FMO DATABASE

FMODB ID: 1N26Z

Calculation Name: 2A4D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2A4D

Chain ID: A

ChEMBL ID:

UniProt ID: Q13404

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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1288771.373016
FMO2-HF: Nuclear repulsion	1232575.104538
FMO2-HF: Total energy	-56196.268478
FMO2-MP2: Total energy	-56356.978263

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:82:GLY)

Summations of interaction energy for fragment #1(A:82:GLY)

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.
1.932	2.989	-0.008	-0.461	-0.588	0.002

Interaction energy analysis for fragmet #1(A:82:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : -0.005

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	84	LYS	1	0.949	0.973	3.796	2.021	3.078	-0.008	-0.461	-0.588	0.002
4	A	85	VAL	0	0.058	0.021	5.844	-0.124	-0.124	0.000	0.000	0.000	0.000
5	A	86	PRO	0	0.021	0.014	9.132	-0.061	-0.061	0.000	0.000	0.000	0.000
6	A	87	ARG	1	0.803	0.906	7.564	1.261	1.261	0.000	0.000	0.000	0.000
7	A	88	ASN	0	0.025	-0.007	7.337	-0.155	-0.155	0.000	0.000	0.000	0.000
8	A	89	PHE	0	0.025	0.015	10.448	0.076	0.076	0.000	0.000	0.000	0.000
9	A	90	ARG	1	0.838	0.922	13.654	0.270	0.270	0.000	0.000	0.000	0.000
10	A	91	LEU	0	-0.031	-0.027	11.052	0.031	0.031	0.000	0.000	0.000	0.000
11	A	92	LEU	0	0.023	0.008	13.451	0.033	0.033	0.000	0.000	0.000	0.000
12	A	93	GLU	-1	-0.870	-0.928	15.939	-0.147	-0.147	0.000	0.000	0.000	0.000
13	A	94	GLU	-1	-0.758	-0.873	17.775	-0.282	-0.282	0.000	0.000	0.000	0.000
14	A	95	LEU	0	-0.020	0.008	16.532	0.020	0.020	0.000	0.000	0.000	0.000
15	A	96	GLU	-1	-0.927	-0.963	19.306	-0.118	-0.118	0.000	0.000	0.000	0.000
16	A	97	GLU	-1	-0.963	-0.991	21.897	-0.132	-0.132	0.000	0.000	0.000	0.000
17	A	98	GLY	0	-0.042	-0.020	22.657	0.014	0.014	0.000	0.000	0.000	0.000
18	A	99	GLN	0	-0.015	-0.001	21.436	0.020	0.020	0.000	0.000	0.000	0.000
19	A	100	LYS	1	0.899	0.964	25.448	0.109	0.109	0.000	0.000	0.000	0.000
20	A	101	GLY	0	-0.009	-0.001	28.427	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	102	VAL	0	0.077	0.027	27.286	0.001	0.001	0.000	0.000	0.000	0.000
22	A	103	GLY	0	-0.061	-0.033	29.951	0.002	0.002	0.000	0.000	0.000	0.000
23	A	104	ASP	-1	-0.862	-0.922	31.946	-0.084	-0.084	0.000	0.000	0.000	0.000
24	A	105	GLY	0	-0.004	0.002	32.846	0.005	0.005	0.000	0.000	0.000	0.000
25	A	106	THR	0	-0.104	-0.066	33.477	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	107	VAL	0	-0.025	-0.019	28.174	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	108	SER	0	-0.017	-0.006	27.182	0.006	0.006	0.000	0.000	0.000	0.000
28	A	109	TRP	0	-0.041	-0.052	20.687	0.010	0.010	0.000	0.000	0.000	0.000
29	A	110	GLY	0	0.057	0.033	21.037	0.012	0.012	0.000	0.000	0.000	0.000
