FMO DATABASE

FMODB ID: 98772

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	OptHSide
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	-1430974.76206
FMO2-HF: Nuclear repulsion	1369983.428243
FMO2-HF: Total energy	-60991.333816
FMO2-MP2: Total energy	-61173.073827

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.
-11.714	-6.202	12.045	-6.446	-11.109	-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 : 0.051 / q_NPA : -0.010

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	0.040	0.034	3.518	-2.979	-1.035	0.014	-0.766	-1.191	0.004
4	A	43	THR	0	0.034	-0.003	2.617	-3.159	-0.991	0.103	-0.888	-1.384	-0.004
5	A	44	GLU	-1	-0.944	-0.955	4.045	-0.123	0.300	0.001	-0.069	-0.354	0.000
6	A	45	ILE	0	-0.050	-0.035	2.403	-0.212	0.158	0.718	-0.250	-0.838	-0.001
7	A	46	SER	0	0.064	0.034	6.580	0.325	0.325	0.000	0.000	0.000	0.000
8	A	47	LYS	1	0.938	0.977	9.460	0.471	0.471	0.000	0.000	0.000	0.000
9	A	48	LYS	1	0.889	0.923	8.090	0.973	0.973	0.000	0.000	0.000	0.000
10	A	49	ILE	0	-0.008	0.014	7.924	0.116	0.116	0.000	0.000	0.000	0.000
11	A	50	THR	0	-0.074	-0.057	11.741	0.126	0.126	0.000	0.000	0.000	0.000
12	A	51	GLU	-1	-0.890	-0.936	14.371	-0.230	-0.230	0.000	0.000	0.000	0.000
13	A	52	SER	0	-0.002	-0.028	13.284	0.044	0.044	0.000	0.000	0.000	0.000
14	A	53	ASN	0	0.007	0.000	15.994	0.026	0.026	0.000	0.000	0.000	0.000
15	A	54	ALA	0	-0.007	-0.002	17.494	0.039	0.039	0.000	0.000	0.000	0.000
16	A	55	VAL	0	0.007	0.015	19.530	0.035	0.035	0.000	0.000	0.000	0.000
17	A	56	VAL	0	0.025	0.011	18.829	0.025	0.025	0.000	0.000	0.000	0.000
18	A	57	LEU	0	-0.060	-0.030	21.203	0.023	0.023	0.000	0.000	0.000	0.000
19	A	58	ALA	0	0.019	0.014	23.463	0.021	0.021	0.000	0.000	0.000	0.000
20	A	59	VAL	0	0.009	-0.007	24.585	0.019	0.019	0.000	0.000	0.000	0.000
21	A	60	LYS	1	1.004	1.016	25.362	0.242	0.242	0.000	0.000	0.000	0.000
22	A	61	GLU	-1	-0.832	-0.883	27.197	-0.140	-0.140	0.000	0.000	0.000	0.000
23	A	62	VAL	0	0.020	0.000	29.569	0.013	0.013	0.000	0.000	0.000	0.000
24	A	63	GLU	-1	-0.857	-0.914	27.019	-0.204	-0.204	0.000	0.000	0.000	0.000
25	A	64	THR	0	-0.078	-0.054	30.466	0.007	0.007	0.000	0.000	0.000	0.000
26	A	65	LEU	0	0.017	0.015	32.894	0.009	0.009	0.000	0.000	0.000	0.000
27	A	66	LEU	0	0.031	0.029	33.591	0.009	0.009	0.000	0.000	0.000	0.000
28	A	67	ALA	0	-0.018	-0.014	34.680	0.007	0.007	0.000	0.000	0.000	0.000
29	A	68	SER	0	-0.044	-0.024	36.643	0.006	0.006	0.000	0.000	0.000	0.000
30	A	69	ILE	0	0.030	0.012	39.003	0.006	0.006	0.000	0.000	0.000	0.000
31	A	70	ASP	-1	-0.845	-0.932	39.493	-0.101	-0.101	0.000	0.000	0.000	0.000
32	A	71	GLU	-1	-0.826	-0.882	40.348	-0.102	-0.102	0.000	0.000	0.000	0.000
33	A	72	LEU	0	-0.027	-0.021	42.220	0.005	0.005	0.000	0.000	0.000	0.000
34	A	73	ALA	0	-0.011	-0.013	44.399	0.005	0.005	0.000	0.000	0.000	0.000
35	A	74	THR	0	-0.072	-0.050	43.389	0.003	0.003	0.000	0.000	0.000	0.000
36	A	75	LYS	1	0.781	0.879	42.399	0.102	0.102	0.000	0.000	0.000	0.000
37	A	76	ALA	0	-0.011	-0.008	47.203	0.003	0.003	0.000	0.000	0.000	0.000
38	A	77	ILE	0	-0.003	0.012	48.768	0.004	0.004	0.000	0.000	0.000	0.000
