FMO DATABASE

FMODB ID: MV78Z

Calculation Name: 3C8J-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3C8J

Chain ID: A

ChEMBL ID:

UniProt ID: Q64329

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	123
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1206796.515731
FMO2-HF: Nuclear repulsion	1152534.209849
FMO2-HF: Total energy	-54262.305882
FMO2-MP2: Total energy	-54414.745187

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:136:THR)

Summations of interaction energy for fragment #1(A:136:THR)

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.
-3.095	-0.08	-0.018	-1.672	-1.326	0.008

Interaction energy analysis for fragmet #1(A:136:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.069 / q_NPA : 0.034

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	138	ARG	1	0.898	0.940	3.762	-2.445	0.570	-0.018	-1.672	-1.326	0.008
4	A	139	GLY	0	-0.030	-0.003	6.689	-0.186	-0.186	0.000	0.000	0.000	0.000
5	A	140	VAL	0	0.010	0.012	9.650	-0.122	-0.122	0.000	0.000	0.000	0.000
6	A	141	LYS	1	0.924	0.970	10.668	0.022	0.022	0.000	0.000	0.000	0.000
7	A	142	TYR	0	-0.016	0.001	14.571	-0.057	-0.057	0.000	0.000	0.000	0.000
8	A	143	TRP	0	0.007	-0.007	16.850	0.047	0.047	0.000	0.000	0.000	0.000
9	A	144	PHE	0	0.031	0.016	19.545	-0.020	-0.020	0.000	0.000	0.000	0.000
10	A	145	CYS	0	-0.022	0.001	23.143	0.002	0.002	0.000	0.000	0.000	0.000
11	A	146	TYR	0	0.016	-0.007	26.195	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	147	SER	0	0.009	0.021	29.661	0.006	0.006	0.000	0.000	0.000	0.000
13	A	148	THR	0	0.022	0.015	31.173	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	149	LYS	1	0.860	0.940	26.853	-0.059	-0.059	0.000	0.000	0.000	0.000
15	A	151	TYR	0	-0.052	-0.098	22.423	0.015	0.015	0.000	0.000	0.000	0.000
16	A	152	TYR	0	0.002	0.001	15.290	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	153	PHE	0	0.014	0.009	18.825	0.028	0.028	0.000	0.000	0.000	0.000
18	A	154	ILE	0	-0.014	-0.032	13.463	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	155	MET	0	-0.021	-0.013	15.651	0.028	0.028	0.000	0.000	0.000	0.000
20	A	156	ASN	0	0.038	0.028	11.069	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	157	LYS	1	0.934	0.963	14.490	-0.032	-0.032	0.000	0.000	0.000	0.000
22	A	158	THR	0	0.000	-0.004	13.075	0.044	0.044	0.000	0.000	0.000	0.000
23	A	159	THR	0	0.022	0.028	15.768	-0.036	-0.036	0.000	0.000	0.000	0.000
24	A	160	TRP	0	0.053	0.017	17.950	0.043	0.043	0.000	0.000	0.000	0.000
25	A	161	SER	0	0.028	-0.004	18.368	0.011	0.011	0.000	0.000	0.000	0.000
26	A	162	GLY	0	0.026	0.025	14.846	0.038	0.038	0.000	0.000	0.000	0.000
27	A	163	CYS	0	-0.041	0.007	14.542	0.066	0.066	0.000	0.000	0.000	0.000
28	A	164	LYS	1	0.990	0.985	16.601	-0.271	-0.271	0.000	0.000	0.000	0.000
29	A	165	ALA	0	-0.031	-0.018	13.474	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	166	ASN	0	-0.030	-0.038	11.281	0.142	0.142	0.000	0.000	0.000	0.000
31	A	167	CYS	0	-0.061	-0.006	12.909	0.000	0.000	0.000	0.000	0.000	0.000
32	A	168	GLN	0	0.026	0.012	15.463	-0.061	-0.061	0.000	0.000	0.000	0.000
33	A	169	HIS	0	-0.044	-0.002	7.897	0.035	0.035	0.000	0.000	0.000	0.000
34	A	170	TYR	0	-0.015	-0.015	9.211	0.009	0.009	0.000	0.000	0.000	0.000
35	A	171	GLY	0	0.022	0.013	14.072	-0.058	-0.058	0.000	0.000	0.000	0.000
36	A	172	VAL	0	-0.061	-0.027	17.178	-0.036	-0.036	0.000	0.000	0.000	0.000