30	A	111	LEU	0	0.027	0.014	14.893	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	112	GLU	-1	-0.982	-0.992	17.874	-0.236	-0.236	0.000	0.000	0.000	0.000
32	A	113	ASP	-1	-0.860	-0.937	16.481	-0.254	-0.254	0.000	0.000	0.000	0.000
33	A	114	ASP	-1	-0.910	-0.961	16.577	-0.263	-0.263	0.000	0.000	0.000	0.000
34	A	115	GLU	-1	-0.956	-0.971	15.991	-0.210	-0.210	0.000	0.000	0.000	0.000
35	A	116	ASP	-1	-0.816	-0.860	11.072	-0.761	-0.761	0.000	0.000	0.000	0.000
36	A	117	MET	0	-0.012	-0.019	9.908	-0.047	-0.047	0.000	0.000	0.000	0.000
37	A	118	THR	0	-0.155	-0.111	6.770	-0.183	-0.183	0.000	0.000	0.000	0.000
38	A	119	LEU	0	0.015	0.009	8.490	-0.133	-0.133	0.000	0.000	0.000	0.000
39	A	120	THR	0	-0.026	-0.010	9.344	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	121	ARG	1	0.927	0.972	11.919	0.454	0.454	0.000	0.000	0.000	0.000
41	A	122	TRP	0	-0.002	0.002	14.242	0.054	0.054	0.000	0.000	0.000	0.000
42	A	123	THR	0	0.001	-0.007	18.390	0.019	0.019	0.000	0.000	0.000	0.000
43	A	124	GLY	0	-0.019	-0.009	22.128	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	125	MET	0	0.009	-0.010	24.530	0.009	0.009	0.000	0.000	0.000	0.000
45	A	126	ILE	0	-0.014	-0.011	28.242	0.000	0.000	0.000	0.000	0.000	0.000
46	A	127	ILE	0	0.020	0.014	31.206	0.004	0.004	0.000	0.000	0.000	0.000
47	A	128	GLY	0	0.042	0.017	34.733	0.000	0.000	0.000	0.000	0.000	0.000
48	A	129	PRO	0	-0.045	-0.036	36.477	0.004	0.004	0.000	0.000	0.000	0.000
49	A	130	PRO	0	0.071	0.034	39.181	0.002	0.002	0.000	0.000	0.000	0.000
50	A	131	ARG	1	0.863	0.931	42.859	0.049	0.049	0.000	0.000	0.000	0.000
51	A	132	THR	0	-0.030	-0.023	40.796	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	133	ILE	0	-0.020	-0.010	40.933	0.001	0.001	0.000	0.000	0.000	0.000
53	A	134	TYR	0	-0.038	-0.043	37.398	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	135	GLU	-1	-0.899	-0.936	39.332	-0.061	-0.061	0.000	0.000	0.000	0.000
55	A	136	ASN	0	-0.045	-0.031	41.081	0.001	0.001	0.000	0.000	0.000	0.000
56	A	137	ARG	1	0.958	1.017	37.388	0.075	0.075	0.000	0.000	0.000	0.000
57	A	138	ILE	0	0.007	0.000	32.083	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	139	TYR	0	-0.025	-0.010	31.262	0.002	0.002	0.000	0.000	0.000	0.000
59	A	140	SER	0	0.064	0.030	27.302	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	141	LEU	0	-0.047	-0.031	24.826	0.005	0.005	0.000	0.000	0.000	0.000
61	A	142	LYS	1	0.958	0.988	20.553	0.213	0.213	0.000	0.000	0.000	0.000
62	A	143	ILE	0	-0.011	-0.011	18.341	0.013	0.013	0.000	0.000	0.000	0.000
63	A	144	GLU	-1	-0.928	-0.954	14.844	-0.418	-0.418	0.000	0.000	0.000	0.000
64	A	145	CYS	0	-0.004	0.006	13.326	0.047	0.047	0.000	0.000	0.000	0.000
65	A	146	GLY	0	0.095	0.042	10.907	-0.116	-0.116	0.000	0.000	0.000	0.000
66	A	147	PRO	0	0.002	-0.021	6.673	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	148	LYS	1	0.936	0.952	7.932	0.390	0.390	0.000	0.000	0.000	0.000
