FMO DATABASE

FMODB ID: YZLJ2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1161388.781553
FMO2-HF: Nuclear repulsion	1108199.041879
FMO2-HF: Total energy	-53189.739673
FMO2-MP2: Total energy	-53338.164456

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.
-7.532	-2.899	0.4	-2.135	-2.897	0

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 : -0.012

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	-0.131	-0.040	2.571	-0.265	3.361	0.200	-1.843	-1.983	0.001
4	A	103	ASP	-1	-0.809	-0.898	3.906	-3.575	-3.365	0.002	-0.086	-0.126	0.000
5	A	104	THR	0	0.034	-0.013	6.119	0.444	0.444	0.000	0.000	0.000	0.000
6	A	105	ASN	0	-0.057	-0.029	7.528	0.228	0.228	0.000	0.000	0.000	0.000
7	A	106	TRP	0	0.010	0.009	6.897	0.229	0.229	0.000	0.000	0.000	0.000
8	A	107	ARG	1	0.831	0.912	5.086	-1.508	-1.508	0.000	0.000	0.000	0.000
9	A	108	TYR	0	0.066	0.018	2.790	-1.925	-1.196	0.199	-0.200	-0.727	-0.001
10	A	109	TYR	0	-0.069	-0.058	4.659	0.999	1.067	-0.001	-0.006	-0.061	0.000
11	A	110	GLY	0	0.031	0.025	7.989	-0.439	-0.439	0.000	0.000	0.000	0.000
12	A	111	ASP	-1	-0.878	-0.945	9.214	-0.052	-0.052	0.000	0.000	0.000	0.000
13	A	112	SER	0	-0.030	-0.017	9.238	-0.310	-0.310	0.000	0.000	0.000	0.000
14	A	114	TYR	0	0.042	0.004	7.700	-0.103	-0.103	0.000	0.000	0.000	0.000
15	A	115	GLY	0	0.035	0.030	9.195	0.169	0.169	0.000	0.000	0.000	0.000
16	A	116	PHE	0	-0.014	-0.015	10.559	-0.022	-0.022	0.000	0.000	0.000	0.000
17	A	117	PHE	0	0.074	0.031	13.026	0.001	0.001	0.000	0.000	0.000	0.000
18	A	118	ARG	1	0.881	0.935	17.227	-0.273	-0.273	0.000	0.000	0.000	0.000
19	A	119	HIS	0	0.036	0.033	19.748	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	120	ASN	0	-0.036	-0.029	22.728	0.027	0.027	0.000	0.000	0.000	0.000
21	A	121	LEU	0	0.023	0.015	23.480	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	122	THR	0	0.056	0.038	26.925	0.019	0.019	0.000	0.000	0.000	0.000
23	A	123	TRP	0	-0.004	-0.009	24.734	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	124	GLU	-1	-0.838	-0.933	25.856	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	125	GLU	-1	-0.878	-0.947	26.745	0.002	0.002	0.000	0.000	0.000	0.000
26	A	126	SER	0	-0.046	-0.030	22.388	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	127	LYS	1	0.907	0.952	21.855	0.005	0.005	0.000	0.000	0.000	0.000
28	A	128	GLN	0	-0.039	-0.024	22.463	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	129	TYR	0	0.028	0.004	17.759	-0.031	-0.031	0.000	0.000	0.000	0.000
30	A	130	CYS	0	-0.050	-0.017	14.456	-0.051	-0.051	0.000	0.000	0.000	0.000
31	A	131	THR	0	-0.003	0.012	18.427	-0.051	-0.051	0.000	0.000	0.000	0.000
32	A	132	ASP	-1	-0.877	-0.923	20.653	-0.193	-0.193	0.000	0.000	0.000	0.000
33	A	133	MET	0	-0.130	-0.055	15.418	-0.048	-0.048	0.000	0.000	0.000	0.000
34	A	134	ASN	0	-0.055	-0.022	15.613	-0.029	-0.029	0.000	0.000	0.000	0.000
35	A	135	ALA	0	-0.051	-0.024	14.682	-0.038	-0.038	0.000	0.000	0.000	0.000
36	A	136	THR	0	0.012	0.008	16.131	0.014	0.014	0.000	0.000	0.000	0.000
37	A	137	LEU	0	-0.002	0.002	16.797	0.037	0.037	0.000	0.000	0.000	0.000
38	A	138	LEU	0	-0.028	-0.015	14.008	0.002	0.002	0.000	0.000	0.000	0.000
