FMO DATABASE

FMODB ID: QV66Y

Calculation Name: 4AY0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4AY0

Chain ID: A

ChEMBL ID:

UniProt ID: P26926

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptAll
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	190
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1985314.062666
FMO2-HF: Nuclear repulsion	1911675.113514
FMO2-HF: Total energy	-73638.949153
FMO2-MP2: Total energy	-73856.632183

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:13:GLY)

Summations of interaction energy for fragment #1(A:13: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.
0.72	1.761	-0.01	-0.463	-0.568	0

Interaction energy analysis for fragmet #1(A:13:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.013

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	15	THR	0	-0.011	0.008	3.871	1.468	2.509	-0.010	-0.463	-0.568
4	A	16	ILE	0	-0.004	-0.009	5.963	-0.308	-0.308	0.000	0.000	0.000
5	A	17	GLY	0	0.021	0.021	9.593	0.095	0.095	0.000	0.000	0.000
6	A	18	GLU	-1	-0.811	-0.878	10.723	-0.243	-0.243	0.000	0.000	0.000
7	A	19	SER	0	0.020	0.004	12.085	0.021	0.021	0.000	0.000	0.000
8	A	20	ARG	1	0.740	0.852	13.997	-0.002	-0.002	0.000	0.000	0.000
9	A	21	ILE	0	0.003	0.007	17.262	0.030	0.030	0.000	0.000	0.000
10	A	22	ILE	0	0.015	0.012	19.985	-0.016	-0.016	0.000	0.000	0.000
11	A	23	TYR	0	-0.014	-0.023	23.523	0.012	0.012	0.000	0.000	0.000
12	A	24	PRO	0	0.023	0.005	26.152	-0.007	-0.007	0.000	0.000	0.000
13	A	25	LEU	0	0.002	0.013	29.681	0.002	0.002	0.000	0.000	0.000
14	A	26	ASP	-1	-0.758	-0.839	31.891	0.009	0.009	0.000	0.000	0.000
15	A	27	ALA	0	-0.015	0.014	29.750	0.003	0.003	0.000	0.000	0.000
16	A	28	ALA	0	0.050	0.031	31.426	-0.003	-0.003	0.000	0.000	0.000
17	A	29	GLY	0	-0.023	-0.016	28.042	0.000	0.000	0.000	0.000	0.000
18	A	30	VAL	0	-0.033	-0.002	22.961	0.003	0.003	0.000	0.000	0.000
19	A	31	MET	0	-0.010	-0.001	22.335	-0.008	-0.008	0.000	0.000	0.000
20	A	32	VAL	0	0.011	0.013	15.871	0.004	0.004	0.000	0.000	0.000
21	A	33	SER	0	0.014	0.011	14.728	-0.003	-0.003	0.000	0.000	0.000
22	A	34	VAL	0	-0.014	-0.015	13.033	0.007	0.007	0.000	0.000	0.000
23	A	35	LYS	1	0.884	0.911	10.067	-0.665	-0.665	0.000	0.000	0.000
24	A	36	ASN	0	-0.003	0.005	10.011	0.041	0.041	0.000	0.000	0.000
25	A	37	THR	0	0.010	-0.003	4.946	-0.077	-0.077	0.000	0.000	0.000
26	A	38	GLN	0	-0.001	0.024	5.779	0.058	0.058	0.000	0.000	0.000
27	A	39	ASP	-1	-0.820	-0.913	9.021	0.605	0.605	0.000	0.000	0.000
28	A	40	TYR	0	-0.005	-0.011	9.686	-0.045	-0.045	0.000	0.000	0.000
29	A	41	PRO	0	-0.026	-0.010	13.329	0.025	0.025	0.000	0.000	0.000
30	A	42	VAL	0	-0.021	-0.014	12.280	-0.032	-0.032	0.000	0.000	0.000