68	A	149	TYR	0	-0.057	-0.002	10.492	0.126	0.126	0.000	0.000	0.000	0.000
69	A	150	PRO	0	0.027	0.001	11.296	-0.101	-0.101	0.000	0.000	0.000	0.000
70	A	151	GLU	-1	-0.850	-0.937	13.188	-0.143	-0.143	0.000	0.000	0.000	0.000
71	A	152	ALA	0	-0.079	-0.031	14.113	0.041	0.041	0.000	0.000	0.000	0.000
72	A	153	PRO	0	-0.006	-0.002	15.860	-0.033	-0.033	0.000	0.000	0.000	0.000
73	A	154	PRO	0	0.012	0.010	16.705	-0.028	-0.028	0.000	0.000	0.000	0.000
74	A	155	PHE	0	-0.019	-0.003	17.388	0.049	0.049	0.000	0.000	0.000	0.000
75	A	156	VAL	0	0.036	0.012	19.210	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	157	ARG	1	0.889	0.936	22.232	0.199	0.199	0.000	0.000	0.000	0.000
77	A	158	PHE	0	0.065	0.018	24.677	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	159	VAL	0	-0.043	-0.022	25.400	0.000	0.000	0.000	0.000	0.000	0.000
79	A	160	THR	0	0.049	0.024	27.976	0.005	0.005	0.000	0.000	0.000	0.000
80	A	161	LYS	1	0.878	0.934	31.572	0.092	0.092	0.000	0.000	0.000	0.000
81	A	162	ILE	0	-0.006	-0.003	32.259	0.004	0.004	0.000	0.000	0.000	0.000
82	A	163	ASN	0	-0.050	-0.019	35.100	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	164	MET	0	0.018	0.012	32.638	0.001	0.001	0.000	0.000	0.000	0.000
84	A	165	ASN	0	0.037	0.017	34.820	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	166	GLY	0	0.036	0.008	32.221	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	167	VAL	0	-0.019	0.003	29.808	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	168	ASN	0	-0.003	0.009	30.161	0.008	0.008	0.000	0.000	0.000	0.000
88	A	169	SER	0	0.065	0.020	31.883	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	170	SER	0	-0.085	-0.043	32.796	0.002	0.002	0.000	0.000	0.000	0.000
90	A	171	ASN	0	0.020	0.001	28.151	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	172	GLY	0	0.086	0.053	27.962	-0.010	-0.010	0.000	0.000	0.000	0.000
92	A	173	VAL	0	-0.038	-0.015	24.613	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	174	VAL	0	-0.002	0.003	25.540	0.015	0.015	0.000	0.000	0.000	0.000
94	A	175	ASP	-1	-0.865	-0.939	25.627	-0.130	-0.130	0.000	0.000	0.000	0.000
95	A	176	PRO	0	0.049	0.011	23.342	0.006	0.006	0.000	0.000	0.000	0.000
96	A	177	ARG	1	0.895	0.930	25.769	0.111	0.111	0.000	0.000	0.000	0.000
97	A	178	ALA	0	-0.024	0.001	28.649	0.008	0.008	0.000	0.000	0.000	0.000
98	A	179	ILE	0	0.006	0.021	27.459	0.006	0.006	0.000	0.000	0.000	0.000
99	A	180	SER	0	0.024	0.013	27.897	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	181	VAL	0	0.032	0.011	25.642	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	182	LEU	0	-0.001	0.000	22.131	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	183	ALA	0	-0.019	-0.005	23.625	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	184	LYS	1	0.864	0.924	25.504	0.093	0.093	0.000	0.000	0.000	0.000
