FMO DATABASE

FMODB ID: 4JNMN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1334582.50755
FMO2-HF: Nuclear repulsion	1275680.751998
FMO2-HF: Total energy	-58901.755552
FMO2-MP2: Total energy	-59072.160648

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.
-4.719	-15.128	20.819	5.151	-15.558	-0.072

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 : -0.029 / 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	0.046	0.008	2.360	6.552	-3.823	3.365	11.172	-4.161	-0.032
4	A	1042	MET	0	0.011	0.030	4.584	0.122	0.214	-0.001	-0.025	-0.066	0.000
5	A	1043	ASN	0	-0.042	-0.029	7.937	0.186	0.186	0.000	0.000	0.000	0.000
6	A	1044	VAL	0	0.003	-0.003	10.745	0.046	0.046	0.000	0.000	0.000	0.000
7	A	1045	VAL	0	-0.010	-0.007	13.074	0.058	0.058	0.000	0.000	0.000	0.000
8	A	1046	ILE	0	-0.028	-0.004	16.413	0.021	0.021	0.000	0.000	0.000	0.000
9	A	1047	GLY	0	0.032	0.015	19.117	0.018	0.018	0.000	0.000	0.000	0.000
10	A	1048	LYS	1	0.945	0.969	21.881	0.311	0.311	0.000	0.000	0.000	0.000
11	A	1049	MET	0	-0.024	-0.002	25.128	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	1050	ASN	0	-0.013	-0.010	28.514	0.008	0.008	0.000	0.000	0.000	0.000
13	A	1051	ALA	0	0.026	0.012	32.157	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	1052	GLU	-1	-0.865	-0.931	34.681	-0.122	-0.122	0.000	0.000	0.000	0.000
15	A	1053	VAL	0	0.042	0.016	37.822	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	1054	GLY	0	-0.032	-0.015	39.025	0.004	0.004	0.000	0.000	0.000	0.000
17	A	1055	GLY	0	-0.020	-0.003	38.364	0.002	0.002	0.000	0.000	0.000	0.000
18	A	1056	GLU	-1	-0.941	-0.980	34.923	-0.155	-0.155	0.000	0.000	0.000	0.000
19	A	1057	VAL	0	-0.008	-0.007	29.864	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	1058	VAL	0	0.014	0.007	27.864	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	1059	VAL	0	-0.003	-0.007	23.270	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	1060	PRO	0	-0.040	-0.005	22.490	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	1061	ILE	0	0.006	-0.009	17.149	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	1062	GLU	-1	-0.924	-0.970	17.903	-0.477	-0.477	0.000	0.000	0.000	0.000
25	A	1063	PHE	0	0.013	0.011	13.342	-0.092	-0.092	0.000	0.000	0.000	0.000
26	A	1064	ASN	0	-0.016	-0.029	13.247	0.023	0.023	0.000	0.000	0.000	0.000
27	A	1065	ASN	0	0.011	0.003	10.616	-0.125	-0.125	0.000	0.000	0.000	0.000
28	A	1066	VAL	0	-0.007	0.006	9.242	-0.365	-0.365	0.000	0.000	0.000	0.000
29	A	1067	PRO	0	0.034	0.016	4.843	0.067	0.067	0.000	0.000	0.000	0.000
30	A	1068	SER	0	0.013	-0.002	7.017	0.278	0.278	0.000	0.000	0.000	0.000
31	A	1069	PHE	0	-0.058	-0.017	2.510	-0.408	0.910	0.675	-0.692	-1.301	-0.005
32	A	1070	GLY	0	0.079	0.058	7.702	0.298	0.298	0.000	0.000	0.000	0.000
33	A	1071	ILE	0	-0.075	-0.045	7.687	-0.218	-0.218	0.000	0.000	0.000	0.000
34	A	1072	ASN	0	0.017	-0.002	9.558	0.185	0.185	0.000	0.000	0.000	0.000
35	A	1073	ASN	0	-0.008	-0.019	10.665	0.182	0.182	0.000	0.000	0.000	0.000
36	A	1074	CYS	0	-0.080	-0.036	10.686	-0.155	-0.155	0.000	0.000	0.000	0.000
