FMO DATABASE

FMODB ID: V57J1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1163220.470919
FMO2-HF: Nuclear repulsion	1110030.24699
FMO2-HF: Total energy	-53190.22393
FMO2-MP2: Total energy	-53338.689887

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.
-4.264	-0.243	0.576	-1.758	-2.839	-0.005

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 : -0.039 / q_NPA : -0.037

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	-0.109	-0.025	2.392	0.357	3.288	0.371	-1.443	-1.859	-0.004
4	A	103	ASP	-1	-0.763	-0.847	3.920	-3.406	-3.185	0.002	-0.078	-0.144	0.000
5	A	104	THR	0	0.034	-0.012	6.129	0.032	0.032	0.000	0.000	0.000	0.000
6	A	105	ASN	0	-0.052	-0.029	7.526	0.217	0.217	0.000	0.000	0.000	0.000
7	A	106	TRP	0	0.030	0.026	6.888	0.313	0.313	0.000	0.000	0.000	0.000
8	A	107	ARG	1	0.843	0.919	5.118	-0.054	-0.054	0.000	0.000	0.000	0.000
9	A	108	TYR	0	0.055	0.008	2.759	-1.690	-0.894	0.204	-0.231	-0.770	-0.001
10	A	109	TYR	0	-0.075	-0.063	4.706	0.701	0.774	-0.001	-0.006	-0.066	0.000
11	A	110	GLY	0	0.055	0.038	8.070	-0.370	-0.370	0.000	0.000	0.000	0.000
12	A	111	ASP	-1	-0.825	-0.915	9.259	0.313	0.313	0.000	0.000	0.000	0.000
13	A	112	SER	0	0.008	-0.014	9.212	-0.248	-0.248	0.000	0.000	0.000	0.000
14	A	114	TYR	0	-0.016	-0.034	7.638	-0.053	-0.053	0.000	0.000	0.000	0.000
15	A	115	GLY	0	0.030	0.026	9.164	0.004	0.004	0.000	0.000	0.000	0.000
16	A	116	PHE	0	-0.010	-0.017	10.403	0.046	0.046	0.000	0.000	0.000	0.000
17	A	117	PHE	0	0.077	0.036	12.986	-0.034	-0.034	0.000	0.000	0.000	0.000
18	A	118	ARG	1	0.888	0.940	17.237	0.106	0.106	0.000	0.000	0.000	0.000
19	A	119	HIS	0	0.052	0.043	19.782	-0.028	-0.028	0.000	0.000	0.000	0.000
20	A	120	ASN	0	-0.036	-0.028	22.737	0.019	0.019	0.000	0.000	0.000	0.000
21	A	121	LEU	0	0.021	0.013	23.512	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	122	THR	0	0.026	-0.013	26.868	0.013	0.013	0.000	0.000	0.000	0.000
23	A	123	TRP	0	-0.023	-0.010	24.650	-0.012	-0.012	0.000	0.000	0.000	0.000
24	A	124	GLU	-1	-0.825	-0.929	25.791	-0.052	-0.052	0.000	0.000	0.000	0.000
25	A	125	GLU	-1	-0.847	-0.898	26.659	-0.078	-0.078	0.000	0.000	0.000	0.000
26	A	126	SER	0	-0.053	-0.045	22.293	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	127	LYS	1	0.865	0.919	21.773	0.026	0.026	0.000	0.000	0.000	0.000
28	A	128	GLN	0	-0.042	-0.019	22.365	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	129	TYR	0	0.020	-0.008	17.714	-0.031	-0.031	0.000	0.000	0.000	0.000
30	A	130	CYS	0	-0.050	-0.019	14.467	-0.027	-0.027	0.000	0.000	0.000	0.000
31	A	131	THR	0	-0.002	0.001	18.307	-0.033	-0.033	0.000	0.000	0.000	0.000
32	A	132	ASP	-1	-0.868	-0.915	20.517	-0.207	-0.207	0.000	0.000	0.000	0.000
33	A	133	MET	0	-0.129	-0.055	15.320	-0.059	-0.059	0.000	0.000	0.000	0.000
34	A	134	ASN	0	-0.061	-0.028	15.472	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	135	ALA	0	-0.044	-0.018	14.609	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	136	THR	0	0.006	0.000	16.040	0.022	0.022	0.000	0.000	0.000	0.000
37	A	137	LEU	0	0.016	0.014	16.726	0.009	0.009	0.000	0.000	0.000	0.000
38	A	138	LEU	0	-0.038	-0.016	14.238	0.012	0.012	0.000	0.000	0.000	0.000
