FMO DATABASE

FMODB ID: ZV88N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1983507.657177
FMO2-HF: Nuclear repulsion	1909869.295265
FMO2-HF: Total energy	-73638.361912
FMO2-MP2: Total energy	-73855.967342

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.
0.658	1.901	-0.013	-0.529	-0.701	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 : -0.005 / 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].
3	A	15	THR	0	-0.014	-0.003	3.789	1.567	2.782	-0.012	-0.529	-0.675
4	A	16	ILE	0	-0.003	-0.001	5.537	-0.335	-0.335	0.000	0.000	0.000
5	A	17	GLY	0	-0.004	0.007	9.206	0.085	0.085	0.000	0.000	0.000
6	A	18	GLU	-1	-0.871	-0.929	10.286	-0.349	-0.349	0.000	0.000	0.000
7	A	19	SER	0	0.007	0.006	11.809	0.038	0.038	0.000	0.000	0.000
8	A	20	ARG	1	0.791	0.881	13.826	0.051	0.051	0.000	0.000	0.000
9	A	21	ILE	0	0.008	0.008	16.899	0.030	0.030	0.000	0.000	0.000
10	A	22	ILE	0	0.006	0.007	19.598	-0.016	-0.016	0.000	0.000	0.000
11	A	23	TYR	0	-0.031	-0.030	23.181	0.012	0.012	0.000	0.000	0.000
12	A	24	PRO	0	0.027	0.010	25.716	-0.007	-0.007	0.000	0.000	0.000
13	A	25	LEU	0	0.011	0.010	29.273	0.001	0.001	0.000	0.000	0.000
14	A	26	ASP	-1	-0.873	-0.935	31.675	-0.001	-0.001	0.000	0.000	0.000
15	A	27	ALA	0	-0.036	0.001	29.403	0.004	0.004	0.000	0.000	0.000
16	A	28	ALA	0	0.037	0.022	31.087	-0.003	-0.003	0.000	0.000	0.000
17	A	29	GLY	0	-0.017	-0.022	27.739	-0.003	-0.003	0.000	0.000	0.000
18	A	30	VAL	0	-0.033	0.005	22.558	0.005	0.005	0.000	0.000	0.000
19	A	31	MET	0	-0.009	-0.006	22.309	-0.009	-0.009	0.000	0.000	0.000
20	A	32	VAL	0	0.007	0.016	15.865	0.005	0.005	0.000	0.000	0.000
21	A	33	SER	0	-0.004	-0.002	15.385	-0.007	-0.007	0.000	0.000	0.000
22	A	34	VAL	0	0.017	0.011	13.117	-0.001	-0.001	0.000	0.000	0.000
23	A	35	LYS	1	0.905	0.932	10.408	-0.618	-0.618	0.000	0.000	0.000
24	A	36	ASN	0	-0.006	0.003	9.922	0.027	0.027	0.000	0.000	0.000
25	A	37	THR	0	-0.016	-0.017	4.716	-0.202	-0.174	-0.001	0.000	-0.026
26	A	38	GLN	0	0.010	0.025	5.750	0.048	0.048	0.000	0.000	0.000
27	A	39	ASP	-1	-0.817	-0.920	9.136	0.622	0.622	0.000	0.000	0.000
28	A	40	TYR	0	0.008	-0.002	9.841	-0.053	-0.053	0.000	0.000	0.000
29	A	41	PRO	0	-0.025	-0.007	13.417	0.019	0.019	0.000	0.000	0.000
30	A	42	VAL	0	-0.027	-0.014	12.185	-0.029	-0.029	0.000	0.000	0.000
31	A	43	LEU	0	-0.029	-0.025	15.374	0.020	0.020	0.000	0.000	0.000
32	A	44	ILE	0	0.002	0.006	13.342	-0.027	-0.027	0.000	0.000	0.000
33	A	45	GLN	0	0.031	0.014	16.802	0.011	0.011	0.000	0.000	0.000
34	A	46	SER	0	0.001	-0.003	17.299	-0.024	-0.024	0.000	0.000	0.000
35	A	47	ARG	1	0.847	0.928	18.930	0.057	0.057	0.000	0.000	0.000