37	A	1075	ASP	-1	-0.814	-0.884	11.932	-0.400	-0.400	0.000	0.000	0.000	0.000
38	A	1076	PHE	0	0.021	-0.002	12.385	-0.101	-0.101	0.000	0.000	0.000	0.000
39	A	1077	LYS	1	0.918	0.976	14.531	0.322	0.322	0.000	0.000	0.000	0.000
40	A	1078	LEU	0	-0.012	0.005	17.026	-0.038	-0.038	0.000	0.000	0.000	0.000
41	A	1079	VAL	0	-0.009	-0.001	19.641	0.033	0.033	0.000	0.000	0.000	0.000
42	A	1080	TYR	0	0.023	0.004	22.674	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	1081	ASP	-1	-0.808	-0.913	25.889	-0.140	-0.140	0.000	0.000	0.000	0.000
44	A	1082	ALA	0	0.027	0.003	29.299	0.002	0.002	0.000	0.000	0.000	0.000
45	A	1083	THR	0	-0.036	-0.008	31.438	0.011	0.011	0.000	0.000	0.000	0.000
46	A	1084	ALA	0	-0.014	0.007	32.359	0.007	0.007	0.000	0.000	0.000	0.000
47	A	1085	LEU	0	-0.033	-0.024	29.045	0.002	0.002	0.000	0.000	0.000	0.000
48	A	1086	GLU	-1	-0.882	-0.939	32.588	-0.131	-0.131	0.000	0.000	0.000	0.000
49	A	1087	LEU	0	-0.028	-0.017	27.429	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	1088	LYS	1	0.881	0.953	31.031	0.150	0.150	0.000	0.000	0.000	0.000
51	A	1089	ASN	0	-0.037	-0.041	29.985	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	1090	VAL	0	-0.008	0.006	23.704	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	1091	GLU	-1	-0.953	-0.956	26.181	-0.217	-0.217	0.000	0.000	0.000	0.000
54	A	1092	ALA	0	-0.022	-0.017	22.701	-0.024	-0.024	0.000	0.000	0.000	0.000
55	A	1093	GLY	0	-0.016	-0.016	21.815	0.022	0.022	0.000	0.000	0.000	0.000
56	A	1094	ASP	-1	-0.935	-0.972	22.156	-0.383	-0.383	0.000	0.000	0.000	0.000
57	A	1095	ILE	0	-0.020	0.011	15.791	0.000	0.000	0.000	0.000	0.000	0.000
58	A	1096	ILE	0	-0.059	-0.011	18.019	-0.024	-0.024	0.000	0.000	0.000	0.000
59	A	1097	LYS	1	0.933	0.973	17.695	0.445	0.445	0.000	0.000	0.000	0.000
60	A	1098	THR	0	-0.009	-0.020	21.068	0.000	0.000	0.000	0.000	0.000	0.000
61	A	1099	PRO	0	0.085	0.034	22.398	0.006	0.006	0.000	0.000	0.000	0.000
62	A	1100	LEU	0	-0.018	-0.011	23.453	0.002	0.002	0.000	0.000	0.000	0.000
63	A	1101	ALA	0	-0.035	-0.011	23.801	0.011	0.011	0.000	0.000	0.000	0.000
64	A	1102	ASN	0	0.024	0.016	19.039	0.030	0.030	0.000	0.000	0.000	0.000
65	A	1103	PHE	0	0.003	-0.001	19.458	-0.032	-0.032	0.000	0.000	0.000	0.000
66	A	1104	SER	0	0.005	0.011	20.928	0.040	0.040	0.000	0.000	0.000	0.000
67	A	1105	ASN	0	0.013	-0.007	21.106	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	1106	ASN	0	0.018	0.028	23.078	0.036	0.036	0.000	0.000	0.000	0.000
69	A	1107	LYS	1	0.942	0.953	24.276	0.191	0.191	0.000	0.000	0.000	0.000
70	A	1108	SER	0	-0.040	-0.026	26.897	0.010	0.010	0.000	0.000	0.000	0.000
71	A	1109	GLU	-1	-0.924	-0.945	25.100	-0.159	-0.159	0.000	0.000	0.000	0.000
72	A	1110	GLU	-1	-0.895	-0.957	27.046	-0.145	-0.145	0.000	0.000	0.000	0.000
73	A	1111	GLY	0	0.015	0.005	27.621	0.002	0.002	0.000	0.000	0.000	0.000
74	A	1112	LYS	1	0.836	0.922	22.001	0.194	0.194	0.000	0.000	0.000	0.000
75	A	1113	ILE	0	0.003	0.004	22.187	0.015	0.015	0.000	0.000	0.000	0.000
