FMO DATABASE

FMODB ID: YVJ42

Calculation Name: 3MTK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3MTK

Chain ID: A

ChEMBL ID:

UniProt ID: A4XHQ4

Base Structure: X-ray

Registration Date: 2023-09-23

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	168
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1796632.8266
FMO2-HF: Nuclear repulsion	1729132.492317
FMO2-HF: Total energy	-67500.334284
FMO2-MP2: Total energy	-67697.599922

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:186:LYS)

Summations of interaction energy for fragment #1(A:186: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.
-105.464	-105.619	23.938	-11.877	-11.906	-0.105

Interaction energy analysis for fragmet #1(A:186:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.933 / q_NPA : 0.949

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	188	GLU	-1	-0.868	-0.927	1.679	-117.940	-119.664	23.147	-11.695	-9.728	-0.102
4	A	189	PHE	0	0.005	-0.003	2.297	4.095	5.247	0.789	-0.110	-1.831	-0.003
5	A	190	LEU	0	0.066	0.040	3.951	4.812	5.229	0.002	-0.072	-0.347	0.000
6	A	191	ALA	0	0.006	0.016	5.807	4.442	4.442	0.000	0.000	0.000	0.000
7	A	192	PHE	0	-0.064	-0.036	6.534	4.289	4.289	0.000	0.000	0.000	0.000
8	A	193	TYR	0	-0.019	0.005	6.701	3.388	3.388	0.000	0.000	0.000	0.000
9	A	194	ASP	-1	-0.855	-0.929	9.042	-19.353	-19.353	0.000	0.000	0.000	0.000
10	A	195	GLU	-1	-0.943	-0.963	6.943	-25.841	-25.841	0.000	0.000	0.000	0.000
11	A	196	LEU	0	0.035	0.040	9.339	-0.106	-0.106	0.000	0.000	0.000	0.000
12	A	197	THR	0	-0.005	-0.010	12.698	0.847	0.847	0.000	0.000	0.000	0.000
13	A	198	GLY	0	-0.010	0.011	10.403	0.372	0.372	0.000	0.000	0.000	0.000
14	A	199	LEU	0	-0.053	-0.031	11.365	-1.132	-1.132	0.000	0.000	0.000	0.000
15	A	200	PRO	0	-0.017	-0.002	11.269	-1.287	-1.287	0.000	0.000	0.000	0.000
16	A	201	ASN	0	0.074	0.009	10.339	2.447	2.447	0.000	0.000	0.000	0.000
17	A	202	LYS	1	0.988	0.981	13.429	15.443	15.443	0.000	0.000	0.000	0.000
18	A	203	ASN	0	-0.024	-0.014	11.512	2.264	2.264	0.000	0.000	0.000	0.000
19	A	204	SER	0	-0.048	-0.036	11.058	-0.349	-0.349	0.000	0.000	0.000	0.000
20	A	205	LEU	0	0.009	0.015	13.523	0.568	0.568	0.000	0.000	0.000	0.000
21	A	206	ILE	0	0.039	0.011	16.941	0.844	0.844	0.000	0.000	0.000	0.000
22	A	207	ARG	1	0.881	0.960	8.927	29.880	29.880	0.000	0.000	0.000	0.000
23	A	208	TRP	0	0.036	-0.008	12.448	0.247	0.247	0.000	0.000	0.000	0.000
24	A	209	LEU	0	0.001	0.012	17.402	0.849	0.849	0.000	0.000	0.000	0.000
25	A	210	ASN	0	-0.009	-0.014	18.525	1.309	1.309	0.000	0.000	0.000	0.000
26	A	211	LEU	0	-0.010	0.007	17.156	0.480	0.480	0.000	0.000	0.000	0.000