36	A	48	ILE	0	0.027	0.008	19.834	-0.009	-0.009	0.000	0.000	0.000
37	A	49	TYR	0	-0.023	-0.002	19.257	-0.003	-0.003	0.000	0.000	0.000
38	A	50	ASP	-1	-0.711	-0.867	22.937	-0.103	-0.103	0.000	0.000	0.000
39	A	51	GLU	-1	-0.917	-0.968	22.850	-0.113	-0.113	0.000	0.000	0.000
40	A	52	ASN	0	-0.026	-0.017	22.408	-0.023	-0.023	0.000	0.000	0.000
41	A	53	LYS	1	0.830	0.923	15.686	0.247	0.247	0.000	0.000	0.000
42	A	54	GLU	-1	-0.895	-0.930	21.166	-0.129	-0.129	0.000	0.000	0.000
43	A	55	LYS	1	0.779	0.870	24.357	0.064	0.064	0.000	0.000	0.000
44	A	56	GLU	-1	-0.748	-0.858	26.058	-0.061	-0.061	0.000	0.000	0.000
45	A	57	SER	0	-0.007	-0.010	29.055	0.002	0.002	0.000	0.000	0.000
46	A	58	GLU	-1	-0.937	-0.965	32.368	-0.026	-0.026	0.000	0.000	0.000
47	A	59	ASP	-1	-0.873	-0.920	27.031	-0.052	-0.052	0.000	0.000	0.000
48	A	60	PRO	0	0.012	0.015	27.468	0.006	0.006	0.000	0.000	0.000
49	A	61	PHE	0	-0.009	-0.014	25.513	0.005	0.005	0.000	0.000	0.000
50	A	62	VAL	0	0.056	0.030	26.734	-0.004	-0.004	0.000	0.000	0.000
51	A	63	VAL	0	-0.033	-0.021	20.479	0.006	0.006	0.000	0.000	0.000
52	A	64	THR	0	-0.075	-0.004	23.915	0.000	0.000	0.000	0.000	0.000
53	A	65	PRO	0	0.054	0.005	21.970	0.007	0.007	0.000	0.000	0.000
54	A	66	PRO	0	0.045	0.012	21.936	0.001	0.001	0.000	0.000	0.000
55	A	67	LEU	0	0.010	-0.012	20.523	-0.012	-0.012	0.000	0.000	0.000
56	A	68	PHE	0	-0.016	-0.005	17.297	0.009	0.009	0.000	0.000	0.000
57	A	69	ARG	1	0.934	0.969	19.011	-0.105	-0.105	0.000	0.000	0.000
58	A	70	LEU	0	-0.022	0.004	13.488	0.008	0.008	0.000	0.000	0.000
59	A	71	ASP	-1	-0.820	-0.927	15.617	0.152	0.152	0.000	0.000	0.000
60	A	72	DAL	0	0.037	0.017	13.108	0.033	0.033	0.000	0.000	0.000
61	A	73	LYS	1	0.805	0.910	9.072	-0.835	-0.835	0.000	0.000	0.000
62	A	74	GLN	0	-0.004	0.018	12.637	0.012	0.012	0.000	0.000	0.000
63	A	75	GLN	0	0.014	-0.007	13.808	0.087	0.087	0.000	0.000	0.000
64	A	76	ASN	0	0.034	0.018	15.628	-0.035	-0.035	0.000	0.000	0.000
65	A	77	SER	0	-0.047	-0.032	17.485	0.018	0.018	0.000	0.000	0.000
66	A	78	LEU	0	-0.017	0.013	17.076	-0.014	-0.014	0.000	0.000	0.000
67	A	79	ARG	1	0.990	0.985	20.563	-0.034	-0.034	0.000	0.000	0.000
68	A	80	ILE	0	-0.024	-0.009	19.678	-0.009	-0.009	0.000	0.000	0.000
69	A	81	ALA	0	0.029	0.003	24.050	0.004	0.004	0.000	0.000	0.000
70	A	82	GLN	0	-0.063	-0.048	27.790	-0.009	-0.009	0.000	0.000	0.000
71	A	83	ALA	0	-0.035	-0.036	29.792	0.004	0.004	0.000	0.000	0.000
72	A	84	GLY	0	0.044	0.025	31.937	-0.001	-0.001	0.000	0.000	0.000
73	A	85	GLY	0	-0.024	0.002	32.100	-0.002	-0.002	0.000	0.000	0.000
74	A	86	VAL	0	-0.002	0.007	33.133	0.003	0.003	0.000	0.000	0.000
75	A	87	PHE	0	-0.013	-0.013	29.537	-0.005	-0.005	0.000	0.000	0.000
