LEU	0	-0.022	-0.012	27.945	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	1088	LYS	1	0.766	0.889	31.672	0.150	0.150	0.000	0.000	0.000	0.000
51	A	1089	ASN	0	-0.013	-0.008	30.525	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	1090	VAL	0	0.008	-0.008	24.172	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	1091	GLU	-1	-0.960	-0.965	26.497	-0.224	-0.224	0.000	0.000	0.000	0.000
54	A	1092	ALA	0	0.003	-0.009	23.194	-0.026	-0.026	0.000	0.000	0.000	0.000
55	A	1093	GLY	0	-0.003	0.000	22.048	0.022	0.022	0.000	0.000	0.000	0.000
56	A	1094	ASP	-1	-0.880	-0.961	22.075	-0.388	-0.388	0.000	0.000	0.000	0.000
57	A	1095	ILE	0	-0.050	0.004	16.015	0.006	0.006	0.000	0.000	0.000	0.000
58	A	1096	ILE	0	-0.064	-0.020	18.098	-0.025	-0.025	0.000	0.000	0.000	0.000
59	A	1097	LYS	1	0.880	0.936	17.286	0.440	0.440	0.000	0.000	0.000	0.000
60	A	1098	THR	0	0.011	-0.013	21.220	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	1099	PRO	0	0.071	0.036	22.438	0.007	0.007	0.000	0.000	0.000	0.000
62	A	1100	LEU	0	-0.028	-0.024	23.501	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	1101	ALA	0	-0.020	-0.001	24.154	0.015	0.015	0.000	0.000	0.000	0.000
64	A	1102	ASN	0	0.002	-0.004	19.152	0.025	0.025	0.000	0.000	0.000	0.000
65	A	1103	PHE	0	0.012	0.000	19.363	-0.039	-0.039	0.000	0.000	0.000	0.000
66	A	1104	SER	0	-0.020	0.007	21.362	0.041	0.041	0.000	0.000	0.000	0.000
67	A	1105	ASN	0	0.032	0.009	21.866	-0.014	-0.014	0.000	0.000	0.000	0.000
68	A	1106	ASN	0	0.000	0.012	23.690	0.038	0.038	0.000	0.000	0.000	0.000
69	A	1107	LYS	1	0.927	0.949	25.012	0.200	0.200	0.000	0.000	0.000	0.000
70	A	1108	SER	0	-0.016	-0.010	27.867	0.009	0.009	0.000	0.000	0.000	0.000
71	A	1109	GLU	-1	-0.786	-0.857	24.602	-0.224	-0.224	0.000	0.000	0.000	0.000
72	A	1110	GLU	-1	-0.867	-0.952	27.847	-0.159	-0.159	0.000	0.000	0.000	0.000
73	A	1111	GLY	0	0.013	0.011	28.426	0.004	0.004	0.000	0.000	0.000	0.000
74	A	1112	LYS	1	0.755	0.869	22.457	0.237	0.237	0.000	0.000	0.000	0.000
75	A	1113	ILE	0	-0.001	0.004	22.911	0.017	0.017	0.000	0.000	0.000	0.000
76	A	1114	SER	0	-0.042	-0.013	19.414	-0.025	-0.025	0.000	0.000	0.000	0.000
77	A	1115	PHE	0	-0.001	-0.020	17.913	0.036	0.036	0.000	0.000	0.000	0.000
78	A	1116	LEU	0	0.022	0.010	16.692	-0.038	-0.038	0.000	0.000	0.000	0.000
79	A	1117	PHE	0	-0.003	-0.013	13.318	0.050	0.050	0.000	0.000	0.000	0.000
80	A	1118	ASN	0	0.005	-0.017	15.385	-0.054	-0.054	0.000	0.000	0.000	0.000
81	A	1119	ASP	-1	-0.688	-0.784	15.448	-0.204	-0.204	0.000	0.000	0.000	0.000
82	A	1120	ALA	0	0.032	0.009	17.170	0.041	0.041	0.000	0.000	0.000	0.000
83	A	1121	SER	0	-0.108	-0.087	19.171	0.036	0.036	0.000	0.000	0.000	0.000
84	A	1122	GLN	0	-0.109	-0.059	16.059	0.058	0.058	0.000	0.000	0.000	0.000