39	A	139	LYS	1	0.869	0.947	16.921	-0.131	-0.131	0.000	0.000	0.000	0.000
40	A	140	ILE	0	-0.046	-0.026	17.072	0.042	0.042	0.000	0.000	0.000	0.000
41	A	141	ASP	-1	-0.797	-0.909	18.607	0.147	0.147	0.000	0.000	0.000	0.000
42	A	142	ASN	0	0.013	-0.005	17.254	0.029	0.029	0.000	0.000	0.000	0.000
43	A	143	ARG	1	0.962	0.953	19.805	-0.285	-0.285	0.000	0.000	0.000	0.000
44	A	144	ASN	0	0.013	0.041	15.368	0.086	0.086	0.000	0.000	0.000	0.000
45	A	145	ILE	0	0.021	0.018	13.194	0.067	0.067	0.000	0.000	0.000	0.000
46	A	146	VAL	0	0.019	0.028	16.124	0.008	0.008	0.000	0.000	0.000	0.000
47	A	147	GLU	-1	-0.872	-0.945	17.733	0.367	0.367	0.000	0.000	0.000	0.000
48	A	148	TYR	0	0.005	0.009	7.528	0.013	0.013	0.000	0.000	0.000	0.000
49	A	149	ILE	0	0.018	0.001	13.125	0.018	0.018	0.000	0.000	0.000	0.000
50	A	150	LYS	1	0.934	0.970	15.340	-0.360	-0.360	0.000	0.000	0.000	0.000
51	A	151	ALA	0	-0.042	-0.005	14.420	-0.040	-0.040	0.000	0.000	0.000	0.000
52	A	152	ARG	1	0.865	0.933	7.566	-1.341	-1.341	0.000	0.000	0.000	0.000
53	A	153	THR	0	-0.030	-0.004	13.798	-0.096	-0.096	0.000	0.000	0.000	0.000
54	A	154	HIS	0	0.040	0.033	17.036	0.031	0.031	0.000	0.000	0.000	0.000
55	A	155	LEU	0	-0.076	-0.033	20.434	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	156	ILE	0	0.026	0.016	21.490	0.013	0.013	0.000	0.000	0.000	0.000
57	A	157	ARG	1	0.817	0.889	17.724	-0.048	-0.048	0.000	0.000	0.000	0.000
58	A	158	TRP	0	-0.032	-0.027	21.748	0.027	0.027	0.000	0.000	0.000	0.000
59	A	159	VAL	0	-0.034	-0.016	19.297	0.007	0.007	0.000	0.000	0.000	0.000
60	A	160	GLY	0	0.040	0.016	20.726	-0.018	-0.018	0.000	0.000	0.000	0.000
61	A	161	LEU	0	-0.025	-0.001	22.260	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	162	SER	0	-0.009	-0.020	25.310	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	163	ARG	1	0.859	0.944	28.683	-0.029	-0.029	0.000	0.000	0.000	0.000
64	A	164	GLN	0	-0.036	-0.026	32.122	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	165	LYS	1	0.886	0.925	33.913	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	166	SER	0	0.042	0.004	36.672	0.004	0.004	0.000	0.000	0.000	0.000
67	A	167	ASN	0	-0.055	-0.031	38.108	0.001	0.001	0.000	0.000	0.000	0.000
68	A	168	GLU	-1	-0.858	-0.874	35.821	0.018	0.018	0.000	0.000	0.000	0.000
69	A	169	VAL	0	0.023	-0.004	33.149	0.003	0.003	0.000	0.000	0.000	0.000
70	A	170	TRP	0	-0.002	0.004	29.160	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	171	LYS	1	0.916	0.964	27.936	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	172	TRP	0	0.067	0.032	21.562	0.000	0.000	0.000	0.000	0.000	0.000
73	A	173	GLU	-1	-0.764	-0.871	21.558	-0.037	-0.037	0.000	0.000	0.000	0.000
74	A	174	ASP	-1	-0.828	-0.861	21.618	0.058	0.058	0.000	0.000	0.000	0.000
75	A	175	GLY	0	-0.017	-0.007	23.632	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	176	SER	0	-0.091	-0.081	24.275	0.007	0.007	0.000	0.000	0.000	0.000
77	A	177	VAL	0	-0.003	-0.019	26.834	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	178	ILE	0	-0.032	-0.009	25.919	0.008	0.008	0.000	0.000	0.000	0.000
79	A	179	SER	0	0.002	-0.017	24.527	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	180	GLU	-1	-0.842	-0.931	27.468	0.096	0.096	0.000	0.000	0.000	0.000
