FMO DATABASE

FMODB ID: GQKJ1

Calculation Name: 2CXH-A-Xray310

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CXH

Chain ID: A

ChEMBL ID:

UniProt ID: Q9YC08

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	182
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1900531.326771
FMO2-HF: Nuclear repulsion	1832452.49237
FMO2-HF: Total energy	-68078.834401
FMO2-MP2: Total energy	-68281.423094

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:12:ACE )

Summations of interaction energy for fragment #1(A:12:ACE )

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.
2.264	3.019	-0.006	-0.367	-0.382	0

Interaction energy analysis for fragmet #1(A:12:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.020 / q_NPA : 0.000

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].
3	A	14	TYR	0	0.007	0.019	3.844	0.836	1.591	-0.006	-0.367	-0.382
4	A	15	ARG	1	0.865	0.940	7.149	1.139	1.139	0.000	0.000	0.000
5	A	16	ILE	0	0.013	-0.001	9.570	0.064	0.064	0.000	0.000	0.000
6	A	17	LEU	0	0.005	0.017	12.205	0.025	0.025	0.000	0.000	0.000
7	A	18	VAL	0	0.014	0.009	13.710	0.057	0.057	0.000	0.000	0.000
8	A	19	THR	0	0.001	-0.023	17.414	0.013	0.013	0.000	0.000	0.000
9	A	20	THR	0	-0.034	-0.024	19.792	0.007	0.007	0.000	0.000	0.000
10	A	21	SER	0	0.054	0.032	22.634	0.002	0.002	0.000	0.000	0.000
11	A	22	ARG	1	0.932	0.956	23.802	0.023	0.023	0.000	0.000	0.000
12	A	23	ARG	1	0.937	0.978	26.614	0.037	0.037	0.000	0.000	0.000
13	A	24	PRO	0	0.002	0.025	26.369	0.003	0.003	0.000	0.000	0.000
14	A	25	SER	0	0.047	-0.022	28.999	0.001	0.001	0.000	0.000	0.000
15	A	26	PRO	0	-0.001	-0.023	30.514	-0.007	-0.007	0.000	0.000	0.000
16	A	27	ARG	1	0.815	0.898	30.919	0.054	0.054	0.000	0.000	0.000
17	A	28	ILE	0	0.022	0.030	26.140	-0.006	-0.006	0.000	0.000	0.000
18	A	29	ARG	1	0.966	0.993	26.178	0.064	0.064	0.000	0.000	0.000
19	A	30	SER	0	-0.089	-0.038	26.349	-0.010	-0.010	0.000	0.000	0.000
20	A	31	PHE	0	0.073	0.021	25.030	-0.007	-0.007	0.000	0.000	0.000
21	A	32	VAL	0	0.050	0.038	21.208	-0.008	-0.008	0.000	0.000	0.000
22	A	33	LYS	1	0.912	0.959	22.458	0.103	0.103	0.000	0.000	0.000
23	A	34	ASP	-1	-0.781	-0.883	23.881	-0.116	-0.116	0.000	0.000	0.000
24	A	35	LEU	0	0.024	0.006	21.180	-0.005	-0.005	0.000	0.000	0.000
25	A	36	SER	0	-0.029	-0.033	19.160	-0.017	-0.017	0.000	0.000	0.000
26	A	37	ALA	0	-0.040	0.001	19.517	-0.022	-0.022	0.000	0.000	0.000
27	A	38	THR	0	-0.021	-0.020	22.013	0.008	0.008	0.000	0.000	0.000
28	A	39	ILE	0	0.009	0.002	16.785	0.006	0.006	0.000	0.000	0.000
29	A	40	PRO	0	0.021	0.016	16.427	-0.026	-0.026	0.000	0.000	0.000
