FMO DATABASE

FMODB ID: 3JV2L

Calculation Name: 3CT6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CT6

Chain ID: A

ChEMBL ID:

UniProt ID: Q9CIV6

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	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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1116463.096503
FMO2-HF: Nuclear repulsion	1065891.133944
FMO2-HF: Total energy	-50571.96256
FMO2-MP2: Total energy	-50718.491791

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-9.516	-5.237	5.188	-3.047	-6.421	-0.02

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.034 / q_NPA : -0.019

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

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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	3	TYR	0	0.011	-0.001	2.577	-4.065	-1.051	0.779	-1.221	-2.573	-0.001
4	A	4	GLY	0	0.035	0.018	6.131	0.537	0.537	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.072	-0.030	9.860	-0.184	-0.184	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.039	0.025	12.757	0.125	0.125	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.035	-0.019	15.370	-0.037	-0.037	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.045	0.020	18.799	0.043	0.043	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.046	-0.053	21.365	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	10	HIS	0	-0.004	-0.013	25.073	0.024	0.024	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.014	-0.017	28.296	0.016	0.016	0.000	0.000	0.000	0.000
12	A	12	PRO	0	0.028	0.013	27.651	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.889	-0.932	28.121	-0.091	-0.091	0.000	0.000	0.000	0.000
14	A	14	ILE	0	0.007	0.005	26.261	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.029	0.029	23.797	-0.012	-0.012	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.003	0.001	24.170	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.030	-0.024	26.134	0.005	0.005	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.020	0.017	21.842	0.002	0.002	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.875	0.948	19.433	0.068	0.068	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.870	0.932	22.415	0.075	0.075	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.031	0.014	24.930	0.002	0.002	0.000	0.000	0.000	0.000
22	A	22	ILE	0	0.019	0.006	18.451	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.801	0.887	16.383	0.095	0.095	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-1.007	-0.989	22.105	-0.088	-0.088	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.077	-0.035	20.367	0.006	0.006	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.003	-0.001	16.966	-0.019	-0.019	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.950	0.986	18.561	0.011	0.011	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.121	-0.100	15.909	0.079	0.079	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.014	0.023	12.455	0.056	0.056	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.063	0.020	10.554	0.046	0.046	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.054	-0.020	12.608	-0.148	-0.148	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.049	-0.036	14.895	0.042	0.042	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.020	-0.027	17.152	-0.056	-0.056	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.031	0.003	20.394	0.038	0.038	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.063	0.001	23.116	-0.029	-0.029	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.008	0.020	25.957	0.021	0.021	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.007	0.011	27.615	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.848	-0.917	28.024	-0.058	-0.058	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.079	-0.053	30.652	0.004	0.004	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.008	0.000	32.742	0.004	0.004	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.874	-0.903	33.917	-0.068	-0.068	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.008	-0.008	32.062	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.010	-0.015	29.816	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.006	0.001	24.210	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	45	SER	0	0.015	-0.032	24.907	0.001	0.001	0.000	0.000	0.000	0.000
46	A	46	PHE	0	0.057	0.029	19.429	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.831	-0.914	21.151	-0.046	-0.046	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.811	0.908	22.072	0.080	0.080	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.020	-0.016	18.033	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	50	MET	0	0.056	0.038	16.117	-0.021	-0.021	0.000	0.000	0.000	0.000
51	A	51	ASN	0	-0.069	-0.050	17.498	0.045	0.045	0.000	0.000	0.000	0.000
52	A	52	ALA	0	-0.003	0.007	18.143	0.027	0.027	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.005	0.020	12.426	-0.032	-0.032	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.787	-0.885	13.284	0.182	0.182	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.921	-0.952	15.126	0.039	0.039	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.067	-0.045	11.187	0.060	0.060	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.874	-0.928	10.786	0.325	0.325	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.066	-0.020	6.880	0.341	0.341	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.861	-0.935	4.400	2.024	2.172	-0.001	-0.012	-0.135	0.000
60	A	60	ASN	0	-0.057	-0.029	2.548	-7.000	-6.090	4.407	-1.775	-3.542	-0.019