37	A	173	PRO	0	0.040	0.014	18.542	0.030	0.030	0.000	0.000	0.000	0.000
38	A	174	ILE	0	-0.003	-0.015	19.982	-0.018	-0.018	0.000	0.000	0.000	0.000
39	A	175	LEU	0	-0.011	-0.010	21.178	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	176	LYS	1	0.858	0.960	24.281	-0.077	-0.077	0.000	0.000	0.000	0.000
41	A	177	ILE	0	-0.048	-0.025	27.727	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	178	GLU	-1	-0.878	-0.936	30.504	0.066	0.066	0.000	0.000	0.000	0.000
43	A	179	ASP	-1	-0.857	-0.951	33.635	0.034	0.034	0.000	0.000	0.000	0.000
44	A	180	GLU	-1	-0.902	-0.984	34.952	0.035	0.035	0.000	0.000	0.000	0.000
45	A	181	ASP	-1	-0.883	-0.921	36.719	0.018	0.018	0.000	0.000	0.000	0.000
46	A	182	GLU	-1	-0.742	-0.808	29.561	0.051	0.051	0.000	0.000	0.000	0.000
47	A	183	LEU	0	-0.024	-0.014	31.832	0.000	0.000	0.000	0.000	0.000	0.000
48	A	184	LYS	1	0.939	0.958	32.283	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	185	PHE	0	-0.039	-0.006	28.196	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	186	LEU	0	0.054	0.018	26.563	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	187	GLN	0	-0.010	0.006	29.034	0.001	0.001	0.000	0.000	0.000	0.000
52	A	188	ARG	1	0.971	0.982	31.269	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	189	HIS	0	-0.020	0.016	25.155	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	190	VAL	0	-0.019	0.000	24.866	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	191	ILE	0	0.065	0.040	22.629	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	192	PRO	0	-0.011	-0.012	25.828	0.013	0.013	0.000	0.000	0.000	0.000
57	A	193	GLY	0	0.014	0.003	24.433	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	194	ASN	0	-0.015	-0.002	23.913	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	195	TYR	0	-0.026	-0.031	21.663	0.012	0.012	0.000	0.000	0.000	0.000
60	A	196	TRP	0	-0.022	-0.003	19.657	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	197	ILE	0	0.029	0.005	22.681	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	198	GLY	0	-0.009	0.001	24.372	0.014	0.014	0.000	0.000	0.000	0.000
63	A	199	LEU	0	-0.010	-0.004	25.093	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	200	SER	0	-0.021	-0.018	26.173	0.008	0.008	0.000	0.000	0.000	0.000
65	A	201	TYR	0	0.028	0.018	28.309	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	202	ASP	-1	-0.815	-0.906	29.890	0.148	0.148	0.000	0.000	0.000	0.000
67	A	203	LYS	1	0.939	0.939	27.912	-0.192	-0.192	0.000	0.000	0.000	0.000
68	A	204	LYS	1	0.904	0.949	30.566	-0.146	-0.146	0.000	0.000	0.000	0.000
69	A	205	LYS	1	0.965	0.983	34.201	-0.112	-0.112	0.000	0.000	0.000	0.000
70	A	206	LYS	1	0.885	0.955	35.427	-0.100	-0.100	0.000	0.000	0.000	0.000
71	A	207	GLU	-1	-0.902	-0.940	35.216	0.077	0.077	0.000	0.000	0.000	0.000
72	A	208	TRP	0	-0.029	-0.007	30.375	0.011	0.011	0.000	0.000	0.000	0.000
73	A	209	ALA	0	0.038	0.019	30.370	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	210	TRP	0	0.030	0.002	28.491	0.012	0.012	0.000	0.000	0.000	0.000
75	A	211	ILE	0	-0.033	-0.027	22.491	0.007	0.007	0.000	0.000	0.000	0.000
76	A	212	ASP	-1	-0.850	-0.927	26.294	0.103	0.103	0.000	0.000	0.000	0.000
77	A	213	ASN	0	-0.081	-0.035	28.390	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	214	GLY	0	0.022	0.027	31.499	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	215	PRO	0	0.001	-0.010	33.653	0.004	0.004	0.000	0.000	0.000	0.000