31	A	43	LEU	0	0.019	0.002	15.427	0.021	0.021	0.000	0.000	0.000
32	A	44	ILE	0	-0.017	-0.005	13.314	-0.019	-0.019	0.000	0.000	0.000
33	A	45	GLN	0	0.028	0.011	16.790	0.007	0.007	0.000	0.000	0.000
34	A	46	SER	0	-0.001	-0.004	17.390	-0.021	-0.021	0.000	0.000	0.000
35	A	47	ARG	1	0.855	0.926	19.021	0.030	0.030	0.000	0.000	0.000
36	A	48	ILE	0	0.020	0.014	19.978	-0.005	-0.005	0.000	0.000	0.000
37	A	49	TYR	0	0.019	0.016	19.740	-0.002	-0.002	0.000	0.000	0.000
38	A	50	ASP	-1	-0.696	-0.842	23.132	-0.090	-0.090	0.000	0.000	0.000
39	A	51	GLU	-1	-0.829	-0.881	22.852	-0.096	-0.096	0.000	0.000	0.000
40	A	52	ASN	0	-0.047	-0.031	22.167	-0.023	-0.023	0.000	0.000	0.000
41	A	53	LYS	1	0.824	0.912	16.289	0.175	0.175	0.000	0.000	0.000
42	A	54	GLU	-1	-0.904	-0.941	21.663	-0.103	-0.103	0.000	0.000	0.000
43	A	55	LYS	1	0.748	0.843	24.826	0.051	0.051	0.000	0.000	0.000
44	A	56	GLU	-1	-0.774	-0.879	26.361	-0.045	-0.045	0.000	0.000	0.000
45	A	57	SER	0	-0.018	-0.017	29.171	0.002	0.002	0.000	0.000	0.000
46	A	58	GLU	-1	-0.866	-0.922	31.991	-0.014	-0.014	0.000	0.000	0.000
47	A	59	ASP	-1	-0.870	-0.917	26.983	-0.038	-0.038	0.000	0.000	0.000
48	A	60	PRO	0	-0.029	-0.002	27.878	0.006	0.006	0.000	0.000	0.000
49	A	61	PHE	0	0.003	-0.020	25.755	0.005	0.005	0.000	0.000	0.000
50	A	62	VAL	0	0.046	0.038	26.535	-0.004	-0.004	0.000	0.000	0.000
51	A	63	VAL	0	-0.020	-0.024	20.783	0.005	0.005	0.000	0.000	0.000
52	A	64	THR	0	-0.043	-0.002	24.113	-0.004	-0.004	0.000	0.000	0.000
53	A	65	PRO	0	0.030	0.008	21.357	0.008	0.008	0.000	0.000	0.000
54	A	66	PRO	0	0.048	0.021	21.770	0.002	0.002	0.000	0.000	0.000
55	A	67	LEU	0	0.013	-0.014	20.725	-0.012	-0.012	0.000	0.000	0.000
56	A	68	PHE	0	-0.010	-0.002	17.329	0.007	0.007	0.000	0.000	0.000
57	A	69	ARG	1	0.847	0.889	18.985	-0.127	-0.127	0.000	0.000	0.000
58	A	70	LEU	0	-0.046	-0.002	13.465	0.010	0.010	0.000	0.000	0.000
59	A	71	ASP	-1	-0.736	-0.853	15.351	0.161	0.161	0.000	0.000	0.000
60	A	72	DAL	0	0.007	0.013	13.191	0.042	0.042	0.000	0.000	0.000
61	A	73	LYS	1	0.815	0.911	8.658	-0.793	-0.793	0.000	0.000	0.000
62	A	74	GLN	0	0.040	0.045	12.395	0.034	0.034	0.000	0.000	0.000
63	A	75	GLN	0	0.017	-0.009	13.610	0.098	0.098	0.000	0.000	0.000
64	A	76	ASN	0	0.034	0.018	15.591	-0.036	-0.036	0.000	0.000	0.000
65	A	77	SER	0	-0.045	-0.024	17.342	0.022	0.022	0.000	0.000	0.000
66	A	78	LEU	0	-0.005	0.011	16.888	-0.014	-0.014	0.000	0.000	0.000
67	A	79	ARG	1	0.936	0.959	20.407	-0.048	-0.048	0.000	0.000	0.000
68	A	80	ILE	0	0.000	-0.004	20.006	-0.008	-0.008	0.000	0.000	0.000
69	A	81	ALA	0	0.009	-0.010	24.237	0.006	0.006	0.000	0.000	0.000
70	A	82	GLN	0	-0.053	-0.037	28.006	-0.008	-0.008	0.000	0.000	0.000
71	A	83	ALA	0	-0.034	-0.028	30.169	0.004	0.004	0.000	0.000	0.000