39	A	78	GLY	0	-0.001	0.007	51.322	0.000	0.000	0.000	0.000	0.000	0.000
40	A	79	LYS	1	0.784	0.883	51.620	0.066	0.066	0.000	0.000	0.000	0.000
41	A	80	LYS	1	0.866	0.930	54.345	0.054	0.054	0.000	0.000	0.000	0.000
42	A	81	ILE	0	0.009	-0.005	51.473	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	82	GLY	0	0.016	0.000	54.356	0.003	0.003	0.000	0.000	0.000	0.000
44	A	83	ASN	0	-0.045	-0.028	55.174	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	84	ASN	0	-0.002	-0.005	55.287	0.000	0.000	0.000	0.000	0.000	0.000
46	A	85	GLY	0	0.039	0.029	51.886	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	86	LEU	0	-0.042	0.003	48.558	0.003	0.003	0.000	0.000	0.000	0.000
48	A	87	GLU	-1	-0.869	-0.926	52.663	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	88	ALA	0	0.020	0.009	55.777	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	89	ASN	0	0.006	-0.010	57.386	0.003	0.003	0.000	0.000	0.000	0.000
51	A	90	GLN	0	-0.003	0.009	57.552	0.000	0.000	0.000	0.000	0.000	0.000
52	A	91	SER	0	-0.046	-0.028	58.484	0.001	0.001	0.000	0.000	0.000	0.000
53	A	92	LYS	1	0.898	0.943	57.725	0.048	0.048	0.000	0.000	0.000	0.000
54	A	93	ASN	0	-0.035	-0.009	53.123	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	94	THR	0	0.063	0.033	53.251	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	95	SER	0	0.035	0.015	52.907	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	96	LEU	0	-0.021	0.004	48.126	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	97	LEU	0	0.030	0.007	48.601	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	98	SER	0	-0.017	-0.009	48.484	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	99	GLY	0	0.005	0.012	46.611	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	100	ALA	0	0.004	0.003	44.068	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	101	TYR	0	-0.007	-0.002	43.568	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	102	ALA	0	0.046	0.041	43.992	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	103	ILE	0	-0.017	-0.012	38.856	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	104	SER	0	-0.049	-0.034	39.313	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	105	ASP	-1	-0.849	-0.934	39.832	-0.075	-0.075	0.000	0.000	0.000	0.000
67	A	106	LEU	0	-0.021	-0.004	36.477	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	107	ILE	0	-0.027	-0.021	35.031	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	108	ALA	0	0.015	0.011	35.089	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	109	GLU	-1	-0.957	-0.980	35.827	-0.092	-0.092	0.000	0.000	0.000	0.000
71	A	110	LYS	1	0.806	0.889	31.345	0.136	0.136	0.000	0.000	0.000	0.000
72	A	111	LEU	0	0.018	0.005	30.547	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	112	ASN	0	-0.047	-0.013	31.567	0.001	0.001	0.000	0.000	0.000	0.000
74	A	113	VAL	0	-0.016	-0.010	29.781	0.005	0.005	0.000	0.000	0.000	0.000
75	A	114	LEU	0	-0.016	0.010	24.970	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	115	LYS	1	0.808	0.893	26.033	0.125	0.125	0.000	0.000	0.000	0.000
77	A	116	ASN	0	0.034	-0.014	19.483	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	117	GLU	-1	-0.890	-0.944	22.040	-0.102	-0.102	0.000	0.000	0.000	0.000