27	A	212	LYS	1	0.854	0.908	20.281	13.292	13.292	0.000	0.000	0.000	0.000
28	A	213	VAL	0	-0.008	-0.005	22.905	0.507	0.507	0.000	0.000	0.000	0.000
29	A	214	SER	0	-0.044	-0.010	23.042	0.335	0.335	0.000	0.000	0.000	0.000
30	A	215	GLN	0	-0.032	-0.009	23.881	0.500	0.500	0.000	0.000	0.000	0.000
31	A	216	MET	0	0.009	0.002	26.944	0.076	0.076	0.000	0.000	0.000	0.000
32	A	217	ASP	-1	-0.821	-0.892	30.737	-9.226	-9.226	0.000	0.000	0.000	0.000
33	A	218	CYS	0	-0.085	-0.022	27.171	-0.294	-0.294	0.000	0.000	0.000	0.000
34	A	219	ILE	0	-0.017	-0.052	29.508	0.058	0.058	0.000	0.000	0.000	0.000
35	A	220	ASP	-1	-0.775	-0.833	31.548	-9.225	-9.225	0.000	0.000	0.000	0.000
36	A	221	THR	0	-0.035	-0.019	25.728	-0.404	-0.404	0.000	0.000	0.000	0.000
37	A	222	TYR	0	-0.074	-0.069	28.399	0.148	0.148	0.000	0.000	0.000	0.000
38	A	223	LEU	0	-0.029	-0.005	23.278	-0.601	-0.601	0.000	0.000	0.000	0.000
39	A	224	ILE	0	0.032	0.002	25.437	0.499	0.499	0.000	0.000	0.000	0.000
40	A	225	PHE	0	-0.011	-0.020	23.381	-0.804	-0.804	0.000	0.000	0.000	0.000
41	A	226	LEU	0	0.035	0.013	24.519	0.463	0.463	0.000	0.000	0.000	0.000
42	A	227	GLU	-1	-0.784	-0.878	24.989	-10.991	-10.991	0.000	0.000	0.000	0.000
43	A	228	VAL	0	-0.008	-0.007	24.049	0.346	0.346	0.000	0.000	0.000	0.000
44	A	229	ARG	1	0.875	0.926	26.925	9.036	9.036	0.000	0.000	0.000	0.000
45	A	230	ASP	-1	-0.875	-0.954	29.648	-8.966	-8.966	0.000	0.000	0.000	0.000
46	A	231	LEU	0	0.073	0.044	22.475	0.140	0.140	0.000	0.000	0.000	0.000
47	A	232	GLU	-1	-0.871	-0.936	26.634	-9.762	-9.762	0.000	0.000	0.000	0.000
48	A	233	LYS	1	0.844	0.909	27.874	9.066	9.066	0.000	0.000	0.000	0.000
49	A	234	LEU	0	0.028	0.030	27.557	0.191	0.191	0.000	0.000	0.000	0.000
50	A	235	ASN	0	0.034	0.022	23.234	-0.098	-0.098	0.000	0.000	0.000	0.000
51	A	236	VAL	0	-0.056	-0.022	26.759	0.058	0.058	0.000	0.000	0.000	0.000
52	A	237	THR	0	-0.074	-0.044	30.064	0.245	0.245	0.000	0.000	0.000	0.000
53	A	238	TYR	0	-0.033	-0.033	28.014	0.195	0.195	0.000	0.000	0.000	0.000
54	A	239	GLY	0	0.027	0.033	26.762	-0.068	-0.068	0.000	0.000	0.000	0.000
55	A	240	TYR	0	0.008	-0.030	21.351	-0.096	-0.096	0.000	0.000	0.000	0.000
56	A	241	ASP	-1	-0.887	-0.929	20.722	-12.212	-12.212	0.000	0.000	0.000	0.000
57	A	242	LEU	0	-0.027	-0.005	21.566	-0.278	-0.278	0.000	0.000	0.000	0.000
58	A	243	VAL	0	0.004	-0.012	22.636	-0.155	-0.155	0.000	0.000	0.000	0.000
59	A	244	ASP	-1	-0.871	-0.933	17.806	-14.221	-14.221	0.000	0.000	0.000	0.000
60	A	245	GLU	-1	-0.872	-0.945	19.076	-13.422	-13.422	0.000	0.000	0.000	0.000
61	A	246	LEU	0	-0.027	-0.006	20.862	-0.078	-0.078	0.000	0.000	0.000	0.000
62	A	247	ILE	0	0.020	0.014	18.061	-0.113	-0.113	0.000	0.000	0.000	0.000