85	A	1123	GLY	0	0.036	0.009	14.595	0.055	0.055	0.000	0.000	0.000	0.000
86	A	1124	SER	0	-0.052	-0.011	15.671	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	1125	MET	0	-0.133	-0.066	17.634	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	1126	GLN	0	-0.007	-0.009	11.786	-0.066	-0.066	0.000	0.000	0.000	0.000
89	A	1127	ILE	0	-0.030	-0.004	13.140	0.035	0.035	0.000	0.000	0.000	0.000
90	A	1128	GLU	-1	-0.826	-0.919	12.513	-0.651	-0.651	0.000	0.000	0.000	0.000
91	A	1129	ASN	0	-0.063	-0.046	13.313	-0.051	-0.051	0.000	0.000	0.000	0.000
92	A	1130	GLY	0	0.015	0.012	14.581	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	1131	GLY	0	0.025	0.009	15.899	0.071	0.071	0.000	0.000	0.000	0.000
94	A	1132	VAL	0	-0.007	-0.001	18.793	-0.037	-0.037	0.000	0.000	0.000	0.000
95	A	1133	PHE	0	0.019	0.002	16.300	0.003	0.003	0.000	0.000	0.000	0.000
96	A	1134	ALA	0	-0.010	-0.021	19.128	0.032	0.032	0.000	0.000	0.000	0.000
97	A	1135	LYS	1	0.928	0.977	22.180	0.304	0.304	0.000	0.000	0.000	0.000
98	A	1136	ILE	0	0.022	0.015	22.712	0.005	0.005	0.000	0.000	0.000	0.000
99	A	1137	THR	0	0.002	0.016	26.940	0.005	0.005	0.000	0.000	0.000	0.000
100	A	1138	PHE	0	0.023	-0.009	26.563	0.002	0.002	0.000	0.000	0.000	0.000
101	A	1139	LYS	1	0.814	0.898	32.027	0.134	0.134	0.000	0.000	0.000	0.000
102	A	1140	VAL	0	-0.014	0.001	34.803	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	1141	LYS	1	0.869	0.936	35.134	0.150	0.150	0.000	0.000	0.000	0.000
104	A	1142	SER	0	0.011	-0.011	38.721	0.000	0.000	0.000	0.000	0.000	0.000
105	A	1143	THR	0	-0.002	0.000	40.456	0.004	0.004	0.000	0.000	0.000	0.000
106	A	1144	THR	0	-0.085	-0.036	35.994	0.004	0.004	0.000	0.000	0.000	0.000
107	A	1145	ALA	0	0.045	0.025	39.245	0.001	0.001	0.000	0.000	0.000	0.000
108	A	1146	THR	0	0.021	0.017	38.016	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	1147	GLY	0	-0.008	-0.004	35.722	0.005	0.005	0.000	0.000	0.000	0.000
110	A	1148	VAL	0	-0.035	-0.015	29.198	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	1149	TYR	0	-0.028	-0.023	30.044	0.003	0.003	0.000	0.000	0.000	0.000
112	A	1150	ASP	-1	-0.810	-0.898	24.654	-0.256	-0.256	0.000	0.000	0.000	0.000
113	A	1151	LEU	0	-0.029	-0.008	23.485	0.006	0.006	0.000	0.000	0.000	0.000
114	A	1152	ARG	1	0.825	0.885	20.025	0.229	0.229	0.000	0.000	0.000	0.000
115	A	1153	LYS	1	0.940	0.965	13.101	0.553	0.553	0.000	0.000	0.000	0.000
116	A	1154	ASP	-1	-0.833	-0.901	17.256	-0.284	-0.284	0.000	0.000	0.000	0.000
117	A	1155	LEU	0	-0.010	-0.015	15.271	-0.040	-0.040	0.000	0.000	0.000	0.000
118	A	1156	VAL	0	-0.026	-0.030	10.259	-0.007	-0.007	0.000	0.000	0.000	0.000
119	A	1157	GLY	0	0.033	0.031	11.558	0.055	0.055	0.000	0.000	0.000	0.000