81	A	181	ASN	0	-0.034	-0.036	26.070	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	182	MET	0	-0.065	-0.019	22.462	0.019	0.019	0.000	0.000	0.000	0.000
83	A	183	PHE	0	0.006	0.013	26.547	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	184	GLU	-1	-0.954	-0.953	28.236	0.166	0.166	0.000	0.000	0.000	0.000
85	A	185	PHE	0	-0.047	-0.036	24.564	0.010	0.010	0.000	0.000	0.000	0.000
86	A	186	LEU	0	-0.056	-0.023	26.848	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	187	GLU	-1	-0.788	-0.877	29.034	0.105	0.105	0.000	0.000	0.000	0.000
88	A	188	ASP	-1	-0.895	-0.943	31.516	0.060	0.060	0.000	0.000	0.000	0.000
89	A	189	GLY	0	-0.011	-0.025	34.029	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	190	LYS	1	0.903	0.937	35.733	-0.033	-0.033	0.000	0.000	0.000	0.000
91	A	191	GLY	0	0.053	0.017	37.048	0.001	0.001	0.000	0.000	0.000	0.000
92	A	192	ASN	0	0.011	-0.007	38.129	0.002	0.002	0.000	0.000	0.000	0.000
93	A	193	MET	0	-0.060	0.031	33.825	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	194	ASN	0	0.063	0.016	33.012	0.009	0.009	0.000	0.000	0.000	0.000
95	A	195	CYS	0	0.082	0.054	28.132	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	196	ALA	0	0.060	0.030	26.239	0.002	0.002	0.000	0.000	0.000	0.000
97	A	197	TYR	0	-0.057	-0.017	24.177	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	198	PHE	0	0.031	0.013	19.492	0.012	0.012	0.000	0.000	0.000	0.000
99	A	199	HIS	0	-0.017	-0.037	22.690	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	200	ASN	0	0.000	-0.010	21.950	0.012	0.012	0.000	0.000	0.000	0.000
101	A	201	GLY	0	-0.007	-0.015	21.940	0.002	0.002	0.000	0.000	0.000	0.000
102	A	202	LYS	1	0.812	0.921	22.864	-0.118	-0.118	0.000	0.000	0.000	0.000
103	A	203	MET	0	-0.003	-0.006	23.507	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	204	HIS	0	0.034	0.015	25.865	-0.010	-0.010	0.000	0.000	0.000	0.000
105	A	205	PRO	0	0.030	0.023	28.688	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	206	THR	0	-0.035	-0.032	29.652	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	207	PHE	0	-0.016	-0.014	32.266	0.000	0.000	0.000	0.000	0.000	0.000
108	A	209	GLU	-1	-0.839	-0.929	30.802	-0.016	-0.016	0.000	0.000	0.000	0.000
109	A	210	ASN	0	-0.051	-0.017	31.363	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	211	LYS	1	0.950	0.978	28.954	0.049	0.049	0.000	0.000	0.000	0.000
111	A	212	HIS	1	0.858	0.926	25.084	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	213	TYR	0	0.023	0.028	20.998	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	214	LEU	0	0.040	0.030	18.290	0.019	0.019	0.000	0.000	0.000	0.000
114	A	215	MET	0	-0.024	-0.003	15.100	0.018	0.018	0.000	0.000	0.000	0.000
115	A	217	GLU	-1	-0.764	-0.874	12.191	0.246	0.246	0.000	0.000	0.000	0.000
116	A	218	ARG	1	0.837	0.900	8.997	0.870	0.870	0.000	0.000	0.000	0.000
117	A	219	LYS	1	0.858	0.940	10.510	0.028	0.028	0.000	0.000	0.000	0.000
118	A	220	ALA	0	-0.017	-0.014	6.830	-0.167	-0.167	0.000	0.000	0.000	0.000
119	A	221	GLY	0	-0.005	0.005	7.816	0.200	0.200	0.000	0.000	0.000	0.000

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