FMO DATABASE

FMODB ID: 17Z8Z

Calculation Name: 2C6U-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2C6U

Chain ID: A

ChEMBL ID:

UniProt ID: Q9P126

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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1163332.570969
FMO2-HF: Nuclear repulsion	1110141.989956
FMO2-HF: Total energy	-53190.581013
FMO2-MP2: Total energy	-53338.999355

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:100:SER)

Summations of interaction energy for fragment #1(A:100:SER)

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.
-4.72	-0.394	0.451	-1.819	-2.959	-0.003

Interaction energy analysis for fragmet #1(A:100:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.022

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	102	CYS	0	-0.065	-0.030	2.916	1.154	3.972	0.174	-1.337	-1.655	-0.001
4	A	103	ASP	-1	-0.772	-0.849	3.740	-3.491	-3.149	0.007	-0.126	-0.223	-0.001
5	A	104	THR	0	0.035	-0.005	6.133	0.164	0.164	0.000	0.000	0.000	0.000
6	A	105	ASN	0	-0.074	-0.043	7.553	0.217	0.217	0.000	0.000	0.000	0.000
7	A	106	TRP	0	0.027	0.033	6.493	0.299	0.299	0.000	0.000	0.000	0.000
8	A	107	ARG	1	0.849	0.915	4.628	-0.424	-0.292	-0.001	-0.004	-0.128	0.000
9	A	108	TYR	0	0.060	0.010	2.654	-2.042	-1.088	0.272	-0.340	-0.886	-0.001
10	A	109	TYR	0	-0.060	-0.039	4.462	0.566	0.646	-0.001	-0.012	-0.067	0.000
11	A	110	GLY	0	0.064	0.035	7.936	-0.390	-0.390	0.000	0.000	0.000	0.000
12	A	111	ASP	-1	-0.819	-0.889	9.494	0.227	0.227	0.000	0.000	0.000	0.000
13	A	112	SER	0	-0.005	-0.019	9.101	-0.264	-0.264	0.000	0.000	0.000	0.000
14	A	114	TYR	0	-0.005	-0.025	7.289	-0.094	-0.094	0.000	0.000	0.000	0.000
15	A	115	GLY	0	0.034	0.018	8.684	0.083	0.083	0.000	0.000	0.000	0.000
16	A	116	PHE	0	-0.001	-0.011	9.716	0.006	0.006	0.000	0.000	0.000	0.000
17	A	117	PHE	0	0.083	0.042	12.388	0.018	0.018	0.000	0.000	0.000	0.000
18	A	118	ARG	1	0.914	0.952	16.676	0.045	0.045	0.000	0.000	0.000	0.000
19	A	119	HIS	0	0.058	0.048	19.797	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	120	ASN	0	-0.012	-0.018	22.686	0.020	0.020	0.000	0.000	0.000	0.000
21	A	121	LEU	0	0.004	0.001	23.066	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	122	THR	0	0.031	0.000	26.423	0.013	0.013	0.000	0.000	0.000	0.000
23	A	123	TRP	0	-0.007	0.008	24.049	-0.012	-0.012	0.000	0.000	0.000	0.000
24	A	124	GLU	-1	-0.792	-0.922	24.999	-0.033	-0.033	0.000	0.000	0.000	0.000
25	A	125	GLU	-1	-0.776	-0.844	26.075	-0.056	-0.056	0.000	0.000	0.000	0.000
26	A	126	SER	0	-0.044	-0.047	21.671	-0.015	-0.015	0.000	0.000	0.000	0.000
27	A	127	LYS	1	0.873	0.940	21.110	0.011	0.011	0.000	0.000	0.000	0.000
28	A	128	GLN	0	-0.069	-0.023	21.927	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	129	TYR	0	0.029	-0.004	17.312	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	130	CYS	0	-0.064	-0.022	14.115	-0.023	-0.023	0.000	0.000	0.000	0.000
31	A	131	THR	0	0.022	0.010	17.765	-0.035	-0.035	0.000	0.000	0.000	0.000
32	A	132	ASP	-1	-0.872	-0.925	20.004	-0.192	-0.192	0.000	0.000	0.000	0.000
33	A	133	MET	0	-0.116	-0.050	14.831	-0.059	-0.059	0.000	0.000	0.000	0.000
34	A	134	ASN	0	-0.058	-0.029	15.078	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	135	ALA	0	-0.044	-0.016	14.248	-0.024	-0.024	0.000	0.000	0.000	0.000
