FMO DATABASE

FMODB ID: N3MRQ

Calculation Name: 3CXJ-A-Xray312

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CXJ

Chain ID: A

ChEMBL ID:

UniProt ID: O27461

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	146
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1399539.990074
FMO2-HF: Nuclear repulsion	1339650.63937
FMO2-HF: Total energy	-59889.350705
FMO2-MP2: Total energy	-60062.707512

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:2:ACE )

Summations of interaction energy for fragment #1(A:2: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.
0.587	2.187	1.204	-1.339	-1.464	-0.004

Interaction energy analysis for fragmet #1(A:2: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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	4	SER	0	0.021	0.006	3.852	0.553	1.609	-0.005	-0.497	-0.553	-0.001
4	A	5	GLN	0	0.082	0.041	2.430	-1.527	-0.983	1.209	-0.842	-0.911	-0.003
5	A	6	GLU	-1	-0.907	-0.939	4.810	-0.704	-0.704	0.000	0.000	0.000	0.000
6	A	7	MET	0	-0.043	-0.017	5.897	0.299	0.299	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.004	0.008	8.010	0.113	0.113	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.964	0.990	7.423	0.064	0.064	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.930	0.972	9.212	0.406	0.406	0.000	0.000	0.000	0.000
10	A	11	TRP	0	-0.033	-0.042	11.441	0.043	0.043	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.001	0.001	11.805	0.030	0.030	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.826	-0.928	13.637	-0.053	-0.053	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.943	-0.943	15.326	-0.219	-0.219	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.919	-0.965	17.616	-0.075	-0.075	0.000	0.000	0.000	0.000
15	A	16	GLY	0	-0.044	-0.013	18.956	0.014	0.014	0.000	0.000	0.000	0.000
16	A	17	PHE	0	-0.062	-0.037	17.447	0.015	0.015	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.038	-0.021	11.867	0.023	0.023	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.918	0.986	16.008	-0.033	-0.033	0.000	0.000	0.000	0.000
19	A	20	MET	0	-0.037	-0.024	15.273	-0.015	-0.015	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.923	-0.962	8.782	0.528	0.528	0.000	0.000	0.000	0.000
21	A	22	VAL	0	-0.048	-0.026	12.305	-0.041	-0.041	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.011	-0.006	12.776	0.060	0.060	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.794	-0.916	13.130	0.297	0.297	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.934	-0.962	13.744	0.352	0.352	0.000	0.000	0.000	0.000
25	A	26	ASN	0	-0.096	-0.032	15.565	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.009	-0.022	12.072	-0.025	-0.025	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.822	0.923	6.775	-0.799	-0.799	0.000	0.000	0.000	0.000
28	A	29	PHE	0	-0.006	-0.017	5.857	0.230	0.230	0.000	0.000	0.000	0.000
29	A	30	HIS	0	0.019	-0.011	8.565	-0.146	-0.146	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.087	-0.049	5.894	-0.113	-0.113	0.000	0.000	0.000	0.000
31	A	32	VAL	0	0.065	0.040	12.676	-0.015	-0.015	0.000	0.000	0.000	0.000
32	A	33	VAL	0	-0.021	-0.018	15.464	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	34	ASN	0	-0.030	-0.024	17.693	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.041	0.080	21.278	-0.018	-0.018	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.054	-0.027	23.287	0.007	0.007	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.862	-0.962	26.032	0.012	0.012	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.896	-0.946	25.240	0.025	0.025	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.131	-0.086	24.552	0.012	0.012	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.021	0.001	20.590	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	41	ILE	0	-0.087	-0.041	18.773	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.864	-0.933	16.826	0.148	0.148	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.064	-0.034	11.828	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	44	ILE	0	0.068	0.029	12.286	0.052	0.052	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.027	0.004	7.042	0.259	0.259	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.011	-0.012	10.994	0.070	0.070	0.000	0.000	0.000	0.000
46	A	47	ALA	0	0.048	0.029	11.605	0.065	0.065	0.000	0.000	0.000	0.000
47	A	48	GLY	0	-0.060	-0.022	11.636	0.069	0.069	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.922	0.967	12.385	-0.242	-0.242	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.889	-0.942	7.004	0.523	0.523	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.866	-0.930	7.935	0.204	0.204	0.000	0.000	0.000	0.000
51	A	52	MET	0	-0.015	-0.004	10.605	-0.069	-0.069	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.013	-0.014	10.139	0.095	0.095	0.000	0.000	0.000	0.000
53	A	54	LEU	0	-0.011	-0.010	12.662	-0.051	-0.051	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.024	-0.020	15.584	0.011	0.011	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.036	0.021	17.645	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	57	CYS	0	-0.010	0.015	20.154	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.041	0.029	22.956	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	59	THR	0	0.013	0.005	25.280	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.005	-0.010	28.751	0.000	0.000	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.043	-0.033	31.449	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.070	0.039	35.039	0.001	0.001	0.000	0.000	0.000	0.000
62	A	63	PRO	0	0.002	0.000	36.808	0.000	0.000	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.894	-0.972	39.893	0.025	0.025	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.047	0.028	37.792	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	66	GLN	0	-0.137	-0.070	36.613	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.025	0.020	41.338	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.042	0.007	44.562	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.010	-0.004	40.377	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.950	0.981	41.800	-0.037	-0.037	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.015	0.029	46.245	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.058	-0.015	45.858	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	73	SER	0	0.058	0.036	49.534	0.001	0.001	0.000	0.000	0.000	0.000