72	A	84	GLY	0	0.044	0.026	32.353	-0.001	-0.001	0.000	0.000	0.000
73	A	85	GLY	0	-0.023	-0.008	32.115	-0.002	-0.002	0.000	0.000	0.000
74	A	86	VAL	0	-0.011	0.005	33.142	0.003	0.003	0.000	0.000	0.000
75	A	87	PHE	0	-0.002	-0.004	29.806	-0.005	-0.005	0.000	0.000	0.000
76	A	88	PRO	0	0.001	0.018	32.694	0.003	0.003	0.000	0.000	0.000
77	A	89	ARG	1	0.840	0.847	34.325	-0.001	-0.001	0.000	0.000	0.000
78	A	90	ASP	-1	-0.821	-0.896	36.560	-0.024	-0.024	0.000	0.000	0.000
79	A	91	LYS	1	0.841	0.911	32.674	0.041	0.041	0.000	0.000	0.000
80	A	92	GLU	-1	-0.724	-0.854	26.761	-0.024	-0.024	0.000	0.000	0.000
81	A	93	SER	0	-0.065	-0.036	28.350	-0.004	-0.004	0.000	0.000	0.000
82	A	94	LEU	0	-0.053	-0.009	20.800	0.006	0.006	0.000	0.000	0.000
83	A	95	LYS	1	0.838	0.915	23.131	0.047	0.047	0.000	0.000	0.000
84	A	96	TRP	0	-0.021	-0.029	14.929	-0.020	-0.020	0.000	0.000	0.000
85	A	97	LEU	0	0.023	0.029	16.638	0.007	0.007	0.000	0.000	0.000
86	A	98	CYS	0	-0.113	-0.065	10.933	0.036	0.036	0.000	0.000	0.000
87	A	99	VAL	0	0.024	-0.001	13.362	0.028	0.028	0.000	0.000	0.000
88	A	100	LYS	1	0.967	0.988	12.952	0.093	0.093	0.000	0.000	0.000
89	A	101	GLY	0	0.031	0.023	12.485	0.042	0.042	0.000	0.000	0.000
90	A	102	ILE	0	-0.043	-0.030	13.539	-0.052	-0.052	0.000	0.000	0.000
91	A	103	PRO	0	0.061	0.031	14.553	0.028	0.028	0.000	0.000	0.000
92	A	104	PRO	0	-0.011	0.015	16.761	-0.012	-0.012	0.000	0.000	0.000
93	A	119	ASN	0	0.022	0.010	9.136	-0.118	-0.118	0.000	0.000	0.000
94	A	121	ILE	0	-0.007	0.003	12.666	-0.024	-0.024	0.000	0.000	0.000
95	A	122	LYS	1	0.810	0.898	14.835	0.168	0.168	0.000	0.000	0.000
96	A	123	LEU	0	0.005	0.002	18.085	0.023	0.023	0.000	0.000	0.000
97	A	124	LEU	0	0.009	-0.001	21.151	-0.010	-0.010	0.000	0.000	0.000
98	A	125	VAL	0	0.012	0.017	23.871	0.012	0.012	0.000	0.000	0.000
99	A	126	ARG	1	0.757	0.822	25.054	-0.006	-0.006	0.000	0.000	0.000
100	A	127	PRO	0	0.023	0.023	29.330	0.006	0.006	0.000	0.000	0.000
101	A	128	ASN	0	-0.016	-0.015	33.111	0.003	0.003	0.000	0.000	0.000
102	A	129	GLU	-1	-0.780	-0.886	34.696	0.002	0.002	0.000	0.000	0.000
103	A	130	LEU	0	-0.044	0.001	31.060	-0.001	-0.001	0.000	0.000	0.000
104	A	131	LYS	1	0.821	0.894	34.812	-0.001	-0.001	0.000	0.000	0.000
105	A	132	GLY	0	0.014	0.014	32.902	-0.004	-0.004	0.000	0.000	0.000
106	A	133	THR	0	0.005	-0.005	27.311	0.002	0.002	0.000	0.000	0.000
107	A	134	PRO	0	0.030	0.007	24.795	-0.003	-0.003	0.000	0.000	0.000
108	A	135	ILE	0	0.073	0.016	25.111	-0.006	-0.006	0.000	0.000	0.000
109	A	136	GLN	0	-0.038	0.000	27.574	0.001	0.001	0.000	0.000	0.000
110	A	137	PHE	0	-0.013	-0.018	30.154	-0.001	-0.001	0.000	0.000	0.000
111	A	138	ALA	0	0.033	0.026	27.267	-0.005	-0.005	0.000	0.000	0.000