76	A	88	PRO	0	-0.006	0.005	32.619	0.004	0.004	0.000	0.000	0.000
77	A	89	ARG	1	0.922	0.929	34.084	0.009	0.009	0.000	0.000	0.000
78	A	90	ASP	-1	-0.865	-0.927	36.277	-0.032	-0.032	0.000	0.000	0.000
79	A	91	LYS	1	0.931	0.952	32.105	0.050	0.050	0.000	0.000	0.000
80	A	92	GLU	-1	-0.751	-0.869	26.366	-0.042	-0.042	0.000	0.000	0.000
81	A	93	SER	0	-0.039	-0.014	28.148	-0.004	-0.004	0.000	0.000	0.000
82	A	94	LEU	0	-0.032	-0.004	20.687	0.003	0.003	0.000	0.000	0.000
83	A	95	LYS	1	0.830	0.908	23.092	0.063	0.063	0.000	0.000	0.000
84	A	96	TRP	0	-0.031	-0.034	15.053	-0.027	-0.027	0.000	0.000	0.000
85	A	97	LEU	0	0.014	0.024	16.412	0.012	0.012	0.000	0.000	0.000
86	A	98	CYS	0	-0.049	-0.004	10.729	0.056	0.056	0.000	0.000	0.000
87	A	99	VAL	0	0.026	-0.003	13.084	0.033	0.033	0.000	0.000	0.000
88	A	100	LYS	1	0.961	0.981	12.988	0.100	0.100	0.000	0.000	0.000
89	A	101	GLY	0	0.026	0.015	12.491	0.044	0.044	0.000	0.000	0.000
90	A	102	ILE	0	-0.060	-0.040	13.456	-0.043	-0.043	0.000	0.000	0.000
91	A	103	PRO	0	0.072	0.036	14.686	0.029	0.029	0.000	0.000	0.000
92	A	104	PRO	0	0.008	0.021	17.051	-0.012	-0.012	0.000	0.000	0.000
93	A	119	ASN	0	-0.034	-0.027	8.407	-0.079	-0.079	0.000	0.000	0.000
94	A	121	ILE	0	0.016	0.019	12.646	-0.035	-0.035	0.000	0.000	0.000
95	A	122	LYS	1	0.896	0.954	14.672	0.194	0.194	0.000	0.000	0.000
96	A	123	LEU	0	0.004	0.012	18.021	0.022	0.022	0.000	0.000	0.000
97	A	124	LEU	0	0.010	-0.008	20.986	-0.010	-0.010	0.000	0.000	0.000
98	A	125	VAL	0	0.012	0.017	23.638	0.012	0.012	0.000	0.000	0.000
99	A	126	ARG	1	0.757	0.836	24.876	0.011	0.011	0.000	0.000	0.000
100	A	127	PRO	0	0.032	0.027	29.117	0.006	0.006	0.000	0.000	0.000
101	A	128	ASN	0	0.035	0.015	32.781	0.002	0.002	0.000	0.000	0.000
102	A	129	GLU	-1	-0.797	-0.898	34.363	-0.007	-0.007	0.000	0.000	0.000
103	A	130	LEU	0	-0.049	0.003	30.916	-0.001	-0.001	0.000	0.000	0.000
104	A	131	LYS	1	0.844	0.914	34.285	0.008	0.008	0.000	0.000	0.000
105	A	132	GLY	0	0.016	0.004	32.718	-0.004	-0.004	0.000	0.000	0.000
106	A	133	THR	0	0.006	0.005	27.133	0.001	0.001	0.000	0.000	0.000
107	A	134	PRO	0	0.060	0.019	24.729	-0.002	-0.002	0.000	0.000	0.000
108	A	135	ILE	0	0.061	0.015	25.031	-0.005	-0.005	0.000	0.000	0.000
109	A	136	GLN	0	-0.059	-0.021	27.477	0.002	0.002	0.000	0.000	0.000
110	A	137	PHE	0	-0.014	-0.014	30.010	0.000	0.000	0.000	0.000	0.000
111	A	138	ALA	0	0.036	0.022	27.229	-0.005	-0.005	0.000	0.000	0.000
112	A	139	GLU	-1	-0.903	-0.951	28.942	-0.046	-0.046	0.000	0.000	0.000
113	A	140	ASN	0	-0.027	-0.039	31.859	-0.001	-0.001	0.000	0.000	0.000
114	A	141	LEU	0	-0.017	0.021	27.361	-0.001	-0.001	0.000	0.000	0.000