73	A	74	MET	0	0.061	0.024	45.804	0.001	0.001	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.916	-0.959	48.087	0.024	0.024	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.989	0.974	48.533	-0.019	-0.019	0.000	0.000	0.000	0.000
76	A	77	ARG	1	0.814	0.918	44.425	-0.030	-0.030	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.041	0.012	43.741	0.002	0.002	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.978	-0.977	43.695	0.022	0.022	0.000	0.000	0.000	0.000
79	A	80	PHE	0	-0.017	-0.021	39.142	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.014	-0.001	38.310	0.001	0.001	0.000	0.000	0.000	0.000
81	A	82	TRP	0	0.025	-0.003	39.069	0.002	0.002	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.941	0.972	40.162	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.017	0.024	34.994	0.000	0.000	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.930	0.983	35.540	-0.041	-0.041	0.000	0.000	0.000	0.000
85	A	86	PHE	0	-0.035	-0.028	35.575	0.001	0.001	0.000	0.000	0.000	0.000
86	A	87	THR	0	-0.041	-0.029	35.025	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	88	LEU	0	0.065	0.031	29.986	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	ASN	0	-0.012	0.015	31.362	0.004	0.004	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.871	0.928	33.108	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	91	PHE	0	-0.029	-0.021	29.039	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.044	-0.005	28.020	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.010	0.012	25.045	0.001	0.001	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.841	-0.902	24.500	0.074	0.074	0.000	0.000	0.000	0.000
94	A	95	PHE	0	-0.077	-0.065	26.052	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	GLN	0	-0.016	-0.002	27.376	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.045	-0.024	29.380	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.828	-0.905	32.162	0.065	0.065	0.000	0.000	0.000	0.000
98	A	99	HIS	0	-0.028	-0.044	34.004	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	100	PRO	0	0.039	0.026	37.360	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.927	-0.961	39.820	0.036	0.036	0.000	0.000	0.000	0.000
101	A	102	ASN	0	-0.046	-0.045	41.275	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	103	VAL	0	-0.024	-0.004	40.963	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.038	-0.012	34.711	0.002	0.002	0.000	0.000	0.000	0.000
104	A	105	ASN	0	0.018	0.017	34.886	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	106	SER	0	0.026	0.016	30.271	0.002	0.002	0.000	0.000	0.000	0.000
106	A	107	TYR	0	-0.048	-0.042	29.791	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.006	0.011	22.749	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	109	VAL	0	-0.017	-0.014	25.069	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.005	-0.028	20.302	0.011	0.011	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.843	-0.930	20.552	0.045	0.045	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.895	-0.939	17.302	0.118	0.118	0.000	0.000	0.000	0.000
112	A	113	ILE	0	-0.068	-0.014	15.263	-0.027	-0.027	0.000	0.000	0.000	0.000
113	A	114	PHE	0	0.025	-0.001	14.408	0.030	0.030	0.000	0.000	0.000	0.000
114	A	115	PHE	0	0.023	-0.023	7.386	-0.056	-0.056	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.927	-0.935	12.981	-0.035	-0.035	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.036	-0.027	16.014	-0.015	-0.015	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.051	-0.001	10.690	0.005	0.005	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.006	-0.007	14.919	-0.029	-0.029	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.878	0.934	15.698	0.162	0.162	0.000	0.000	0.000	0.000
120	A	121	ASP	-1	-0.897	-0.953	16.501	-0.039	-0.039	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.943	0.992	17.888	0.006	0.006	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.003	-0.003	12.988	0.017	0.017	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.015	-0.007	16.969	0.020	0.020	0.000	0.000	0.000	0.000
124	A	125	SER	0	-0.042	-0.023	19.405	0.011	0.011	0.000	0.000	0.000	0.000
125	A	126	SER	0	0.019	0.001	19.072	0.001	0.001	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.021	0.032	16.292	0.008	0.008	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.897	0.927	20.571	0.015	0.015	0.000	0.000	0.000	0.000
128	A	129	ASN	0	-0.064	-0.035	23.764	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.080	0.044	21.538	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	131	PHE	0	-0.009	-0.004	24.482	0.001	0.001	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.955	0.958	26.066	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	133	ALA	0	0.018	0.024	27.631	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.937	0.976	27.220	-0.043	-0.043	0.000	0.000	0.000	0.000
134	A	135	LEU	0	-0.043	-0.007	29.569	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	136	GLN	0	0.018	0.002	31.572	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	137	VAL	0	0.000	0.002	32.795	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	138	MET	0	0.005	0.012	32.510	0.001	0.001	0.000	0.000	0.000	0.000
138	A	139	TRP	0	0.016	-0.011	34.804	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	140	MET	0	-0.039	-0.001	36.870	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	141	ILE	0	-0.017	0.000	36.141	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	142	GLN	0	0.019	-0.003	36.877	0.001	0.001	0.000	0.000	0.000	0.000
142	A	143	GLU	-1	-0.978	-0.973	40.562	0.015	0.015	0.000	0.000	0.000	0.000
143	A	144	ARG	1	0.829	0.922	42.564	-0.023	-0.023	0.000	0.000	0.000	0.000
144	A	145	PHE	0	-0.055	-0.054	42.226	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	146	GLY	0	0.040	0.046	44.125	0.000	0.000	0.000	0.000	0.000	0.000
146	A	147	NME	0	-0.043	-0.017	40.070	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ACE )