36	A	136	THR	0	0.024	0.014	15.780	0.017	0.017	0.000	0.000	0.000	0.000
37	A	137	LEU	0	0.008	0.004	16.374	0.012	0.012	0.000	0.000	0.000	0.000
38	A	138	LEU	0	-0.037	-0.019	13.680	0.010	0.010	0.000	0.000	0.000	0.000
39	A	139	LYS	1	0.843	0.934	16.449	-0.147	-0.147	0.000	0.000	0.000	0.000
40	A	140	ILE	0	-0.045	-0.037	16.648	0.050	0.050	0.000	0.000	0.000	0.000
41	A	141	ASP	-1	-0.752	-0.870	18.709	0.160	0.160	0.000	0.000	0.000	0.000
42	A	142	ASN	0	0.010	-0.017	17.008	0.026	0.026	0.000	0.000	0.000	0.000
43	A	143	ARG	1	0.970	0.963	19.639	-0.296	-0.296	0.000	0.000	0.000	0.000
44	A	144	ASN	0	-0.004	0.018	15.497	0.095	0.095	0.000	0.000	0.000	0.000
45	A	145	ILE	0	0.015	0.018	12.904	0.085	0.085	0.000	0.000	0.000	0.000
46	A	146	VAL	0	0.020	0.022	15.877	0.017	0.017	0.000	0.000	0.000	0.000
47	A	147	GLU	-1	-0.865	-0.935	17.642	0.423	0.423	0.000	0.000	0.000	0.000
48	A	148	TYR	0	0.018	0.004	7.132	0.017	0.017	0.000	0.000	0.000	0.000
49	A	149	ILE	0	0.032	0.016	12.677	0.035	0.035	0.000	0.000	0.000	0.000
50	A	150	LYS	1	0.887	0.946	15.056	-0.440	-0.440	0.000	0.000	0.000	0.000
51	A	151	ALA	0	-0.043	-0.011	14.190	-0.045	-0.045	0.000	0.000	0.000	0.000
52	A	152	ARG	1	0.840	0.919	7.259	-1.661	-1.661	0.000	0.000	0.000	0.000
53	A	153	THR	0	-0.040	-0.012	13.231	-0.098	-0.098	0.000	0.000	0.000	0.000
54	A	154	HIS	0	0.039	0.033	16.647	0.029	0.029	0.000	0.000	0.000	0.000
55	A	155	LEU	0	-0.065	-0.033	19.965	-0.037	-0.037	0.000	0.000	0.000	0.000
56	A	156	ILE	0	0.025	0.016	20.938	0.016	0.016	0.000	0.000	0.000	0.000
57	A	157	ARG	1	0.784	0.872	16.765	-0.123	-0.123	0.000	0.000	0.000	0.000
58	A	158	TRP	0	-0.047	-0.037	21.367	0.025	0.025	0.000	0.000	0.000	0.000
59	A	159	VAL	0	-0.010	-0.004	18.748	0.014	0.014	0.000	0.000	0.000	0.000
60	A	160	GLY	0	0.033	0.025	20.046	-0.021	-0.021	0.000	0.000	0.000	0.000
61	A	161	LEU	0	-0.035	-0.014	21.615	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	162	SER	0	-0.022	-0.025	24.782	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	163	ARG	1	0.870	0.916	28.234	-0.042	-0.042	0.000	0.000	0.000	0.000
64	A	164	GLN	0	-0.039	-0.028	31.632	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	165	LYS	1	0.883	0.928	33.840	-0.023	-0.023	0.000	0.000	0.000	0.000
66	A	166	SER	0	0.051	0.010	36.251	0.004	0.004	0.000	0.000	0.000	0.000
67	A	167	ASN	0	-0.056	-0.033	38.067	0.000	0.000	0.000	0.000	0.000	0.000
68	A	168	GLU	-1	-0.860	-0.872	35.359	0.029	0.029	0.000	0.000	0.000	0.000
69	A	169	VAL	0	0.032	0.015	33.085	0.004	0.004	0.000	0.000	0.000	0.000
70	A	170	TRP	0	0.007	0.006	29.005	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	171	LYS	1	0.869	0.932	27.944	-0.033	-0.033	0.000	0.000	0.000	0.000
72	A	172	TRP	0	0.032	0.016	21.199	0.004	0.004	0.000	0.000	0.000	0.000
73	A	173	GLU	-1	-0.786	-0.898	21.421	-0.021	-0.021	0.000	0.000	0.000	0.000
74	A	174	ASP	-1	-0.814	-0.855	21.015	0.072	0.072	0.000	0.000	0.000	0.000
75	A	175	GLY	0	0.005	0.011	22.977	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	176	SER	0	-0.069	-0.064	24.176	0.005	0.005	0.000	0.000	0.000	0.000
77	A	177	VAL	0	-0.002	-0.019	26.835	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	178	ILE	0	-0.018	-0.004	25.410	0.008	0.008	0.000	0.000	0.000	0.000