63	A	248	ILE	0	0.008	0.012	15.765	-0.304	-0.304	0.000	0.000	0.000	0.000
64	A	249	HIS	0	-0.107	-0.062	18.950	0.189	0.189	0.000	0.000	0.000	0.000
65	A	250	ILE	0	-0.017	-0.012	22.465	0.072	0.072	0.000	0.000	0.000	0.000
66	A	251	SER	0	-0.035	-0.037	17.266	0.187	0.187	0.000	0.000	0.000	0.000
67	A	252	LYS	1	0.893	0.952	18.308	14.148	14.148	0.000	0.000	0.000	0.000
68	A	253	ARG	1	0.874	0.921	21.264	10.456	10.456	0.000	0.000	0.000	0.000
69	A	254	ILE	0	0.020	0.009	22.225	0.153	0.153	0.000	0.000	0.000	0.000
70	A	255	LYS	1	0.909	0.931	16.917	16.051	16.051	0.000	0.000	0.000	0.000
71	A	256	ASP	-1	-0.995	-0.991	21.528	-11.718	-11.718	0.000	0.000	0.000	0.000
72	A	257	ILE	0	-0.032	-0.005	24.559	0.192	0.192	0.000	0.000	0.000	0.000
73	A	258	ALA	0	-0.032	0.003	23.212	0.224	0.224	0.000	0.000	0.000	0.000
74	A	259	GLY	0	0.045	0.024	24.210	0.426	0.426	0.000	0.000	0.000	0.000
75	A	260	GLU	-1	-0.946	-0.978	21.605	-14.445	-14.445	0.000	0.000	0.000	0.000
76	A	261	GLY	0	-0.090	-0.041	21.268	-0.558	-0.558	0.000	0.000	0.000	0.000
77	A	262	ASN	0	-0.045	-0.027	23.026	0.061	0.061	0.000	0.000	0.000	0.000
78	A	263	LYS	1	0.911	0.968	14.512	19.429	19.429	0.000	0.000	0.000	0.000
79	A	264	ALA	0	0.079	0.034	18.490	0.698	0.698	0.000	0.000	0.000	0.000
80	A	265	PHE	0	-0.060	-0.044	15.308	-1.311	-1.311	0.000	0.000	0.000	0.000
81	A	266	LYS	1	0.894	0.968	15.159	16.436	16.436	0.000	0.000	0.000	0.000
82	A	267	ILE	0	-0.044	-0.034	15.633	-1.065	-1.065	0.000	0.000	0.000	0.000
83	A	268	GLY	0	0.018	0.009	17.963	0.112	0.112	0.000	0.000	0.000	0.000
84	A	269	PHE	0	0.020	0.004	18.735	-0.274	-0.274	0.000	0.000	0.000	0.000
85	A	270	ASP	-1	-0.834	-0.908	19.711	-12.109	-12.109	0.000	0.000	0.000	0.000
86	A	271	ARG	1	0.784	0.884	21.249	12.044	12.044	0.000	0.000	0.000	0.000
87	A	272	PHE	0	-0.009	-0.013	18.715	-0.992	-0.992	0.000	0.000	0.000	0.000
88	A	273	ALA	0	-0.016	-0.012	20.250	0.555	0.555	0.000	0.000	0.000	0.000
89	A	274	ILE	0	0.010	0.008	20.814	-0.723	-0.723	0.000	0.000	0.000	0.000
90	A	275	ILE	0	-0.028	-0.002	20.635	0.288	0.288	0.000	0.000	0.000	0.000
91	A	276	CYS	0	0.020	-0.005	23.460	-0.253	-0.253	0.000	0.000	0.000	0.000
92	A	277	LYS	1	0.978	1.017	26.071	12.068	12.068	0.000	0.000	0.000	0.000
93	A	278	SER	0	-0.060	-0.053	28.698	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	279	GLU	-1	-0.890	-0.928	32.116	-8.671	-8.671	0.000	0.000	0.000	0.000
95	A	280	ASN	0	0.032	0.010	35.680	0.105	0.105	0.000	0.000	0.000	0.000
96	A	281	ILE	0	0.016	0.001	31.205	-0.138	-0.138	0.000	0.000	0.000	0.000
97	A	282	SER	0	0.058	0.035	33.850	-0.155	-0.155	0.000	0.000	0.000	0.000
98	A	283	ASP	-1	-0.845	-0.903	35.830	-8.757	-8.757	0.000	0.000	0.000	0.000