30	A	41	GLY	0	0.055	0.032	13.028	-0.018	-0.018	0.000	0.000	0.000
31	A	42	ALA	0	-0.024	0.008	12.853	-0.065	-0.065	0.000	0.000	0.000
32	A	43	PHE	0	-0.014	-0.007	11.281	0.027	0.027	0.000	0.000	0.000
33	A	44	ARG	1	0.940	0.979	16.546	0.175	0.175	0.000	0.000	0.000
34	A	45	PHE	0	0.033	0.013	16.003	-0.017	-0.017	0.000	0.000	0.000
35	A	46	THR	0	-0.018	-0.018	18.604	0.018	0.018	0.000	0.000	0.000
36	A	47	ARG	1	0.827	0.928	20.585	0.060	0.060	0.000	0.000	0.000
37	A	48	GLY	0	0.040	0.013	21.788	0.005	0.005	0.000	0.000	0.000
38	A	49	HIS	0	-0.028	-0.035	23.724	0.006	0.006	0.000	0.000	0.000
39	A	50	TYR	0	0.084	0.060	18.777	0.002	0.002	0.000	0.000	0.000
40	A	51	SER	0	-0.035	-0.019	19.894	0.000	0.000	0.000	0.000	0.000
41	A	52	MET	0	-0.004	-0.019	17.139	-0.013	-0.013	0.000	0.000	0.000
42	A	53	GLU	-1	-0.811	-0.892	15.978	0.061	0.061	0.000	0.000	0.000
43	A	54	GLU	-1	-0.847	-0.936	14.927	-0.016	-0.016	0.000	0.000	0.000
44	A	55	LEU	0	-0.035	-0.027	14.844	-0.020	-0.020	0.000	0.000	0.000
45	A	56	ALA	0	0.060	0.039	11.488	-0.055	-0.055	0.000	0.000	0.000
46	A	57	ARG	1	0.912	0.952	10.120	-0.096	-0.096	0.000	0.000	0.000
47	A	58	GLU	-1	-0.888	-0.940	10.637	-0.189	-0.189	0.000	0.000	0.000
48	A	59	ALA	0	-0.020	-0.013	9.382	-0.086	-0.086	0.000	0.000	0.000
49	A	60	ILE	0	0.031	0.027	5.314	-0.252	-0.252	0.000	0.000	0.000
50	A	61	ILE	0	-0.016	0.007	6.407	-0.292	-0.292	0.000	0.000	0.000
51	A	62	ARG	1	0.757	0.883	9.010	0.229	0.229	0.000	0.000	0.000
52	A	63	GLY	0	0.073	0.032	4.963	-0.060	-0.060	0.000	0.000	0.000
53	A	64	ALA	0	-0.091	-0.046	5.967	-0.248	-0.248	0.000	0.000	0.000
54	A	65	ASP	-1	-0.718	-0.839	5.599	-0.264	-0.264	0.000	0.000	0.000
55	A	66	ARG	1	0.847	0.931	7.315	0.288	0.288	0.000	0.000	0.000
56	A	67	ILE	0	0.002	0.010	11.097	-0.056	-0.056	0.000	0.000	0.000
57	A	68	VAL	0	0.004	0.004	13.877	0.037	0.037	0.000	0.000	0.000
58	A	69	VAL	0	-0.030	-0.015	17.323	-0.006	-0.006	0.000	0.000	0.000
59	A	70	VAL	0	-0.031	-0.020	20.330	0.011	0.011	0.000	0.000	0.000
60	A	71	GLY	0	-0.010	-0.015	23.684	0.003	0.003	0.000	0.000	0.000
61	A	72	GLU	-1	-0.777	-0.876	26.601	-0.053	-0.053	0.000	0.000	0.000
62	A	73	ARG	1	0.901	0.944	30.267	0.044	0.044	0.000	0.000	0.000
63	A	74	ARG	1	0.953	0.965	33.600	0.025	0.025	0.000	0.000	0.000
64	A	75	GLY	0	0.085	0.058	34.218	0.000	0.000	0.000	0.000	0.000
65	A	76	ASN	0	-0.033	-0.016	33.098	-0.007	-0.007	0.000	0.000	0.000
66	A	77	PRO	0	0.032	0.002	27.933	0.002	0.002	0.000	0.000	0.000
67	A	78	GLY	0	-0.044	-0.024	29.147	0.003	0.003	0.000	0.000	0.000
68	A	79	ILE	0	-0.051	-0.022	25.369	0.005	0.005	0.000	0.000	0.000