120	A	1158	SER	0	-0.051	-0.028	8.634	-0.226	-0.226	0.000	0.000	0.000	0.000
121	A	1159	PHE	0	0.011	0.005	7.419	0.187	0.187	0.000	0.000	0.000	0.000
122	A	1160	SER	0	-0.056	-0.046	6.360	-0.273	-0.273	0.000	0.000	0.000	0.000
123	A	1161	GLY	0	0.062	0.035	6.213	-0.055	-0.055	0.000	0.000	0.000	0.000
124	A	1162	LEU	0	0.004	0.000	7.220	0.578	0.578	0.000	0.000	0.000	0.000
125	A	1163	LYS	1	0.846	0.921	3.082	-11.559	-9.805	0.129	-0.925	-0.958	0.011
126	A	1164	ASP	-1	-0.772	-0.891	6.363	0.811	0.811	0.000	0.000	0.000	0.000
127	A	1165	ASN	0	-0.016	-0.003	9.547	0.104	0.104	0.000	0.000	0.000	0.000
128	A	1166	LYS	1	0.828	0.907	8.553	-0.995	-0.995	0.000	0.000	0.000	0.000
129	A	1167	MET	0	0.025	0.029	7.483	0.405	0.405	0.000	0.000	0.000	0.000
130	A	1168	THR	0	-0.045	-0.010	2.467	1.846	2.214	2.320	-0.953	-1.735	0.003
131	A	1169	SER	0	0.021	0.017	3.180	-2.286	-1.585	0.040	-0.184	-0.557	0.000
132	A	1170	ILE	0	-0.018	-0.017	2.564	-4.766	-2.112	3.145	-2.321	-3.478	-0.027
133	A	1171	GLY	0	0.008	0.014	2.595	0.061	0.911	0.244	-0.263	-0.830	-0.002
134	A	1172	ALA	0	0.031	-0.001	3.870	0.380	0.440	0.004	-0.012	-0.052	0.000
135	A	1173	GLU	-1	-0.863	-0.931	7.261	-1.045	-1.045	0.000	0.000	0.000	0.000
136	A	1174	PHE	0	0.012	-0.004	9.935	0.069	0.069	0.000	0.000	0.000	0.000
137	A	1175	THR	0	-0.002	0.010	13.443	0.068	0.068	0.000	0.000	0.000	0.000
138	A	1176	ASN	0	0.007	-0.004	16.526	-0.006	-0.006	0.000	0.000	0.000	0.000
139	A	1177	GLY	0	0.073	0.019	19.185	0.013	0.013	0.000	0.000	0.000	0.000
140	A	1178	SER	0	-0.079	-0.041	22.525	0.010	0.010	0.000	0.000	0.000	0.000
141	A	1179	ILE	0	0.042	0.026	26.257	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	1180	THR	0	-0.009	-0.001	29.808	0.008	0.008	0.000	0.000	0.000	0.000
143	A	1181	VAL	0	-0.045	-0.010	32.599	0.000	0.000	0.000	0.000	0.000	0.000
144	A	1182	ALA	0	0.035	0.004	35.950	0.006	0.006	0.000	0.000	0.000	0.000
145	A	1183	ALA	0	-0.003	-0.017	38.558	0.002	0.002	0.000	0.000	0.000	0.000
146	A	1184	THR	0	-0.034	-0.039	42.369	0.000	0.000	0.000	0.000	0.000	0.000
147	A	1185	ALA	0	-0.025	-0.005	44.110	0.005	0.005	0.000	0.000	0.000	0.000
148	A	1186	PRO	0	-0.012	-0.016	46.396	0.000	0.000	0.000	0.000	0.000	0.000
149	A	1187	LEU	0	0.020	0.004	47.281	0.000	0.000	0.000	0.000	0.000	0.000
150	A	1188	GLU	-1	-0.917	-0.924	50.830	-0.065	-0.065	0.000	0.000	0.000	0.000
151	A	1189	HIS	0	-0.041	-0.027	52.135	0.002	0.002	0.000	0.000	0.000	0.000
152	A	1190	HIS	0	-0.033	-0.036	55.481	0.002	0.002	0.000	0.000	0.000	0.000
153	A	1191	HIS	0	-0.027	-0.005	56.499	0.001	0.001	0.000	0.000	0.000	0.000
154	A	1192	HIS	0	-0.010	0.001	59.963	0.003	0.003	0.000	0.000	0.000	0.000

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