80	A	216	SER	0	-0.004	-0.019	33.492	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	217	LYS	1	0.941	0.965	35.618	-0.042	-0.042	0.000	0.000	0.000	0.000
82	A	218	LEU	0	0.018	0.011	33.394	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	219	ASP	-1	-0.794	-0.880	35.727	0.073	0.073	0.000	0.000	0.000	0.000
84	A	220	MET	0	-0.034	-0.023	38.027	0.000	0.000	0.000	0.000	0.000	0.000
85	A	221	LYS	1	0.963	0.986	37.190	-0.044	-0.044	0.000	0.000	0.000	0.000
86	A	222	ILE	0	0.018	-0.001	33.793	0.000	0.000	0.000	0.000	0.000	0.000
87	A	223	LYS	1	0.971	0.987	37.927	-0.051	-0.051	0.000	0.000	0.000	0.000
88	A	224	LYS	1	0.904	0.960	40.238	-0.039	-0.039	0.000	0.000	0.000	0.000
89	A	225	MET	0	-0.047	-0.037	37.389	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	226	ASN	0	-0.086	-0.023	39.270	0.003	0.003	0.000	0.000	0.000	0.000
91	A	227	PHE	0	0.041	0.027	33.639	0.000	0.000	0.000	0.000	0.000	0.000
92	A	228	LYS	1	0.961	0.987	36.419	-0.064	-0.064	0.000	0.000	0.000	0.000
93	A	229	SER	0	-0.048	-0.033	31.957	0.006	0.006	0.000	0.000	0.000	0.000
94	A	230	ARG	1	0.944	0.968	32.359	-0.105	-0.105	0.000	0.000	0.000	0.000
95	A	231	GLY	0	-0.035	-0.020	28.698	0.012	0.012	0.000	0.000	0.000	0.000
96	A	232	CYS	0	-0.069	-0.050	23.531	0.006	0.006	0.000	0.000	0.000	0.000
97	A	233	VAL	0	0.079	0.042	27.188	-0.011	-0.011	0.000	0.000	0.000	0.000
98	A	234	PHE	0	-0.060	-0.020	25.489	0.014	0.014	0.000	0.000	0.000	0.000
99	A	235	LEU	0	-0.006	-0.002	26.531	-0.011	-0.011	0.000	0.000	0.000	0.000
100	A	236	SER	0	0.061	0.025	27.014	0.001	0.001	0.000	0.000	0.000	0.000
101	A	237	LYS	1	0.808	0.872	29.329	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	238	ALA	0	-0.003	0.001	31.503	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	239	ARG	1	0.928	0.971	32.741	-0.047	-0.047	0.000	0.000	0.000	0.000
104	A	240	ILE	0	-0.011	-0.006	31.031	0.002	0.002	0.000	0.000	0.000	0.000
105	A	241	GLU	-1	-0.929	-0.966	30.904	0.063	0.063	0.000	0.000	0.000	0.000
106	A	242	ASP	-1	-0.777	-0.877	30.498	0.099	0.099	0.000	0.000	0.000	0.000
107	A	243	ILE	0	0.006	0.009	26.642	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	244	ASP	-1	-0.841	-0.929	25.863	0.200	0.200	0.000	0.000	0.000	0.000
109	A	246	ASN	0	-0.009	-0.011	21.132	0.048	0.048	0.000	0.000	0.000	0.000
110	A	247	ILE	0	0.000	0.012	20.925	0.012	0.012	0.000	0.000	0.000	0.000
111	A	248	PRO	0	0.020	0.000	17.619	0.014	0.014	0.000	0.000	0.000	0.000
112	A	249	TYR	0	-0.008	-0.011	19.312	-0.044	-0.044	0.000	0.000	0.000	0.000
113	A	250	TYR	0	-0.001	0.016	17.949	0.028	0.028	0.000	0.000	0.000	0.000
114	A	252	ILE	0	0.036	0.033	19.116	-0.016	-0.016	0.000	0.000	0.000	0.000
115	A	254	GLY	0	0.027	0.002	20.310	-0.027	-0.027	0.000	0.000	0.000	0.000
116	A	255	LYS	1	0.941	0.967	22.281	-0.069	-0.069	0.000	0.000	0.000	0.000
117	A	256	LYS	1	0.962	0.988	24.699	-0.066	-0.066	0.000	0.000	0.000	0.000
118	A	257	LEU	0	0.005	0.000	25.667	0.003	0.003	0.000	0.000	0.000	0.000
119	A	258	ASP	-1	-0.914	-0.954	28.672	0.036	0.036	0.000	0.000	0.000	0.000
120	A	259	LYS	1	0.922	0.952	27.837	0.008	0.008	0.000	0.000	0.000	0.000
121	A	260	PHE	0	-0.038	-0.009	30.535	0.002	0.002	0.000	0.000	0.000	0.000
122	A	261	PRO	0	-0.028	-0.022	26.489	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	262	ASP	-1	-0.898	-0.931	26.347	-0.034	-0.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:136:THR)