39	A	139	LYS	1	0.902	0.962	16.955	-0.158	-0.158	0.000	0.000	0.000	0.000
40	A	140	ILE	0	-0.041	-0.029	17.066	0.061	0.061	0.000	0.000	0.000	0.000
41	A	141	ASP	-1	-0.855	-0.930	18.576	0.206	0.206	0.000	0.000	0.000	0.000
42	A	142	ASN	0	0.051	0.016	17.419	0.044	0.044	0.000	0.000	0.000	0.000
43	A	143	ARG	1	1.015	0.981	19.732	-0.436	-0.436	0.000	0.000	0.000	0.000
44	A	144	ASN	0	0.005	0.035	15.259	0.122	0.122	0.000	0.000	0.000	0.000
45	A	145	ILE	0	0.009	0.019	13.314	0.122	0.122	0.000	0.000	0.000	0.000
46	A	146	VAL	0	0.020	0.026	16.046	0.050	0.050	0.000	0.000	0.000	0.000
47	A	147	GLU	-1	-0.905	-0.967	17.851	0.655	0.655	0.000	0.000	0.000	0.000
48	A	148	TYR	0	-0.012	0.000	7.888	-0.024	-0.024	0.000	0.000	0.000	0.000
49	A	149	ILE	0	0.010	-0.004	13.157	0.097	0.097	0.000	0.000	0.000	0.000
50	A	150	LYS	1	0.932	0.970	15.268	-0.617	-0.617	0.000	0.000	0.000	0.000
51	A	151	ALA	0	-0.036	-0.001	14.572	-0.042	-0.042	0.000	0.000	0.000	0.000
52	A	152	ARG	1	0.896	0.948	8.093	-2.421	-2.421	0.000	0.000	0.000	0.000
53	A	153	THR	0	-0.015	0.005	13.959	-0.084	-0.084	0.000	0.000	0.000	0.000
54	A	154	HIS	0	0.049	0.041	17.154	0.026	0.026	0.000	0.000	0.000	0.000
55	A	155	LEU	0	-0.090	-0.040	20.446	-0.058	-0.058	0.000	0.000	0.000	0.000
56	A	156	ILE	0	0.027	0.015	21.458	0.022	0.022	0.000	0.000	0.000	0.000
57	A	157	ARG	1	0.800	0.888	17.888	-0.398	-0.398	0.000	0.000	0.000	0.000
58	A	158	TRP	0	-0.030	-0.027	21.747	0.023	0.023	0.000	0.000	0.000	0.000
59	A	159	VAL	0	-0.034	-0.014	19.216	0.028	0.028	0.000	0.000	0.000	0.000
60	A	160	GLY	0	0.037	0.010	20.744	-0.028	-0.028	0.000	0.000	0.000	0.000
61	A	161	LEU	0	-0.017	0.003	22.295	-0.015	-0.015	0.000	0.000	0.000	0.000
62	A	162	SER	0	-0.020	-0.023	25.329	0.000	0.000	0.000	0.000	0.000	0.000
63	A	163	ARG	1	0.878	0.957	28.713	-0.091	-0.091	0.000	0.000	0.000	0.000
64	A	164	GLN	0	0.004	-0.003	32.154	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	165	LYS	1	0.902	0.952	33.962	-0.037	-0.037	0.000	0.000	0.000	0.000
66	A	166	SER	0	0.046	0.003	36.703	0.006	0.006	0.000	0.000	0.000	0.000
67	A	167	ASN	0	-0.053	-0.033	38.131	0.001	0.001	0.000	0.000	0.000	0.000
68	A	168	GLU	-1	-0.915	-0.924	35.948	0.042	0.042	0.000	0.000	0.000	0.000
69	A	169	VAL	0	0.023	0.004	33.040	0.008	0.008	0.000	0.000	0.000	0.000
70	A	170	TRP	0	0.003	0.005	29.145	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	171	LYS	1	0.924	0.964	27.937	-0.033	-0.033	0.000	0.000	0.000	0.000
72	A	172	TRP	0	0.065	0.031	21.749	0.014	0.014	0.000	0.000	0.000	0.000
73	A	173	GLU	-1	-0.798	-0.905	21.626	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	174	ASP	-1	-0.823	-0.870	21.682	0.054	0.054	0.000	0.000	0.000	0.000
75	A	175	GLY	0	-0.021	-0.009	23.691	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	176	SER	0	-0.094	-0.067	24.316	0.009	0.009	0.000	0.000	0.000	0.000
77	A	177	VAL	0	0.001	-0.019	26.855	0.006	0.006	0.000	0.000	0.000	0.000
78	A	178	ILE	0	-0.040	-0.010	25.956	0.007	0.007	0.000	0.000	0.000	0.000
79	A	179	SER	0	0.001	-0.018	24.558	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	180	GLU	-1	-0.854	-0.937	27.441	0.147	0.147	0.000	0.000	0.000	0.000