99	A	284	PHE	0	-0.032	-0.009	27.224	-0.145	-0.145	0.000	0.000	0.000	0.000
100	A	285	ILE	0	-0.004	-0.014	30.994	-0.264	-0.264	0.000	0.000	0.000	0.000
101	A	286	GLU	-1	-0.830	-0.887	32.690	-8.217	-8.217	0.000	0.000	0.000	0.000
102	A	287	ARG	1	0.856	0.934	32.367	9.452	9.452	0.000	0.000	0.000	0.000
103	A	288	MET	0	0.067	0.040	27.623	-0.218	-0.218	0.000	0.000	0.000	0.000
104	A	289	LEU	0	-0.012	0.000	30.917	-0.152	-0.152	0.000	0.000	0.000	0.000
105	A	290	SER	0	-0.057	-0.046	32.569	0.099	0.099	0.000	0.000	0.000	0.000
106	A	291	GLN	0	0.023	-0.002	31.211	0.041	0.041	0.000	0.000	0.000	0.000
107	A	292	LEU	0	-0.041	-0.007	26.556	-0.101	-0.101	0.000	0.000	0.000	0.000
108	A	293	LEU	0	0.031	0.023	30.193	-0.033	-0.033	0.000	0.000	0.000	0.000
109	A	294	LEU	0	-0.045	-0.011	32.658	0.304	0.304	0.000	0.000	0.000	0.000
110	A	295	PRO	0	-0.051	-0.012	31.470	-0.250	-0.250	0.000	0.000	0.000	0.000
111	A	296	TYR	0	0.017	0.011	26.257	-0.361	-0.361	0.000	0.000	0.000	0.000
112	A	297	ASN	0	-0.025	-0.002	29.170	0.199	0.199	0.000	0.000	0.000	0.000
113	A	298	VAL	0	0.056	0.018	24.487	-0.236	-0.236	0.000	0.000	0.000	0.000
114	A	299	ASN	0	0.040	0.025	25.886	0.116	0.116	0.000	0.000	0.000	0.000
115	A	300	GLY	0	-0.004	0.004	27.806	0.216	0.216	0.000	0.000	0.000	0.000
116	A	301	ASN	0	-0.046	-0.027	29.504	0.154	0.154	0.000	0.000	0.000	0.000
117	A	302	LEU	0	-0.018	0.001	30.482	-0.227	-0.227	0.000	0.000	0.000	0.000
118	A	303	ILE	0	0.003	-0.008	28.198	0.180	0.180	0.000	0.000	0.000	0.000
119	A	304	ARG	1	0.915	0.945	31.256	8.214	8.214	0.000	0.000	0.000	0.000
120	A	305	VAL	0	0.016	0.015	27.878	0.061	0.061	0.000	0.000	0.000	0.000
121	A	306	ASN	0	0.021	0.027	31.173	0.172	0.172	0.000	0.000	0.000	0.000
122	A	307	PHE	0	0.022	-0.005	26.202	-0.386	-0.386	0.000	0.000	0.000	0.000
123	A	308	ASN	0	-0.004	-0.002	30.149	0.328	0.328	0.000	0.000	0.000	0.000
124	A	309	ILE	0	-0.006	-0.012	29.267	-0.466	-0.466	0.000	0.000	0.000	0.000
125	A	310	GLY	0	0.074	0.065	29.508	0.371	0.371	0.000	0.000	0.000	0.000
126	A	311	ALA	0	-0.018	-0.021	29.088	-0.536	-0.536	0.000	0.000	0.000	0.000
127	A	312	ALA	0	0.007	-0.002	29.634	0.346	0.346	0.000	0.000	0.000	0.000
128	A	313	GLN	0	0.024	0.023	29.807	-0.225	-0.225	0.000	0.000	0.000	0.000
129	A	314	ILE	0	-0.076	-0.044	24.762	-0.112	-0.112	0.000	0.000	0.000	0.000
130	A	315	GLU	-1	-0.847	-0.934	28.874	-9.158	-9.158	0.000	0.000	0.000	0.000
131	A	316	ASN	0	-0.131	-0.085	28.715	-0.119	-0.119	0.000	0.000	0.000	0.000
132	A	317	SER	0	0.073	0.041	30.882	0.181	0.181	0.000	0.000	0.000	0.000
133	A	318	ASN	0	0.024	0.013	31.638	0.216	0.216	0.000	0.000	0.000	0.000