112	A	139	GLU	-1	-0.774	-0.855	29.104	-0.041	-0.041	0.000	0.000	0.000
113	A	140	ASN	0	-0.011	-0.020	32.069	-0.001	-0.001	0.000	0.000	0.000
114	A	141	LEU	0	-0.056	-0.002	27.667	0.000	0.000	0.000	0.000	0.000
115	A	142	SER	0	-0.052	-0.026	32.343	0.000	0.000	0.000	0.000	0.000
116	A	143	TRP	0	0.067	0.005	27.446	-0.008	-0.008	0.000	0.000	0.000
117	A	144	LYS	1	0.902	0.971	34.772	0.059	0.059	0.000	0.000	0.000
118	A	145	VAL	0	-0.002	-0.007	34.472	-0.007	-0.007	0.000	0.000	0.000
119	A	146	ASP	-1	-0.852	-0.915	36.170	-0.060	-0.060	0.000	0.000	0.000
120	A	147	GLY	0	-0.006	-0.009	36.340	-0.005	-0.005	0.000	0.000	0.000
121	A	148	GLY	0	-0.021	-0.005	35.382	-0.003	-0.003	0.000	0.000	0.000
122	A	149	LYS	1	0.822	0.902	29.342	0.114	0.114	0.000	0.000	0.000
123	A	150	LEU	0	0.002	0.013	28.697	0.007	0.007	0.000	0.000	0.000
124	A	151	ILE	0	-0.024	-0.016	30.793	-0.007	-0.007	0.000	0.000	0.000
125	A	152	ALA	0	0.026	0.022	29.460	0.005	0.005	0.000	0.000	0.000
126	A	153	GLU	-1	-0.830	-0.919	31.436	-0.049	-0.049	0.000	0.000	0.000
127	A	154	ASN	0	-0.006	0.002	29.330	0.006	0.006	0.000	0.000	0.000
128	A	155	PRO	0	0.045	0.028	32.598	0.001	0.001	0.000	0.000	0.000
129	A	156	SER	0	-0.031	-0.021	31.285	0.005	0.005	0.000	0.000	0.000
130	A	157	PRO	0	0.013	-0.008	32.991	-0.004	-0.004	0.000	0.000	0.000
131	A	158	PHE	0	0.041	0.014	27.872	0.002	0.002	0.000	0.000	0.000
132	A	159	TYR	0	-0.016	-0.030	24.515	-0.003	-0.003	0.000	0.000	0.000
133	A	160	MET	0	-0.022	0.019	24.950	0.001	0.001	0.000	0.000	0.000
134	A	161	ASN	0	0.032	-0.003	20.131	-0.029	-0.029	0.000	0.000	0.000
135	A	162	ILE	0	-0.012	0.005	21.125	0.002	0.002	0.000	0.000	0.000
136	A	163	GLY	0	-0.014	-0.014	18.181	-0.018	-0.018	0.000	0.000	0.000
137	A	164	GLU	-1	-0.863	-0.919	18.178	-0.165	-0.165	0.000	0.000	0.000
138	A	165	LEU	0	0.005	0.001	20.869	0.023	0.023	0.000	0.000	0.000
139	A	166	THR	0	-0.030	-0.008	23.579	-0.014	-0.014	0.000	0.000	0.000
140	A	167	PHE	0	0.045	0.007	26.238	0.012	0.012	0.000	0.000	0.000
141	A	168	GLY	0	0.024	0.007	29.583	-0.006	-0.006	0.000	0.000	0.000
142	A	169	GLY	0	-0.055	-0.021	28.980	0.001	0.001	0.000	0.000	0.000
143	A	170	LYS	1	0.918	0.973	26.329	0.117	0.117	0.000	0.000	0.000
144	A	171	SER	0	0.045	0.014	21.357	0.006	0.006	0.000	0.000	0.000
145	A	172	ILE	0	-0.048	-0.019	23.355	-0.002	-0.002	0.000	0.000	0.000
146	A	173	PRO	0	0.007	-0.001	19.905	-0.006	-0.006	0.000	0.000	0.000
147	A	174	SER	0	0.034	0.025	17.314	0.016	0.016	0.000	0.000	0.000
148	A	175	HIS	1	0.881	0.934	19.851	0.133	0.133	0.000	0.000	0.000
149	A	176	TYR	0	-0.055	-0.052	21.044	0.004	0.004	0.000	0.000	0.000
150	A	177	ILE	0	0.003	0.011	23.297	-0.002	-0.002	0.000	0.000	0.000
151	A	178	PRO	0	0.024	0.017	27.113	0.007	0.007	0.000	0.000	0.000