81	A	181	ASN	0	-0.029	-0.030	26.000	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	182	MET	0	-0.078	-0.024	22.203	0.030	0.030	0.000	0.000	0.000	0.000
83	A	183	PHE	0	0.014	0.015	26.496	0.006	0.006	0.000	0.000	0.000	0.000
84	A	184	GLU	-1	-0.958	-0.956	28.348	0.285	0.285	0.000	0.000	0.000	0.000
85	A	185	PHE	0	-0.034	-0.029	24.404	0.024	0.024	0.000	0.000	0.000	0.000
86	A	186	LEU	0	-0.065	-0.028	26.795	0.009	0.009	0.000	0.000	0.000	0.000
87	A	187	GLU	-1	-0.899	-0.957	28.990	0.219	0.219	0.000	0.000	0.000	0.000
88	A	188	ASP	-1	-0.886	-0.936	31.468	0.138	0.138	0.000	0.000	0.000	0.000
89	A	189	GLY	0	-0.020	-0.033	33.997	0.004	0.004	0.000	0.000	0.000	0.000
90	A	190	LYS	1	0.904	0.936	35.711	-0.101	-0.101	0.000	0.000	0.000	0.000
91	A	191	GLY	0	0.061	0.024	37.046	0.002	0.002	0.000	0.000	0.000	0.000
92	A	192	ASN	0	-0.015	-0.017	38.142	0.002	0.002	0.000	0.000	0.000	0.000
93	A	193	MET	0	-0.061	0.036	33.823	0.000	0.000	0.000	0.000	0.000	0.000
94	A	194	ASN	0	0.053	0.004	33.036	0.010	0.010	0.000	0.000	0.000	0.000
95	A	195	CYS	0	0.088	0.055	28.157	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	196	ALA	0	0.050	0.027	26.136	0.004	0.004	0.000	0.000	0.000	0.000
97	A	197	TYR	0	-0.061	-0.019	24.174	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	198	PHE	0	0.035	0.018	19.306	0.009	0.009	0.000	0.000	0.000	0.000
99	A	199	HIS	0	-0.023	-0.045	22.659	0.020	0.020	0.000	0.000	0.000	0.000
100	A	200	ASN	0	-0.005	-0.008	22.081	0.030	0.030	0.000	0.000	0.000	0.000
101	A	201	GLY	0	-0.013	-0.027	21.861	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	202	LYS	1	0.934	1.003	22.804	-0.286	-0.286	0.000	0.000	0.000	0.000
103	A	203	MET	0	-0.002	-0.001	23.444	0.010	0.010	0.000	0.000	0.000	0.000
104	A	204	HIS	0	0.037	0.019	25.828	-0.022	-0.022	0.000	0.000	0.000	0.000
105	A	205	PRO	0	0.023	0.021	28.675	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	206	THR	0	-0.021	-0.031	29.568	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	207	PHE	0	-0.015	-0.014	32.268	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	209	GLU	-1	-0.854	-0.932	30.847	0.051	0.051	0.000	0.000	0.000	0.000
109	A	210	ASN	0	-0.048	-0.017	31.477	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	211	LYS	1	0.951	0.977	29.005	-0.057	-0.057	0.000	0.000	0.000	0.000
111	A	212	HIS	1	0.866	0.932	25.105	-0.142	-0.142	0.000	0.000	0.000	0.000
112	A	213	TYR	0	0.025	0.026	21.000	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	214	LEU	0	0.039	0.025	18.585	0.011	0.011	0.000	0.000	0.000	0.000
114	A	215	MET	0	-0.020	-0.009	15.090	0.084	0.084	0.000	0.000	0.000	0.000
115	A	217	GLU	-1	-0.807	-0.920	12.256	0.370	0.370	0.000	0.000	0.000	0.000
116	A	218	ARG	1	0.911	0.961	7.905	0.927	0.927	0.000	0.000	0.000	0.000
117	A	219	LYS	1	0.957	0.984	10.592	0.384	0.384	0.000	0.000	0.000	0.000
118	A	220	ALA	0	-0.011	-0.009	6.893	-0.196	-0.196	0.000	0.000	0.000	0.000
119	A	221	GLY	0	-0.006	0.005	7.810	0.229	0.229	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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