115	A	142	SER	0	-0.032	0.008	32.094	0.002	0.002	0.000	0.000	0.000
116	A	143	TRP	0	0.068	0.018	27.074	-0.007	-0.007	0.000	0.000	0.000
117	A	144	LYS	1	0.991	0.995	34.247	0.064	0.064	0.000	0.000	0.000
118	A	145	VAL	0	-0.004	-0.003	34.135	-0.007	-0.007	0.000	0.000	0.000
119	A	146	ASP	-1	-0.861	-0.923	35.860	-0.063	-0.063	0.000	0.000	0.000
120	A	147	GLY	0	-0.011	-0.008	36.005	-0.005	-0.005	0.000	0.000	0.000
121	A	148	GLY	0	-0.031	-0.010	34.898	-0.004	-0.004	0.000	0.000	0.000
122	A	149	LYS	1	0.921	0.962	30.372	0.112	0.112	0.000	0.000	0.000
123	A	150	LEU	0	0.002	0.012	28.287	0.008	0.008	0.000	0.000	0.000
124	A	151	ILE	0	-0.012	-0.015	30.167	-0.009	-0.009	0.000	0.000	0.000
125	A	152	ALA	0	0.003	0.002	29.087	0.006	0.006	0.000	0.000	0.000
126	A	153	GLU	-1	-0.914	-0.972	31.123	-0.057	-0.057	0.000	0.000	0.000
127	A	154	ASN	0	-0.019	-0.021	29.020	0.006	0.006	0.000	0.000	0.000
128	A	155	PRO	0	0.068	0.044	32.167	0.001	0.001	0.000	0.000	0.000
129	A	156	SER	0	-0.065	-0.028	30.785	0.006	0.006	0.000	0.000	0.000
130	A	157	PRO	0	0.020	-0.001	32.564	-0.004	-0.004	0.000	0.000	0.000
131	A	158	PHE	0	0.025	0.002	27.376	0.001	0.001	0.000	0.000	0.000
132	A	159	TYR	0	0.013	-0.003	24.036	-0.005	-0.005	0.000	0.000	0.000
133	A	160	MET	0	-0.031	0.019	25.128	0.003	0.003	0.000	0.000	0.000
134	A	161	ASN	0	0.020	-0.012	19.587	-0.027	-0.027	0.000	0.000	0.000
135	A	162	ILE	0	0.013	0.014	20.745	0.003	0.003	0.000	0.000	0.000
136	A	163	GLY	0	0.009	-0.004	17.660	-0.023	-0.023	0.000	0.000	0.000
137	A	164	GLU	-1	-0.908	-0.954	17.823	-0.182	-0.182	0.000	0.000	0.000
138	A	165	LEU	0	0.007	0.003	20.466	0.024	0.024	0.000	0.000	0.000
139	A	166	THR	0	-0.031	-0.009	23.322	-0.012	-0.012	0.000	0.000	0.000
140	A	167	PHE	0	0.056	0.006	25.841	0.013	0.013	0.000	0.000	0.000
141	A	168	GLY	0	0.012	0.011	29.207	-0.005	-0.005	0.000	0.000	0.000
142	A	169	GLY	0	-0.048	-0.020	28.460	0.000	0.000	0.000	0.000	0.000
143	A	170	LYS	1	0.928	0.977	25.896	0.124	0.124	0.000	0.000	0.000
144	A	171	SER	0	0.029	0.006	20.921	0.007	0.007	0.000	0.000	0.000
145	A	172	ILE	0	-0.042	-0.014	22.999	-0.003	-0.003	0.000	0.000	0.000
146	A	173	PRO	0	0.005	-0.004	19.141	-0.007	-0.007	0.000	0.000	0.000
147	A	174	SER	0	0.021	0.022	17.048	0.018	0.018	0.000	0.000	0.000
148	A	175	HIS	1	0.900	0.938	19.468	0.153	0.153	0.000	0.000	0.000
149	A	176	TYR	0	-0.079	-0.045	20.872	0.003	0.003	0.000	0.000	0.000
150	A	177	ILE	0	0.021	0.019	22.758	-0.002	-0.002	0.000	0.000	0.000
151	A	178	PRO	0	0.003	0.006	26.483	0.006	0.006	0.000	0.000	0.000
152	A	179	PRO	0	0.006	0.009	27.898	0.002	0.002	0.000	0.000	0.000
