FMO DATABASE

FMODB ID: MN88Z

Calculation Name: 1G5Z-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1G5Z

Chain ID: A

ChEMBL ID:

UniProt ID: O31117

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	164
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1434585.199825
FMO2-HF: Nuclear repulsion	1373593.103741
FMO2-HF: Total energy	-60992.096084
FMO2-MP2: Total energy	-61173.696307

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:40:PRO)

Summations of interaction energy for fragment #1(A:40:PRO)

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.
-13.784	-6.213	6.621	-4.863	-9.332	-0.009

Interaction energy analysis for fragmet #1(A:40:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.064 / q_NPA : 0.009

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	42	LEU	0	0.036	0.020	3.692	-2.785	-0.935	0.002	-0.808	-1.045	0.003
4	A	43	THR	0	-0.003	-0.002	3.175	-2.238	-1.045	0.016	-0.461	-0.748	-0.001
5	A	44	GLU	-1	-0.891	-0.929	4.374	-0.296	-0.004	-0.001	-0.027	-0.264	0.000
6	A	45	ILE	0	-0.015	-0.008	2.603	-0.288	0.091	0.880	-0.275	-0.984	-0.001
7	A	46	SER	0	-0.002	-0.009	6.648	0.239	0.239	0.000	0.000	0.000	0.000
8	A	47	LYS	1	0.887	0.959	9.263	0.361	0.361	0.000	0.000	0.000	0.000
9	A	48	LYS	1	0.882	0.919	8.134	0.845	0.845	0.000	0.000	0.000	0.000
10	A	49	ILE	0	0.016	0.023	7.801	0.108	0.108	0.000	0.000	0.000	0.000
11	A	50	THR	0	-0.039	-0.038	11.638	0.120	0.120	0.000	0.000	0.000	0.000
12	A	51	GLU	-1	-0.858	-0.913	14.429	-0.180	-0.180	0.000	0.000	0.000	0.000
13	A	52	SER	0	0.012	-0.023	13.529	0.027	0.027	0.000	0.000	0.000	0.000
14	A	53	ASN	0	-0.010	-0.010	15.674	0.027	0.027	0.000	0.000	0.000	0.000
15	A	54	ALA	0	-0.004	0.004	17.417	0.036	0.036	0.000	0.000	0.000	0.000
16	A	55	VAL	0	0.002	0.004	19.503	0.030	0.030	0.000	0.000	0.000	0.000
17	A	56	VAL	0	0.010	-0.001	18.913	0.022	0.022	0.000	0.000	0.000	0.000
18	A	57	LEU	0	-0.033	-0.018	21.198	0.023	0.023	0.000	0.000	0.000	0.000
19	A	58	ALA	0	0.006	0.007	23.455	0.019	0.019	0.000	0.000	0.000	0.000
20	A	59	VAL	0	0.006	0.000	24.520	0.017	0.017	0.000	0.000	0.000	0.000
21	A	60	LYS	1	0.887	0.939	25.043	0.230	0.230	0.000	0.000	0.000	0.000
22	A	61	GLU	-1	-0.802	-0.874	26.989	-0.128	-0.128	0.000	0.000	0.000	0.000
23	A	62	VAL	0	0.019	0.008	29.575	0.011	0.011	0.000	0.000	0.000	0.000
24	A	63	GLU	-1	-0.809	-0.873	26.748	-0.204	-0.204	0.000	0.000	0.000	0.000
25	A	64	THR	0	-0.040	-0.028	30.217	0.006	0.006	0.000	0.000	0.000	0.000
26	A	65	LEU	0	0.007	0.010	32.749	0.008	0.008	0.000	0.000	0.000	0.000
27	A	66	LEU	0	0.021	0.016	33.322	0.008	0.008	0.000	0.000	0.000	0.000
28	A	67	ALA	0	-0.011	-0.008	34.484	0.006	0.006	0.000	0.000	0.000	0.000
29	A	68	SER	0	-0.058	-0.038	36.434	0.007	0.007	0.000	0.000	0.000	0.000
30	A	69	ILE	0	0.027	0.010	38.875	0.006	0.006	0.000	0.000	0.000	0.000
31	A	70	ASP	-1	-0.813	-0.909	39.071	-0.101	-0.101	0.000	0.000	0.000	0.000
32	A	71	GLU	-1	-0.856	-0.891	39.913	-0.101	-0.101	0.000	0.000	0.000	0.000
33	A	72	LEU	0	-0.011	-0.015	41.849	0.005	0.005	0.000	0.000	0.000	0.000
34	A	73	ALA	0	-0.013	-0.013	44.162	0.004	0.004	0.000	0.000	0.000	0.000
35	A	74	THR	0	-0.062	-0.056	43.001	0.003	0.003	0.000	0.000	0.000	0.000
36	A	75	LYS	1	0.788	0.885	41.978	0.101	0.101	0.000	0.000	0.000	0.000