104	A	185	TRP	0	0.008	-0.005	17.863	0.010	0.010	0.000	0.000	0.000	0.000
105	A	186	GLN	0	-0.021	-0.005	22.201	0.019	0.019	0.000	0.000	0.000	0.000
106	A	187	ASN	0	0.003	0.007	17.409	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	188	SER	0	0.004	0.010	19.019	-0.018	-0.018	0.000	0.000	0.000	0.000
108	A	189	TYR	0	-0.055	-0.021	21.429	0.010	0.010	0.000	0.000	0.000	0.000
109	A	190	SER	0	0.054	0.022	19.953	-0.016	-0.016	0.000	0.000	0.000	0.000
110	A	191	ILE	0	0.063	0.029	17.532	0.020	0.020	0.000	0.000	0.000	0.000
111	A	192	LYS	1	0.903	0.972	21.476	0.157	0.157	0.000	0.000	0.000	0.000
112	A	193	VAL	0	-0.007	-0.001	24.407	0.012	0.012	0.000	0.000	0.000	0.000
113	A	194	VAL	0	0.001	0.006	22.276	0.013	0.013	0.000	0.000	0.000	0.000
114	A	195	LEU	0	-0.007	0.007	24.465	0.012	0.012	0.000	0.000	0.000	0.000
115	A	196	GLN	0	0.009	-0.009	27.258	0.010	0.010	0.000	0.000	0.000	0.000
116	A	197	GLU	-1	-0.827	-0.908	28.818	-0.089	-0.089	0.000	0.000	0.000	0.000
117	A	198	LEU	0	-0.008	-0.010	26.846	0.009	0.009	0.000	0.000	0.000	0.000
118	A	199	ARG	1	0.939	0.967	30.802	0.097	0.097	0.000	0.000	0.000	0.000
119	A	200	ARG	1	0.849	0.920	33.248	0.092	0.092	0.000	0.000	0.000	0.000
120	A	201	LEU	0	-0.006	-0.008	31.788	0.007	0.007	0.000	0.000	0.000	0.000
121	A	202	MET	0	-0.038	0.012	32.063	0.006	0.006	0.000	0.000	0.000	0.000
122	A	203	MET	0	0.012	0.003	36.769	0.006	0.006	0.000	0.000	0.000	0.000
123	A	204	SER	0	-0.075	-0.015	38.571	0.006	0.006	0.000	0.000	0.000	0.000
124	A	205	LYS	1	0.969	0.948	40.498	0.050	0.050	0.000	0.000	0.000	0.000
125	A	206	GLU	-1	-0.974	-0.979	39.022	-0.068	-0.068	0.000	0.000	0.000	0.000
126	A	207	ASN	0	0.074	0.026	36.577	0.000	0.000	0.000	0.000	0.000	0.000
127	A	208	MET	0	-0.027	0.004	40.225	0.001	0.001	0.000	0.000	0.000	0.000
128	A	209	LYS	1	0.932	0.953	42.201	0.052	0.052	0.000	0.000	0.000	0.000
129	A	210	LEU	0	0.004	0.031	39.231	0.003	0.003	0.000	0.000	0.000	0.000
130	A	211	PRO	0	0.067	0.030	42.502	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	212	GLN	0	-0.009	-0.017	38.270	-0.007	-0.007	0.000	0.000	0.000	0.000
132	A	213	PRO	0	-0.012	0.011	37.231	0.004	0.004	0.000	0.000	0.000	0.000
133	A	214	PRO	0	0.034	-0.002	40.370	0.000	0.000	0.000	0.000	0.000	0.000
134	A	215	GLU	-1	-0.900	-0.956	38.435	-0.079	-0.079	0.000	0.000	0.000	0.000
135	A	216	GLY	0	0.013	0.006	36.380	0.002	0.002	0.000	0.000	0.000	0.000
136	A	217	GLN	0	-0.042	-0.004	35.888	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	218	CYS	0	0.008	0.005	30.373	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	219	TYR	0	-0.064	-0.005	28.580	0.006	0.006	0.000	0.000	0.000	0.000
139	A	220	SER	0	-0.007	0.001	25.069	-0.010	-0.010	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:82:GLY)