153	A	180	LYS	1	0.830	0.914	30.663	0.035	0.035	0.000	0.000	0.000
154	A	181	SER	0	0.007	0.016	31.526	0.000	0.000	0.000	0.000	0.000
155	A	182	THR	0	0.003	0.001	31.752	-0.001	-0.001	0.000	0.000	0.000
156	A	183	TRP	0	0.014	-0.013	25.301	-0.002	-0.002	0.000	0.000	0.000
157	A	184	ALA	0	0.005	0.017	29.153	0.002	0.002	0.000	0.000	0.000
158	A	185	PHE	0	-0.043	-0.025	23.107	-0.008	-0.008	0.000	0.000	0.000
159	A	186	ASP	-1	-0.873	-0.942	26.560	-0.142	-0.142	0.000	0.000	0.000
160	A	187	LEU	0	-0.014	-0.010	27.077	-0.010	-0.010	0.000	0.000	0.000
161	A	188	PRO	0	-0.001	0.000	26.020	0.004	0.004	0.000	0.000	0.000
162	A	189	LYS	1	0.988	0.980	28.823	0.123	0.123	0.000	0.000	0.000
163	A	190	GLY	0	0.016	-0.002	31.802	-0.004	-0.004	0.000	0.000	0.000
164	A	191	LEU	0	-0.014	-0.002	29.171	0.005	0.005	0.000	0.000	0.000
165	A	192	ALA	0	0.021	0.017	33.827	0.002	0.002	0.000	0.000	0.000
166	A	193	GLY	0	0.011	0.011	37.326	0.003	0.003	0.000	0.000	0.000
167	A	194	ALA	0	-0.040	-0.009	33.657	0.003	0.003	0.000	0.000	0.000
168	A	195	ARG	1	0.948	0.935	35.733	0.060	0.060	0.000	0.000	0.000
169	A	196	ASN	0	0.037	0.032	32.697	0.001	0.001	0.000	0.000	0.000
170	A	197	VAL	0	0.027	0.013	28.903	-0.008	-0.008	0.000	0.000	0.000
171	A	198	SER	0	-0.007	-0.001	27.435	0.013	0.013	0.000	0.000	0.000
172	A	199	TRP	0	-0.033	-0.024	24.763	-0.015	-0.015	0.000	0.000	0.000
173	A	200	ARG	1	0.923	0.980	20.985	0.109	0.109	0.000	0.000	0.000
174	A	201	ILE	0	-0.001	0.000	21.966	-0.019	-0.019	0.000	0.000	0.000
175	A	202	ILE	0	-0.013	0.003	15.884	0.004	0.004	0.000	0.000	0.000
176	A	203	ASN	0	0.040	0.020	19.675	0.010	0.010	0.000	0.000	0.000
177	A	204	ASP	-1	-0.740	-0.881	19.751	-0.016	-0.016	0.000	0.000	0.000
178	A	205	GLN	0	-0.053	-0.030	19.197	-0.002	-0.002	0.000	0.000	0.000
179	A	206	GLY	0	0.008	0.011	15.566	0.027	0.027	0.000	0.000	0.000
180	A	207	GLY	0	-0.009	-0.004	15.174	-0.016	-0.016	0.000	0.000	0.000
181	A	208	LEU	0	-0.029	-0.018	16.683	-0.014	-0.014	0.000	0.000	0.000
182	A	209	ASP	-1	-0.840	-0.919	19.163	-0.018	-0.018	0.000	0.000	0.000
183	A	210	ARG	1	0.877	0.936	22.940	0.028	0.028	0.000	0.000	0.000
184	A	211	LEU	0	-0.029	-0.009	24.964	-0.007	-0.007	0.000	0.000	0.000
185	A	212	TYR	0	-0.007	0.010	26.687	0.012	0.012	0.000	0.000	0.000
186	A	213	SER	0	0.025	-0.008	29.028	-0.008	-0.008	0.000	0.000	0.000
187	A	214	LYS	1	0.843	0.926	31.731	0.062	0.062	0.000	0.000	0.000
188	A	215	ASN	0	-0.011	-0.005	33.922	-0.009	-0.009	0.000	0.000	0.000
189	A	216	VAL	0	-0.006	0.004	34.411	0.002	0.002	0.000	0.000	0.000
190	A	217	THR	0	-0.025	0.005	36.790	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)