37	A	76	ALA	0	-0.006	-0.005	47.066	0.003	0.003	0.000	0.000	0.000	0.000
38	A	77	ILE	0	0.009	0.018	48.609	0.004	0.004	0.000	0.000	0.000	0.000
39	A	78	GLY	0	0.013	0.026	51.214	0.000	0.000	0.000	0.000	0.000	0.000
40	A	79	LYS	1	0.759	0.874	51.528	0.064	0.064	0.000	0.000	0.000	0.000
41	A	80	LYS	1	0.868	0.933	54.289	0.053	0.053	0.000	0.000	0.000	0.000
42	A	81	ILE	0	0.042	0.015	51.117	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	82	GLY	0	-0.012	-0.004	54.177	0.003	0.003	0.000	0.000	0.000	0.000
44	A	83	ASN	0	-0.038	-0.028	55.198	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	84	ASN	0	0.012	0.010	54.910	0.000	0.000	0.000	0.000	0.000	0.000
46	A	85	GLY	0	0.036	0.031	51.329	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	86	LEU	0	-0.028	-0.007	48.165	0.002	0.002	0.000	0.000	0.000	0.000
48	A	87	GLU	-1	-0.857	-0.924	52.179	-0.054	-0.054	0.000	0.000	0.000	0.000
49	A	88	ALA	0	0.005	-0.012	55.557	0.000	0.000	0.000	0.000	0.000	0.000
50	A	89	ASN	0	-0.021	-0.027	56.886	0.003	0.003	0.000	0.000	0.000	0.000
51	A	90	GLN	0	0.000	0.014	57.518	0.000	0.000	0.000	0.000	0.000	0.000
52	A	91	SER	0	-0.040	-0.033	57.839	0.001	0.001	0.000	0.000	0.000	0.000
53	A	92	LYS	1	0.896	0.950	57.455	0.047	0.047	0.000	0.000	0.000	0.000
54	A	93	ASN	0	-0.033	-0.019	52.800	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	94	THR	0	0.041	0.010	52.741	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	95	SER	0	0.026	0.023	52.716	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	96	LEU	0	-0.002	0.008	47.715	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	97	LEU	0	0.009	-0.003	48.173	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	98	SER	0	-0.005	-0.007	48.307	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	99	GLY	0	-0.004	0.004	46.619	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	100	ALA	0	0.007	-0.007	43.916	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	101	TYR	0	-0.081	-0.058	43.564	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	102	ALA	0	0.051	0.042	44.048	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	103	ILE	0	-0.023	-0.012	38.900	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	104	SER	0	-0.042	-0.032	39.378	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	105	ASP	-1	-0.810	-0.884	39.883	-0.068	-0.068	0.000	0.000	0.000	0.000
67	A	106	LEU	0	0.010	0.012	36.347	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	107	ILE	0	-0.032	-0.027	35.009	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	108	ALA	0	0.028	0.013	35.100	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	109	GLU	-1	-0.949	-0.974	36.094	-0.081	-0.081	0.000	0.000	0.000	0.000
71	A	110	LYS	1	0.797	0.886	31.404	0.123	0.123	0.000	0.000	0.000	0.000
72	A	111	LEU	0	-0.009	-0.011	30.820	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	112	ASN	0	-0.038	-0.009	31.955	0.001	0.001	0.000	0.000	0.000	0.000
74	A	113	VAL	0	0.003	0.004	29.752	0.003	0.003	0.000	0.000	0.000	0.000
75	A	114	LEU	0	0.000	0.013	25.073	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	115	LYS	1	0.790	0.876	25.824	0.113	0.113	0.000	0.000	0.000	0.000
77	A	116	ASN	0	0.008	-0.026	19.521	-0.012	-0.012	0.000	0.000	0.000	0.000
78	A	117	GLU	-1	-0.896	-0.942	22.057	-0.084	-0.084	0.000	0.000	0.000	0.000