61	A	61	LEU	0	0.004	-0.002	5.600	0.235	0.235	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.026	0.003	8.306	0.007	0.007	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.004	-0.015	10.996	0.221	0.221	0.000	0.000	0.000	0.000
64	A	64	PHE	0	-0.002	-0.005	14.083	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	65	PHE	0	0.065	0.015	17.659	0.054	0.054	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.747	-0.803	21.072	-0.221	-0.221	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.055	-0.038	24.794	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.083	0.039	24.964	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.031	-0.039	25.122	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	70	ALA	0	-0.041	-0.010	22.793	0.012	0.012	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.728	0.840	15.927	0.520	0.520	0.000	0.000	0.000	0.000
72	A	72	MET	0	0.046	0.017	20.239	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.011	-0.013	21.261	0.009	0.009	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.017	0.004	16.081	0.005	0.005	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.794	-0.866	16.438	-0.491	-0.491	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.001	-0.005	16.940	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.027	-0.021	15.311	0.021	0.021	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.008	-0.009	12.230	-0.028	-0.028	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.981	-0.978	13.125	-0.260	-0.260	0.000	0.000	0.000	0.000
80	A	80	MET	0	-0.116	-0.055	15.426	0.063	0.063	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.031	-0.040	11.337	0.060	0.060	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.939	-0.957	9.553	0.210	0.210	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.802	0.909	7.261	-0.319	-0.319	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.901	-0.954	3.552	-2.252	-2.045	0.003	-0.039	-0.171	0.000
85	A	85	LEU	0	-0.003	-0.004	6.545	-0.180	-0.180	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.036	-0.013	7.968	-0.066	-0.066	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.011	-0.001	10.375	0.108	0.108	0.000	0.000	0.000	0.000
88	A	88	PHE	0	0.013	0.001	11.578	0.018	0.018	0.000	0.000	0.000	0.000
89	A	89	ASN	0	0.000	0.001	16.085	0.058	0.058	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.050	0.025	18.514	0.017	0.017	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.004	0.003	21.061	0.019	0.019	0.000	0.000	0.000	0.000
92	A	92	LEU	0	0.001	0.011	20.835	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	93	ILE	0	0.029	0.008	21.429	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.848	-0.939	22.380	-0.283	-0.283	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.042	0.034	19.735	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	96	ALA	0	0.043	0.024	17.381	-0.052	-0.052	0.000	0.000	0.000	0.000
97	A	97	TYR	0	-0.006	0.010	17.620	-0.028	-0.028	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.018	-0.025	18.133	0.005	0.005	0.000	0.000	0.000	0.000
99	A	99	ALA	0	0.000	-0.009	13.835	-0.025	-0.025	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.004	-0.020	14.115	-0.059	-0.059	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.015	0.007	15.671	0.011	0.011	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.044	-0.020	14.569	0.016	0.016	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.006	-0.002	8.602	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.786	-0.872	12.348	-0.155	-0.155	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.071	-0.028	15.034	0.057	0.057	0.000	0.000	0.000	0.000
106	A	106	GLY	0	-0.010	0.003	11.395	0.033	0.033	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.046	-0.018	11.183	-0.068	-0.068	0.000	0.000	0.000	0.000
108	A	108	THR	0	0.019	-0.002	8.591	-0.154	-0.154	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.101	0.031	6.370	0.070	0.070	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.890	-0.943	8.454	-1.095	-1.095	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.040	0.019	11.368	0.126	0.126	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.016	0.006	9.888	0.107	0.107	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.840	0.925	9.437	1.682	1.682	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.911	-0.937	13.718	-0.464	-0.464	0.000	0.000	0.000	0.000
115	A	115	GLN	0	-0.072	-0.058	16.506	0.122	0.122	0.000	0.000	0.000	0.000
116	A	116	LEU	0	0.011	0.015	14.369	0.074	0.074	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.928	-0.947	18.061	-0.409	-0.409	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.851	0.919	19.339	0.469	0.469	0.000	0.000	0.000	0.000
119	A	119	MET	0	-0.087	-0.041	20.671	0.031	0.031	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.012	0.003	19.703	0.006	0.006	0.000	0.000	0.000	0.000
121	A	121	ILE	0	-0.036	-0.017	21.928	0.039	0.039	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.818	-0.904	23.923	-0.251	-0.251	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.738	0.881	21.993	0.359	0.359	0.000	0.000	0.000	0.000
124	A	124	ARG	1	0.859	0.891	25.707	0.210	0.210	0.000	0.000	0.000	0.000
125	A	125	SER	0	-0.023	-0.001	29.203	0.012	0.012	0.000	0.000	0.000	0.000
126	A	126	HIS	0	0.022	0.003	27.605	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	127	HIS	0	0.023	0.007	30.679	0.003	0.003	0.000	0.000	0.000	0.000
128	A	128	HIS	0	-0.034	-0.017	32.570	0.008	0.008	0.000	0.000	0.000	0.000
129	A	129	HIS	0	-0.056	-0.041	35.948	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	130	HIS	0	0.003	0.020	37.915	0.007	0.007	0.000	0.000	0.000	0.000

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