69	A	80	ILE	0	0.038	0.027	21.146	-0.006	-0.006	0.000	0.000	0.000
70	A	81	ARG	1	0.902	0.966	21.022	0.032	0.032	0.000	0.000	0.000
71	A	82	VAL	0	0.024	0.008	15.476	-0.016	-0.016	0.000	0.000	0.000
72	A	83	TYR	0	-0.031	-0.028	14.697	0.017	0.017	0.000	0.000	0.000
73	A	84	ALA	0	0.045	0.032	11.447	-0.056	-0.056	0.000	0.000	0.000
74	A	85	VAL	0	-0.068	-0.037	7.701	0.011	0.011	0.000	0.000	0.000
75	A	86	GLU	-1	-0.889	-0.941	7.522	0.376	0.376	0.000	0.000	0.000
76	A	87	GLY	0	0.039	0.016	8.119	0.196	0.196	0.000	0.000	0.000
77	A	88	PRO	0	-0.068	-0.053	9.446	-0.110	-0.110	0.000	0.000	0.000
78	A	89	GLU	-1	-0.907	-0.934	11.815	0.186	0.186	0.000	0.000	0.000
79	A	90	ARG	1	0.921	0.946	13.823	-0.082	-0.082	0.000	0.000	0.000
80	A	91	PRO	0	0.010	0.021	13.041	0.010	0.010	0.000	0.000	0.000
81	A	92	ASP	-1	-0.799	-0.890	14.685	0.099	0.099	0.000	0.000	0.000
82	A	93	ASN	0	-0.110	-0.077	16.012	-0.027	-0.027	0.000	0.000	0.000
83	A	94	ILE	0	0.075	0.029	14.087	0.006	0.006	0.000	0.000	0.000
84	A	95	VAL	0	0.049	0.023	18.159	-0.001	-0.001	0.000	0.000	0.000
85	A	96	SER	0	-0.088	-0.049	20.375	-0.005	-0.005	0.000	0.000	0.000
86	A	97	PHE	0	0.065	0.033	20.970	0.005	0.005	0.000	0.000	0.000
87	A	98	ILE	0	-0.033	-0.016	25.634	-0.002	-0.002	0.000	0.000	0.000
88	A	99	VAL	0	0.028	0.023	27.104	-0.002	-0.002	0.000	0.000	0.000
89	A	100	LYS	1	0.937	0.963	29.667	0.030	0.030	0.000	0.000	0.000
90	A	101	GLY	0	-0.045	-0.029	32.332	0.003	0.003	0.000	0.000	0.000
91	A	102	VAL	0	-0.019	0.005	28.894	-0.003	-0.003	0.000	0.000	0.000
92	A	103	SER	0	0.008	0.021	32.065	0.004	0.004	0.000	0.000	0.000
93	A	104	LEU	0	-0.018	-0.027	29.347	-0.006	-0.006	0.000	0.000	0.000
94	A	105	SER	0	0.007	0.000	29.646	0.007	0.007	0.000	0.000	0.000
95	A	106	ARG	1	0.913	0.932	28.653	0.097	0.097	0.000	0.000	0.000
96	A	107	GLU	-1	-0.799	-0.888	34.392	-0.059	-0.059	0.000	0.000	0.000
97	A	108	ARG	1	0.876	0.952	33.980	0.062	0.062	0.000	0.000	0.000
98	A	109	ARG	1	0.917	0.975	36.356	0.055	0.055	0.000	0.000	0.000
99	A	110	TRP	0	0.038	0.009	30.984	0.005	0.005	0.000	0.000	0.000
100	A	111	GLY	0	0.020	0.003	31.579	-0.001	-0.001	0.000	0.000	0.000
101	A	112	LEU	0	-0.017	-0.019	25.821	-0.001	-0.001	0.000	0.000	0.000
102	A	113	PRO	0	0.029	0.026	23.538	0.007	0.007	0.000	0.000	0.000
103	A	114	SER	0	-0.027	-0.018	24.766	-0.007	-0.007	0.000	0.000	0.000
104	A	115	LEU	0	-0.038	-0.017	19.486	0.005	0.005	0.000	0.000	0.000
105	A	116	ARG	1	0.859	0.913	20.772	0.174	0.174	0.000	0.000	0.000
106	A	117	GLY	0	-0.018	0.007	16.578	-0.018	-0.018	0.000	0.000	0.000
107	A	118	GLY	0	0.006	-0.003	14.450	0.017	0.017	0.000	0.000	0.000