76	A	1114	SER	0	-0.082	-0.024	19.461	-0.046	-0.046	0.000	0.000	0.000	0.000
77	A	1115	PHE	0	0.035	-0.003	17.122	0.036	0.036	0.000	0.000	0.000	0.000
78	A	1116	LEU	0	0.017	0.005	16.331	-0.035	-0.035	0.000	0.000	0.000	0.000
79	A	1117	PHE	0	-0.017	-0.012	13.573	0.034	0.034	0.000	0.000	0.000	0.000
80	A	1118	ASN	0	0.017	-0.018	15.443	-0.044	-0.044	0.000	0.000	0.000	0.000
81	A	1119	ASP	-1	-0.710	-0.794	15.454	-0.212	-0.212	0.000	0.000	0.000	0.000
82	A	1120	ALA	0	0.014	0.004	17.144	0.044	0.044	0.000	0.000	0.000	0.000
83	A	1121	SER	0	-0.099	-0.089	19.221	0.033	0.033	0.000	0.000	0.000	0.000
84	A	1122	GLN	0	-0.101	-0.049	16.421	0.048	0.048	0.000	0.000	0.000	0.000
85	A	1123	GLY	0	0.036	0.003	15.054	0.054	0.054	0.000	0.000	0.000	0.000
86	A	1124	SER	0	-0.042	-0.012	16.140	-0.030	-0.030	0.000	0.000	0.000	0.000
87	A	1125	MET	0	-0.136	-0.071	17.755	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	1126	GLN	0	0.035	0.010	11.698	-0.036	-0.036	0.000	0.000	0.000	0.000
89	A	1127	ILE	0	-0.041	-0.017	12.840	0.033	0.033	0.000	0.000	0.000	0.000
90	A	1128	GLU	-1	-0.881	-0.961	12.063	-0.801	-0.801	0.000	0.000	0.000	0.000
91	A	1129	ASN	0	-0.040	-0.027	13.290	-0.091	-0.091	0.000	0.000	0.000	0.000
92	A	1130	GLY	0	0.008	0.014	14.769	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	1131	GLY	0	0.031	0.011	15.574	0.083	0.083	0.000	0.000	0.000	0.000
94	A	1132	VAL	0	-0.001	-0.010	18.300	-0.041	-0.041	0.000	0.000	0.000	0.000
95	A	1133	PHE	0	0.049	0.027	16.257	0.013	0.013	0.000	0.000	0.000	0.000
96	A	1134	ALA	0	0.003	-0.005	18.925	0.039	0.039	0.000	0.000	0.000	0.000
97	A	1135	LYS	1	0.933	0.971	21.829	0.304	0.304	0.000	0.000	0.000	0.000
98	A	1136	ILE	0	0.033	0.023	22.084	0.013	0.013	0.000	0.000	0.000	0.000
99	A	1137	THR	0	0.016	0.021	26.248	0.003	0.003	0.000	0.000	0.000	0.000
100	A	1138	PHE	0	0.020	-0.011	25.970	0.004	0.004	0.000	0.000	0.000	0.000
101	A	1139	LYS	1	0.964	0.987	31.510	0.123	0.123	0.000	0.000	0.000	0.000
102	A	1140	VAL	0	-0.016	-0.005	33.795	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	1141	LYS	1	0.903	0.973	35.218	0.134	0.134	0.000	0.000	0.000	0.000
104	A	1142	SER	0	0.003	-0.019	38.302	0.000	0.000	0.000	0.000	0.000	0.000
105	A	1143	THR	0	0.010	-0.002	39.983	0.003	0.003	0.000	0.000	0.000	0.000
106	A	1144	THR	0	-0.074	-0.031	35.241	0.005	0.005	0.000	0.000	0.000	0.000
107	A	1145	ALA	0	0.040	0.033	37.938	0.002	0.002	0.000	0.000	0.000	0.000
108	A	1146	THR	0	0.016	0.014	36.915	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	1147	GLY	0	-0.002	0.001	34.752	0.006	0.006	0.000	0.000	0.000	0.000
110	A	1148	VAL	0	-0.022	-0.013	28.170	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	1149	TYR	0	-0.031	-0.024	29.099	0.005	0.005	0.000	0.000	0.000	0.000
112	A	1150	ASP	-1	-0.840	-0.919	23.584	-0.237	-0.237	0.000	0.000	0.000	0.000
113	A	1151	LEU	0	-0.046	-0.022	22.725	0.006	0.006	0.000	0.000	0.000	0.000
114	A	1152	ARG	1	0.831	0.899	19.226	0.210	0.210	0.000	0.000	0.000	0.000
115	A	1153	LYS	1	0.961	0.982	12.278	0.565	0.565	0.000	0.000	0.000	0.000