79	A	118	GLU	-1	-0.918	-0.944	17.175	-0.274	-0.274	0.000	0.000	0.000	0.000
80	A	119	LEU	0	0.008	0.000	21.054	0.004	0.004	0.000	0.000	0.000	0.000
81	A	120	LYS	1	0.890	0.936	23.858	0.102	0.102	0.000	0.000	0.000	0.000
82	A	121	GLU	-1	-0.823	-0.892	26.956	-0.129	-0.129	0.000	0.000	0.000	0.000
83	A	122	LYS	1	0.871	0.907	24.944	0.164	0.164	0.000	0.000	0.000	0.000
84	A	123	ILE	0	-0.007	0.008	25.125	0.002	0.002	0.000	0.000	0.000	0.000
85	A	124	ASP	-1	-0.823	-0.885	29.285	-0.091	-0.091	0.000	0.000	0.000	0.000
86	A	125	THR	0	-0.001	0.004	31.635	0.004	0.004	0.000	0.000	0.000	0.000
87	A	126	ALA	0	0.047	0.031	31.512	0.005	0.005	0.000	0.000	0.000	0.000
88	A	127	LYS	1	0.905	0.943	31.737	0.107	0.107	0.000	0.000	0.000	0.000
89	A	128	GLN	0	-0.052	-0.028	34.972	0.005	0.005	0.000	0.000	0.000	0.000
90	A	129	CYS	0	-0.046	-0.025	36.624	0.005	0.005	0.000	0.000	0.000	0.000
91	A	130	SER	0	0.037	0.007	36.455	0.002	0.002	0.000	0.000	0.000	0.000
92	A	131	THR	0	-0.047	-0.021	38.473	0.005	0.005	0.000	0.000	0.000	0.000
93	A	132	GLU	-1	-0.864	-0.921	41.183	-0.069	-0.069	0.000	0.000	0.000	0.000
94	A	133	PHE	0	0.009	-0.003	40.918	0.003	0.003	0.000	0.000	0.000	0.000
95	A	134	THR	0	0.031	0.009	42.387	0.002	0.002	0.000	0.000	0.000	0.000
96	A	135	ASN	0	-0.004	-0.022	44.320	0.004	0.004	0.000	0.000	0.000	0.000
97	A	136	LYS	1	0.821	0.936	46.343	0.061	0.061	0.000	0.000	0.000	0.000
98	A	137	LEU	0	0.016	0.013	45.329	0.003	0.003	0.000	0.000	0.000	0.000
99	A	138	LYS	1	0.920	0.965	46.600	0.063	0.063	0.000	0.000	0.000	0.000
100	A	139	SER	0	-0.053	-0.028	50.562	0.003	0.003	0.000	0.000	0.000	0.000
101	A	140	GLU	-1	-0.822	-0.906	52.030	-0.049	-0.049	0.000	0.000	0.000	0.000
102	A	141	HIS	0	0.027	0.005	53.859	0.000	0.000	0.000	0.000	0.000	0.000
103	A	142	ALA	0	-0.038	-0.015	54.877	0.000	0.000	0.000	0.000	0.000	0.000
104	A	143	VAL	0	-0.017	-0.014	56.609	0.001	0.001	0.000	0.000	0.000	0.000
105	A	144	LEU	0	-0.049	-0.031	50.696	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	145	GLY	0	0.034	0.020	54.369	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	146	LEU	0	-0.044	-0.004	56.177	0.002	0.002	0.000	0.000	0.000	0.000
108	A	147	ASP	-1	-0.822	-0.931	58.702	-0.046	-0.046	0.000	0.000	0.000	0.000
109	A	148	ASN	0	-0.090	-0.030	59.405	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	149	LEU	0	0.031	0.040	53.573	0.000	0.000	0.000	0.000	0.000	0.000
111	A	150	THR	0	0.069	0.011	57.529	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	151	ASP	-1	-0.752	-0.894	54.752	-0.058	-0.058	0.000	0.000	0.000	0.000
113	A	152	ASP	-1	-0.802	-0.867	53.828	-0.056	-0.056	0.000	0.000	0.000	0.000
114	A	153	ASN	0	0.011	-0.016	53.936	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	154	ALA	0	0.038	0.033	51.502	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	155	GLN	0	0.006	-0.009	49.583	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	156	ARG	1	0.770	0.873	49.129	0.051	0.051	0.000	0.000	0.000	0.000
118	A	157	ALA	0	-0.029	-0.022	48.869	0.000	0.000	0.000	0.000	0.000	0.000