108	A	119	GLU	-1	-0.779	-0.872	15.518	-0.237	-0.237	0.000	0.000	0.000
109	A	120	VAL	0	0.007	0.000	15.033	-0.037	-0.037	0.000	0.000	0.000
110	A	121	LEU	0	0.003	-0.005	16.841	0.024	0.024	0.000	0.000	0.000
111	A	122	VAL	0	0.021	0.020	18.595	0.003	0.003	0.000	0.000	0.000
112	A	123	ALA	0	-0.023	-0.003	21.353	0.002	0.002	0.000	0.000	0.000
113	A	124	ARG	1	0.942	0.968	23.160	0.073	0.073	0.000	0.000	0.000
114	A	125	PRO	0	-0.019	0.005	26.510	-0.001	-0.001	0.000	0.000	0.000
115	A	126	LEU	0	-0.002	-0.021	29.249	0.001	0.001	0.000	0.000	0.000
116	A	127	ASP	-1	-0.747	-0.816	32.750	-0.028	-0.028	0.000	0.000	0.000
117	A	128	SER	0	0.002	-0.018	32.613	-0.002	-0.002	0.000	0.000	0.000
118	A	129	GLY	0	0.018	0.019	34.078	0.003	0.003	0.000	0.000	0.000
119	A	130	VAL	0	0.016	0.000	30.672	0.000	0.000	0.000	0.000	0.000
120	A	131	ALA	0	0.010	-0.008	29.810	-0.002	-0.002	0.000	0.000	0.000
121	A	132	VAL	0	0.023	0.014	28.020	-0.006	-0.006	0.000	0.000	0.000
122	A	133	GLU	-1	-0.788	-0.883	26.483	-0.011	-0.011	0.000	0.000	0.000
123	A	134	PHE	0	-0.070	-0.054	25.122	-0.002	-0.002	0.000	0.000	0.000
124	A	135	ALA	0	-0.004	-0.002	23.756	-0.009	-0.009	0.000	0.000	0.000
125	A	136	ASP	-1	-0.852	-0.921	21.972	-0.030	-0.030	0.000	0.000	0.000
126	A	137	ALA	0	-0.043	-0.030	20.373	-0.001	-0.001	0.000	0.000	0.000
127	A	138	PHE	0	-0.038	-0.033	19.428	-0.011	-0.011	0.000	0.000	0.000
128	A	139	VAL	0	-0.024	0.014	16.857	-0.023	-0.023	0.000	0.000	0.000
129	A	140	ILE	0	0.008	0.016	15.579	-0.016	-0.016	0.000	0.000	0.000
130	A	141	ALA	0	-0.034	-0.032	14.681	-0.011	-0.011	0.000	0.000	0.000
131	A	142	PHE	0	-0.059	-0.062	14.896	-0.018	-0.018	0.000	0.000	0.000
132	A	143	HIS	0	-0.019	-0.012	9.266	0.008	0.008	0.000	0.000	0.000
133	A	144	ALA	0	-0.054	-0.012	13.812	-0.014	-0.014	0.000	0.000	0.000
134	A	145	ARG	1	0.984	0.980	15.038	0.188	0.188	0.000	0.000	0.000
135	A	146	LEU	0	0.062	0.025	18.725	-0.001	-0.001	0.000	0.000	0.000
136	A	147	LYS	1	0.933	0.972	21.387	0.044	0.044	0.000	0.000	0.000
137	A	148	PRO	0	-0.013	-0.015	21.276	-0.012	-0.012	0.000	0.000	0.000
138	A	149	PRO	0	-0.065	-0.035	19.320	0.006	0.006	0.000	0.000	0.000
139	A	150	GLU	-1	-0.855	-0.923	21.720	-0.064	-0.064	0.000	0.000	0.000
140	A	151	ALA	0	-0.033	-0.010	23.078	0.003	0.003	0.000	0.000	0.000
141	A	152	ALA	0	-0.038	-0.012	19.301	-0.005	-0.005	0.000	0.000	0.000
142	A	153	GLY	0	0.062	0.037	21.183	0.012	0.012	0.000	0.000	0.000
143	A	154	TYR	0	-0.003	-0.032	20.337	-0.019	-0.019	0.000	0.000	0.000
144	A	155	VAL	0	-0.034	0.006	21.021	0.015	0.015	0.000	0.000	0.000
145	A	156	GLU	-1	-0.886	-0.958	22.130	-0.085	-0.085	0.000	0.000	0.000