79	A	118	GLU	-1	-0.877	-0.925	17.237	-0.217	-0.217	0.000	0.000	0.000	0.000
80	A	119	LEU	0	-0.009	-0.003	20.680	0.000	0.000	0.000	0.000	0.000	0.000
81	A	120	LYS	1	0.909	0.955	23.605	0.087	0.087	0.000	0.000	0.000	0.000
82	A	121	GLU	-1	-0.798	-0.885	26.730	-0.126	-0.126	0.000	0.000	0.000	0.000
83	A	122	LYS	1	0.842	0.912	24.687	0.156	0.156	0.000	0.000	0.000	0.000
84	A	123	ILE	0	0.009	0.008	24.998	0.002	0.002	0.000	0.000	0.000	0.000
85	A	124	ASP	-1	-0.822	-0.894	29.117	-0.081	-0.081	0.000	0.000	0.000	0.000
86	A	125	THR	0	-0.013	-0.019	31.241	0.003	0.003	0.000	0.000	0.000	0.000
87	A	126	ALA	0	0.024	0.016	31.414	0.004	0.004	0.000	0.000	0.000	0.000
88	A	127	LYS	1	0.893	0.942	31.908	0.095	0.095	0.000	0.000	0.000	0.000
89	A	128	GLN	0	-0.047	-0.015	35.006	0.005	0.005	0.000	0.000	0.000	0.000
90	A	129	CYS	0	-0.031	-0.020	36.225	0.004	0.004	0.000	0.000	0.000	0.000
91	A	130	SER	0	0.042	0.014	36.739	0.001	0.001	0.000	0.000	0.000	0.000
92	A	131	THR	0	-0.048	-0.024	38.671	0.004	0.004	0.000	0.000	0.000	0.000
93	A	132	GLU	-1	-0.879	-0.928	41.080	-0.067	-0.067	0.000	0.000	0.000	0.000
94	A	133	PHE	0	0.011	-0.002	40.726	0.003	0.003	0.000	0.000	0.000	0.000
95	A	134	THR	0	0.027	0.013	42.223	0.002	0.002	0.000	0.000	0.000	0.000
96	A	135	ASN	0	0.018	-0.010	44.213	0.004	0.004	0.000	0.000	0.000	0.000
97	A	136	LYS	1	0.844	0.955	46.202	0.058	0.058	0.000	0.000	0.000	0.000
98	A	137	LEU	0	0.009	0.012	45.194	0.003	0.003	0.000	0.000	0.000	0.000
99	A	138	LYS	1	0.889	0.952	46.238	0.059	0.059	0.000	0.000	0.000	0.000
100	A	139	SER	0	-0.066	-0.046	50.412	0.003	0.003	0.000	0.000	0.000	0.000
101	A	140	GLU	-1	-0.815	-0.904	52.029	-0.047	-0.047	0.000	0.000	0.000	0.000
102	A	141	HIS	0	0.021	0.019	53.912	0.000	0.000	0.000	0.000	0.000	0.000
103	A	142	ALA	0	-0.015	-0.004	54.973	0.000	0.000	0.000	0.000	0.000	0.000
104	A	143	VAL	0	-0.042	-0.019	56.456	0.001	0.001	0.000	0.000	0.000	0.000
105	A	144	LEU	0	-0.048	-0.043	50.620	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	145	GLY	0	0.039	0.022	54.204	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	146	LEU	0	0.014	0.021	56.038	0.001	0.001	0.000	0.000	0.000	0.000
108	A	147	ASP	-1	-0.892	-0.937	58.590	-0.043	-0.043	0.000	0.000	0.000	0.000
109	A	148	ASN	0	-0.052	-0.031	59.807	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	149	LEU	0	0.002	0.026	53.199	0.000	0.000	0.000	0.000	0.000	0.000
111	A	150	THR	0	0.080	0.023	57.112	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	151	ASP	-1	-0.745	-0.874	54.756	-0.056	-0.056	0.000	0.000	0.000	0.000
113	A	152	ASP	-1	-0.755	-0.847	53.626	-0.055	-0.055	0.000	0.000	0.000	0.000
114	A	153	ASN	0	0.004	-0.017	53.661	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	154	ALA	0	0.047	0.031	51.249	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	155	GLN	0	-0.001	-0.016	49.466	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	156	ARG	1	0.785	0.857	48.847	0.049	0.049	0.000	0.000	0.000	0.000
118	A	157	ALA	0	0.002	0.011	48.701	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	158	ILE	0	0.007	-0.006	44.794	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	159	LEU	0	-0.013	0.008	44.333	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	160	LYS	1	0.818	0.913	37.695	0.113	0.113	0.000	0.000	0.000	0.000
122	A	161	LYS	1	0.858	0.912	39.235	0.102	0.102	0.000	0.000	0.000	0.000