152	A	179	PRO	0	0.009	0.017	28.398	0.001	0.001	0.000	0.000	0.000
153	A	180	LYS	1	0.774	0.868	31.122	0.025	0.025	0.000	0.000	0.000
154	A	181	SER	0	-0.001	0.014	31.908	0.000	0.000	0.000	0.000	0.000
155	A	182	THR	0	-0.001	-0.003	32.176	-0.001	-0.001	0.000	0.000	0.000
156	A	183	TRP	0	0.028	-0.003	25.562	0.000	0.000	0.000	0.000	0.000
157	A	184	ALA	0	0.014	0.016	29.568	0.002	0.002	0.000	0.000	0.000
158	A	185	PHE	0	-0.028	-0.011	23.551	-0.006	-0.006	0.000	0.000	0.000
159	A	186	ASP	-1	-0.810	-0.906	26.804	-0.131	-0.131	0.000	0.000	0.000
160	A	187	LEU	0	0.009	0.006	27.443	-0.009	-0.009	0.000	0.000	0.000
161	A	188	PRO	0	-0.011	-0.003	26.031	0.004	0.004	0.000	0.000	0.000
162	A	189	LYS	1	1.016	0.992	28.820	0.122	0.122	0.000	0.000	0.000
163	A	190	GLY	0	0.005	-0.009	32.055	-0.003	-0.003	0.000	0.000	0.000
164	A	191	LEU	0	-0.017	-0.004	29.219	0.005	0.005	0.000	0.000	0.000
165	A	192	ALA	0	0.002	0.005	33.890	0.002	0.002	0.000	0.000	0.000
166	A	193	GLY	0	0.034	0.029	37.412	0.004	0.004	0.000	0.000	0.000
167	A	194	ALA	0	-0.053	-0.007	33.950	0.003	0.003	0.000	0.000	0.000
168	A	195	ARG	1	0.920	0.932	36.013	0.057	0.057	0.000	0.000	0.000
169	A	196	ASN	0	0.047	0.033	32.613	0.001	0.001	0.000	0.000	0.000
170	A	197	VAL	0	0.021	0.010	29.379	-0.008	-0.008	0.000	0.000	0.000
171	A	198	SER	0	0.015	0.010	28.122	0.012	0.012	0.000	0.000	0.000
172	A	199	TRP	0	-0.028	-0.014	25.119	-0.015	-0.015	0.000	0.000	0.000
173	A	200	ARG	1	0.876	0.935	21.076	0.107	0.107	0.000	0.000	0.000
174	A	201	ILE	0	-0.009	-0.009	22.315	-0.015	-0.015	0.000	0.000	0.000
175	A	202	ILE	0	-0.018	0.002	15.791	0.001	0.001	0.000	0.000	0.000
176	A	203	ASN	0	0.062	0.029	19.764	0.010	0.010	0.000	0.000	0.000
177	A	204	ASP	-1	-0.721	-0.855	20.002	0.001	0.001	0.000	0.000	0.000
178	A	205	GLN	0	-0.022	-0.015	19.634	0.000	0.000	0.000	0.000	0.000
179	A	206	GLY	0	0.026	0.025	15.854	0.030	0.030	0.000	0.000	0.000
180	A	207	GLY	0	0.003	-0.002	15.296	-0.010	-0.010	0.000	0.000	0.000
181	A	208	LEU	0	-0.042	-0.026	16.972	-0.011	-0.011	0.000	0.000	0.000
182	A	209	ASP	-1	-0.776	-0.864	19.355	-0.013	-0.013	0.000	0.000	0.000
183	A	210	ARG	1	0.759	0.838	23.168	0.025	0.025	0.000	0.000	0.000
184	A	211	LEU	0	-0.030	-0.004	25.551	-0.007	-0.007	0.000	0.000	0.000
185	A	212	TYR	0	-0.049	-0.037	26.634	0.012	0.012	0.000	0.000	0.000
186	A	213	SER	0	0.025	-0.014	29.343	-0.008	-0.008	0.000	0.000	0.000
187	A	214	LYS	1	0.806	0.905	32.095	0.055	0.055	0.000	0.000	0.000
188	A	215	ASN	0	-0.007	-0.010	34.523	-0.008	-0.008	0.000	0.000	0.000
189	A	216	VAL	0	-0.004	0.014	34.565	0.003	0.003	0.000	0.000	0.000
190	A	217	THR	0	-0.019	-0.011	37.102	0.005	0.005	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:13:GLY)