134	A	319	GLU	-1	-0.874	-0.919	28.545	-10.720	-10.720	0.000	0.000	0.000	0.000
135	A	320	ALA	0	0.032	0.009	24.757	0.087	0.087	0.000	0.000	0.000	0.000
136	A	321	ALA	0	0.023	0.023	21.655	0.164	0.164	0.000	0.000	0.000	0.000
137	A	322	ALA	0	0.011	-0.004	23.624	0.181	0.181	0.000	0.000	0.000	0.000
138	A	323	ASN	0	0.036	-0.005	25.028	-0.056	-0.056	0.000	0.000	0.000	0.000
139	A	324	LEU	0	0.026	0.036	25.884	0.325	0.325	0.000	0.000	0.000	0.000
140	A	325	MET	0	-0.011	-0.017	20.821	-0.124	-0.124	0.000	0.000	0.000	0.000
141	A	326	ARG	1	0.834	0.919	25.714	11.111	11.111	0.000	0.000	0.000	0.000
142	A	327	ARG	1	0.970	0.989	28.658	10.221	10.221	0.000	0.000	0.000	0.000
143	A	328	CYS	0	-0.038	-0.006	27.173	0.239	0.239	0.000	0.000	0.000	0.000
144	A	329	ASP	-1	-0.858	-0.917	27.552	-10.720	-10.720	0.000	0.000	0.000	0.000
145	A	330	LEU	0	-0.010	-0.003	29.158	0.260	0.260	0.000	0.000	0.000	0.000
146	A	331	ALA	0	0.031	0.032	32.033	0.265	0.265	0.000	0.000	0.000	0.000
147	A	332	LEU	0	-0.006	-0.010	27.877	0.167	0.167	0.000	0.000	0.000	0.000
148	A	333	ILE	0	-0.051	-0.022	31.746	0.199	0.199	0.000	0.000	0.000	0.000
149	A	334	LYS	1	0.801	0.871	33.951	8.232	8.232	0.000	0.000	0.000	0.000
150	A	335	ALA	0	0.022	0.019	33.988	0.210	0.210	0.000	0.000	0.000	0.000
151	A	336	LYS	1	0.750	0.862	29.849	10.042	10.042	0.000	0.000	0.000	0.000
152	A	337	GLU	-1	-0.891	-0.919	35.756	-7.854	-7.854	0.000	0.000	0.000	0.000
153	A	338	GLU	-1	-0.931	-0.956	39.035	-7.299	-7.299	0.000	0.000	0.000	0.000
154	A	339	GLY	0	0.026	0.028	38.557	0.198	0.198	0.000	0.000	0.000	0.000
155	A	340	LEU	0	-0.086	-0.049	34.685	-0.269	-0.269	0.000	0.000	0.000	0.000
156	A	341	ASN	0	-0.029	-0.034	34.347	-0.115	-0.115	0.000	0.000	0.000	0.000
157	A	342	GLU	-1	-0.823	-0.887	35.624	-7.760	-7.760	0.000	0.000	0.000	0.000
158	A	343	TYR	0	-0.097	-0.111	33.743	-0.457	-0.457	0.000	0.000	0.000	0.000
159	A	344	VAL	0	0.047	0.037	34.257	0.219	0.219	0.000	0.000	0.000	0.000
160	A	345	ILE	0	-0.025	-0.015	33.620	-0.412	-0.412	0.000	0.000	0.000	0.000
161	A	346	PHE	0	0.002	-0.011	33.944	0.217	0.217	0.000	0.000	0.000	0.000
162	A	347	LYS	1	0.916	0.944	34.635	8.433	8.433	0.000	0.000	0.000	0.000
163	A	348	PRO	0	-0.010	-0.002	35.167	0.172	0.172	0.000	0.000	0.000	0.000
164	A	349	SER	0	0.047	0.037	37.790	0.066	0.066	0.000	0.000	0.000	0.000
165	A	350	ILE	0	-0.107	-0.052	35.375	-0.019	-0.019	0.000	0.000	0.000	0.000
166	A	351	GLU	-1	-0.953	-0.985	38.840	-7.144	-7.144	0.000	0.000	0.000	0.000
167	A	352	ILE	0	-0.016	-0.017	39.317	-0.256	-0.256	0.000	0.000	0.000	0.000
168	A	353	GLN	0	0.041	0.030	38.578	0.166	0.166	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:186:LYS)