146	A	157	ALA	0	-0.014	-0.006	23.275	0.001	0.001	0.000	0.000	0.000
147	A	158	VAL	0	-0.025	-0.015	25.098	0.006	0.006	0.000	0.000	0.000
148	A	159	ILE	0	-0.019	-0.017	24.822	0.000	0.000	0.000	0.000	0.000
149	A	160	GLU	-1	-0.876	-0.939	29.380	-0.036	-0.036	0.000	0.000	0.000
150	A	161	SER	0	-0.063	-0.082	33.010	-0.001	-0.001	0.000	0.000	0.000
151	A	162	LEU	0	-0.073	-0.032	34.531	0.000	0.000	0.000	0.000	0.000
152	A	163	ASP	-1	-0.789	-0.895	36.327	-0.022	-0.022	0.000	0.000	0.000
153	A	164	ALA	0	0.030	0.007	35.967	-0.001	-0.001	0.000	0.000	0.000
154	A	165	ARG	1	0.865	0.933	32.427	0.011	0.011	0.000	0.000	0.000
155	A	166	THR	0	-0.041	-0.035	32.681	-0.003	-0.003	0.000	0.000	0.000
156	A	167	VAL	0	0.050	0.046	28.773	0.001	0.001	0.000	0.000	0.000
157	A	168	ALA	0	0.009	-0.002	31.897	-0.002	-0.002	0.000	0.000	0.000
158	A	169	VAL	0	-0.010	-0.006	25.809	-0.001	-0.001	0.000	0.000	0.000
159	A	170	THR	0	-0.013	-0.017	29.259	-0.001	-0.001	0.000	0.000	0.000
160	A	171	PHE	0	0.015	0.010	22.469	-0.001	-0.001	0.000	0.000	0.000
161	A	172	ARG	1	0.929	0.962	26.659	0.079	0.079	0.000	0.000	0.000
162	A	173	TYR	0	0.017	0.001	23.706	-0.010	-0.010	0.000	0.000	0.000
163	A	174	GLY	0	0.024	0.020	27.334	0.005	0.005	0.000	0.000	0.000
164	A	175	GLY	0	0.009	0.013	29.558	0.006	0.006	0.000	0.000	0.000
165	A	176	ALA	0	0.010	-0.004	31.054	0.006	0.006	0.000	0.000	0.000
166	A	177	PRO	0	-0.053	-0.011	30.521	-0.006	-0.006	0.000	0.000	0.000
167	A	178	VAL	0	0.011	0.000	26.524	-0.002	-0.002	0.000	0.000	0.000
168	A	179	GLY	0	0.041	0.016	26.903	-0.001	-0.001	0.000	0.000	0.000
169	A	180	PRO	0	-0.069	-0.015	26.045	0.010	0.010	0.000	0.000	0.000
170	A	181	MET	0	-0.001	0.006	28.430	-0.002	-0.002	0.000	0.000	0.000
171	A	182	LEU	0	-0.020	-0.024	25.361	0.003	0.003	0.000	0.000	0.000
172	A	183	ARG	1	1.007	1.029	30.040	0.041	0.041	0.000	0.000	0.000
173	A	184	LEU	0	-0.038	-0.029	25.736	0.000	0.000	0.000	0.000	0.000
174	A	185	GLY	0	0.036	0.019	29.848	0.003	0.003	0.000	0.000	0.000
175	A	186	LYS	1	0.848	0.914	28.853	0.008	0.008	0.000	0.000	0.000
176	A	187	PRO	0	-0.079	-0.038	26.468	0.002	0.002	0.000	0.000	0.000
177	A	188	ALA	0	-0.004	0.000	29.696	0.001	0.001	0.000	0.000	0.000
178	A	189	GLU	-1	-0.840	-0.931	25.745	0.027	0.027	0.000	0.000	0.000
179	A	190	MET	0	-0.098	-0.036	24.419	-0.002	-0.002	0.000	0.000	0.000
180	A	191	VAL	0	0.038	0.000	20.631	-0.007	-0.007	0.000	0.000	0.000
181	A	192	LYS	1	0.855	0.977	21.107	0.000	0.000	0.000	0.000	0.000
182	A	193	NME	0	0.016	0.015	18.471	0.007	0.007	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:ACE )