123	A	162	HIS	0	0.005	0.008	45.223	0.000	0.000	0.000	0.000	0.000	0.000
124	A	163	ALA	0	-0.001	0.004	48.717	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	164	ASN	0	-0.055	-0.022	50.836	0.001	0.001	0.000	0.000	0.000	0.000
126	A	165	LYS	1	0.883	0.917	45.676	0.069	0.069	0.000	0.000	0.000	0.000
127	A	166	ASP	-1	-0.784	-0.873	48.652	-0.054	-0.054	0.000	0.000	0.000	0.000
128	A	167	LYS	1	0.793	0.881	50.084	0.052	0.052	0.000	0.000	0.000	0.000
129	A	168	GLY	0	0.081	0.048	46.446	0.000	0.000	0.000	0.000	0.000	0.000
130	A	169	ALA	0	0.003	0.019	44.615	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	170	ALA	0	0.018	0.003	43.603	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	171	GLU	-1	-0.873	-0.953	42.254	-0.070	-0.070	0.000	0.000	0.000	0.000
133	A	172	LEU	0	0.010	0.017	39.365	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	173	GLU	-1	-0.826	-0.919	38.933	-0.108	-0.108	0.000	0.000	0.000	0.000
135	A	174	LYS	1	0.846	0.918	37.697	0.065	0.065	0.000	0.000	0.000	0.000
136	A	175	LEU	0	0.021	0.012	35.143	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	176	PHE	0	0.015	0.008	34.458	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	177	LYS	1	0.827	0.888	32.625	0.124	0.124	0.000	0.000	0.000	0.000
139	A	178	ALA	0	0.007	0.019	31.855	-0.008	-0.008	0.000	0.000	0.000	0.000
140	A	179	VAL	0	0.059	0.019	29.750	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	180	GLU	-1	-0.786	-0.848	28.557	-0.168	-0.168	0.000	0.000	0.000	0.000
142	A	181	ASN	0	-0.058	-0.062	27.302	-0.023	-0.023	0.000	0.000	0.000	0.000
143	A	182	LEU	0	0.001	0.013	24.895	-0.012	-0.012	0.000	0.000	0.000	0.000
144	A	183	SER	0	0.001	-0.028	24.130	-0.026	-0.026	0.000	0.000	0.000	0.000
145	A	184	LYS	1	0.800	0.889	22.817	0.161	0.161	0.000	0.000	0.000	0.000
146	A	185	ALA	0	0.053	0.037	20.998	-0.026	-0.026	0.000	0.000	0.000	0.000
147	A	186	ALA	0	0.031	0.030	19.413	-0.026	-0.026	0.000	0.000	0.000	0.000
148	A	187	GLN	0	-0.050	-0.043	18.318	-0.060	-0.060	0.000	0.000	0.000	0.000
149	A	188	ASP	-1	-0.894	-0.954	17.172	-0.412	-0.412	0.000	0.000	0.000	0.000
150	A	189	THR	0	0.017	0.012	14.859	-0.070	-0.070	0.000	0.000	0.000	0.000
151	A	190	LEU	0	-0.004	0.000	13.478	-0.084	-0.084	0.000	0.000	0.000	0.000
152	A	191	LYS	1	0.849	0.913	12.904	0.450	0.450	0.000	0.000	0.000	0.000
153	A	192	ASN	0	-0.032	-0.017	11.332	-0.139	-0.139	0.000	0.000	0.000	0.000
154	A	193	ALA	0	0.043	0.027	8.971	-0.179	-0.179	0.000	0.000	0.000	0.000
155	A	194	VAL	0	-0.033	-0.026	7.939	-0.254	-0.254	0.000	0.000	0.000	0.000
156	A	195	LYS	1	0.947	0.976	8.453	0.456	0.456	0.000	0.000	0.000	0.000
157	A	196	GLU	-1	-0.822	-0.889	5.275	-1.243	-1.243	0.000	0.000	0.000	0.000
158	A	197	LEU	0	-0.018	-0.004	3.547	-1.757	-0.984	0.025	-0.216	-0.582	-0.001
159	A	198	THR	0	-0.059	-0.025	3.569	-1.672	-1.062	0.014	-0.257	-0.367	-0.002
160	A	199	SER	0	-0.022	-0.006	3.958	0.881	1.016	-0.001	-0.030	-0.105	0.000
161	A	200	PRO	0	-0.008	-0.008	2.681	-3.255	-1.697	0.574	-0.711	-1.421	-0.009
162	A	201	ILE	0	-0.002	-0.008	2.190	-1.794	-1.191	5.106	-2.035	-3.674	0.002
163	A	202	VAL	0	-0.025	-0.011	3.824	-0.304	-0.126	0.006	-0.043	-0.142	0.000
164	A	203	ALA	0	0.016	0.025	6.737	-0.327	-0.327	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:40:PRO)