116	A	1154	ASP	-1	-0.875	-0.938	16.581	-0.236	-0.236	0.000	0.000	0.000	0.000
117	A	1155	LEU	0	-0.039	-0.035	14.873	-0.052	-0.052	0.000	0.000	0.000	0.000
118	A	1156	VAL	0	-0.026	-0.016	9.185	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	1157	GLY	0	0.015	0.023	11.569	0.082	0.082	0.000	0.000	0.000	0.000
120	A	1158	SER	0	-0.057	-0.030	8.408	-0.267	-0.267	0.000	0.000	0.000	0.000
121	A	1159	PHE	0	0.051	0.017	6.370	0.137	0.137	0.000	0.000	0.000	0.000
122	A	1160	SER	0	-0.030	-0.024	6.131	-0.270	-0.270	0.000	0.000	0.000	0.000
123	A	1161	GLY	0	0.062	0.037	6.112	-0.168	-0.168	0.000	0.000	0.000	0.000
124	A	1162	LEU	0	-0.024	0.000	7.151	0.693	0.693	0.000	0.000	0.000	0.000
125	A	1163	LYS	1	0.927	0.971	4.357	-6.096	-5.918	-0.001	-0.045	-0.131	0.000
126	A	1164	ASP	-1	-0.882	-0.948	6.843	-0.008	-0.008	0.000	0.000	0.000	0.000
127	A	1165	ASN	0	-0.012	-0.014	10.256	0.020	0.020	0.000	0.000	0.000	0.000
128	A	1166	LYS	1	0.883	0.955	8.541	-0.898	-0.898	0.000	0.000	0.000	0.000
129	A	1167	MET	0	0.061	0.035	7.897	0.287	0.287	0.000	0.000	0.000	0.000
130	A	1168	THR	0	-0.076	-0.041	2.429	0.841	0.712	3.020	-1.080	-1.811	0.006
131	A	1169	SER	0	0.017	0.015	3.428	-2.701	-1.822	0.014	-0.308	-0.584	0.000
132	A	1170	ILE	0	0.004	-0.011	2.229	-2.457	-4.805	12.163	-4.049	-5.766	-0.041
133	A	1171	GLY	0	-0.004	0.003	2.510	0.264	0.476	1.540	-0.148	-1.604	0.000
134	A	1172	ALA	0	0.019	0.004	3.446	0.754	0.518	0.044	0.326	-0.134	0.000
135	A	1173	GLU	-1	-0.908	-0.950	6.648	-0.819	-0.819	0.000	0.000	0.000	0.000
136	A	1174	PHE	0	-0.024	-0.019	8.818	0.093	0.093	0.000	0.000	0.000	0.000
137	A	1175	THR	0	-0.009	0.004	12.397	0.048	0.048	0.000	0.000	0.000	0.000
138	A	1176	ASN	0	0.015	0.010	15.605	-0.027	-0.027	0.000	0.000	0.000	0.000
139	A	1177	GLY	0	0.054	0.023	18.531	0.005	0.005	0.000	0.000	0.000	0.000
140	A	1178	SER	0	-0.070	-0.040	21.807	0.011	0.011	0.000	0.000	0.000	0.000
141	A	1179	ILE	0	0.032	0.031	25.404	-0.008	-0.008	0.000	0.000	0.000	0.000
142	A	1180	THR	0	-0.032	-0.021	28.879	0.008	0.008	0.000	0.000	0.000	0.000
143	A	1181	VAL	0	-0.015	0.008	31.521	0.001	0.001	0.000	0.000	0.000	0.000
144	A	1182	ALA	0	0.001	-0.011	34.905	0.006	0.006	0.000	0.000	0.000	0.000
145	A	1183	ALA	0	-0.004	-0.013	37.734	0.001	0.001	0.000	0.000	0.000	0.000
146	A	1184	THR	0	0.022	0.016	41.463	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	1185	ALA	0	-0.036	-0.007	43.119	0.005	0.005	0.000	0.000	0.000	0.000
148	A	1186	PRO	0	0.000	0.002	45.712	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	1187	LEU	0	0.017	-0.002	46.831	0.000	0.000	0.000	0.000	0.000	0.000
150	A	1188	GLU	-1	-0.891	-0.907	49.942	-0.066	-0.066	0.000	0.000	0.000	0.000
151	A	1189	HIS	0	-0.058	-0.041	51.279	0.002	0.002	0.000	0.000	0.000	0.000
152	A	1190	HIS	0	-0.039	-0.047	54.562	0.002	0.002	0.000	0.000	0.000	0.000
153	A	1191	HIS	0	-0.014	-0.004	55.882	0.001	0.001	0.000	0.000	0.000	0.000
154	A	1192	HIS	0	-0.010	0.005	58.752	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)