79	A	179	SER	0	-0.008	-0.026	24.159	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	180	GLU	-1	-0.854	-0.937	26.923	0.114	0.114	0.000	0.000	0.000	0.000
81	A	181	ASN	0	-0.028	-0.029	25.805	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	182	MET	0	-0.072	-0.003	21.938	0.021	0.021	0.000	0.000	0.000	0.000
83	A	183	PHE	0	-0.004	0.003	26.221	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	184	GLU	-1	-0.957	-0.962	27.798	0.191	0.191	0.000	0.000	0.000	0.000
85	A	185	PHE	0	-0.061	-0.041	24.457	0.012	0.012	0.000	0.000	0.000	0.000
86	A	186	LEU	0	-0.035	-0.015	26.110	0.002	0.002	0.000	0.000	0.000	0.000
87	A	187	GLU	-1	-0.801	-0.884	28.627	0.129	0.129	0.000	0.000	0.000	0.000
88	A	188	ASP	-1	-0.861	-0.940	31.146	0.063	0.063	0.000	0.000	0.000	0.000
89	A	189	GLY	0	0.034	0.010	33.594	0.000	0.000	0.000	0.000	0.000	0.000
90	A	190	LYS	1	0.840	0.910	35.377	-0.058	-0.058	0.000	0.000	0.000	0.000
91	A	191	GLY	0	0.061	0.025	36.993	0.001	0.001	0.000	0.000	0.000	0.000
92	A	192	ASN	0	0.019	0.001	38.038	0.003	0.003	0.000	0.000	0.000	0.000
93	A	193	MET	0	-0.084	0.002	33.444	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	194	ASN	0	0.061	0.029	32.663	0.009	0.009	0.000	0.000	0.000	0.000
95	A	195	CYS	0	0.039	0.033	27.657	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	196	ALA	0	0.050	0.026	26.188	0.002	0.002	0.000	0.000	0.000	0.000
97	A	197	TYR	0	-0.040	-0.013	23.656	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	198	PHE	0	0.050	0.022	19.304	0.010	0.010	0.000	0.000	0.000	0.000
99	A	199	HIS	0	0.004	-0.029	22.389	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	200	ASN	0	-0.007	-0.014	21.669	0.014	0.014	0.000	0.000	0.000	0.000
101	A	201	GLY	0	0.011	0.005	21.357	0.009	0.009	0.000	0.000	0.000	0.000
102	A	202	LYS	1	0.812	0.910	22.314	-0.148	-0.148	0.000	0.000	0.000	0.000
103	A	203	MET	0	0.003	0.000	22.895	0.002	0.002	0.000	0.000	0.000	0.000
104	A	204	HIS	0	0.018	0.011	25.398	-0.016	-0.016	0.000	0.000	0.000	0.000
105	A	205	PRO	0	0.035	0.018	28.340	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	206	THR	0	-0.020	-0.016	29.151	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	207	PHE	0	0.011	0.000	31.868	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	209	GLU	-1	-0.818	-0.935	30.011	0.001	0.001	0.000	0.000	0.000	0.000
109	A	210	ASN	0	-0.064	-0.034	31.001	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	211	LYS	1	0.805	0.908	28.531	0.044	0.044	0.000	0.000	0.000	0.000
111	A	212	HIS	1	0.851	0.923	24.789	-0.030	-0.030	0.000	0.000	0.000	0.000
112	A	213	TYR	0	0.027	0.031	20.613	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	214	LEU	0	0.017	0.019	17.869	0.014	0.014	0.000	0.000	0.000	0.000
114	A	215	MET	0	-0.038	-0.005	14.684	0.036	0.036	0.000	0.000	0.000	0.000
115	A	217	GLU	-1	-0.773	-0.877	11.786	0.286	0.286	0.000	0.000	0.000	0.000
116	A	218	ARG	1	0.843	0.908	8.633	0.858	0.858	0.000	0.000	0.000	0.000
117	A	219	LYS	1	0.850	0.926	10.328	0.046	0.046	0.000	0.000	0.000	0.000
118	A	220	ALA	0	0.006	-0.005	6.706	-0.187	-0.187	0.000	0.000	0.000	0.000
119	A	221	GLY	0	-0.020	-0.003	7.692	0.192	0.192	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:100:SER)