119	A	158	ILE	0	-0.009	-0.019	44.956	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	159	LEU	0	-0.002	0.014	44.527	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	160	LYS	1	0.859	0.938	37.939	0.115	0.115	0.000	0.000	0.000	0.000
122	A	161	LYS	1	0.950	0.961	40.275	0.101	0.101	0.000	0.000	0.000	0.000
123	A	162	HIS	0	0.008	0.010	45.591	0.000	0.000	0.000	0.000	0.000	0.000
124	A	163	ALA	0	0.008	0.002	49.031	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	164	ASN	0	-0.056	-0.007	51.496	0.001	0.001	0.000	0.000	0.000	0.000
126	A	165	LYS	1	0.908	0.921	45.696	0.071	0.071	0.000	0.000	0.000	0.000
127	A	166	ASP	-1	-0.802	-0.895	48.898	-0.056	-0.056	0.000	0.000	0.000	0.000
128	A	167	LYS	1	0.823	0.907	50.206	0.054	0.054	0.000	0.000	0.000	0.000
129	A	168	GLY	0	0.093	0.057	46.763	0.000	0.000	0.000	0.000	0.000	0.000
130	A	169	ALA	0	0.007	0.034	44.980	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	170	ALA	0	0.013	0.014	43.776	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	171	GLU	-1	-0.849	-0.942	42.737	-0.072	-0.072	0.000	0.000	0.000	0.000
133	A	172	LEU	0	-0.019	0.000	39.716	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	173	GLU	-1	-0.894	-0.975	39.053	-0.109	-0.109	0.000	0.000	0.000	0.000
135	A	174	LYS	1	0.886	0.940	38.102	0.069	0.069	0.000	0.000	0.000	0.000
136	A	175	LEU	0	0.001	0.008	35.339	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	176	PHE	0	-0.013	-0.013	34.206	-0.009	-0.009	0.000	0.000	0.000	0.000
138	A	177	LYS	1	0.825	0.890	33.448	0.122	0.122	0.000	0.000	0.000	0.000
139	A	178	ALA	0	-0.006	0.008	32.157	-0.009	-0.009	0.000	0.000	0.000	0.000
140	A	179	VAL	0	0.067	0.021	29.896	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	180	GLU	-1	-0.787	-0.851	28.800	-0.166	-0.166	0.000	0.000	0.000	0.000
142	A	181	ASN	0	-0.047	-0.047	27.700	-0.022	-0.022	0.000	0.000	0.000	0.000
143	A	182	LEU	0	-0.001	0.010	25.212	-0.012	-0.012	0.000	0.000	0.000	0.000
144	A	183	SER	0	0.000	-0.023	24.512	-0.027	-0.027	0.000	0.000	0.000	0.000
145	A	184	LYS	1	0.802	0.894	23.042	0.158	0.158	0.000	0.000	0.000	0.000
146	A	185	ALA	0	0.028	0.015	21.703	-0.024	-0.024	0.000	0.000	0.000	0.000
147	A	186	ALA	0	0.048	0.044	19.849	-0.022	-0.022	0.000	0.000	0.000	0.000
148	A	187	GLN	0	-0.065	-0.057	18.435	-0.061	-0.061	0.000	0.000	0.000	0.000
149	A	188	ASP	-1	-0.941	-0.979	17.574	-0.402	-0.402	0.000	0.000	0.000	0.000
150	A	189	THR	0	0.036	0.009	15.255	-0.062	-0.062	0.000	0.000	0.000	0.000
151	A	190	LEU	0	-0.014	-0.001	13.586	-0.086	-0.086	0.000	0.000	0.000	0.000
152	A	191	LYS	1	0.864	0.919	12.678	0.452	0.452	0.000	0.000	0.000	0.000
153	A	192	ASN	0	0.010	0.026	11.323	-0.122	-0.122	0.000	0.000	0.000	0.000
154	A	193	ALA	0	0.077	0.042	8.704	-0.180	-0.180	0.000	0.000	0.000	0.000
155	A	194	VAL	0	-0.055	-0.030	7.883	-0.262	-0.262	0.000	0.000	0.000	0.000
156	A	195	LYS	1	0.976	0.976	8.498	0.404	0.404	0.000	0.000	0.000	0.000
157	A	196	GLU	-1	-0.918	-0.919	5.658	-1.131	-1.131	0.000	0.000	0.000	0.000
158	A	197	LEU	0	0.010	0.001	3.966	-0.969	-0.619	0.001	-0.047	-0.304	0.000
159	A	198	THR	0	-0.067	-0.035	3.631	-1.525	-1.005	0.009	-0.190	-0.339	-0.001
160	A	199	SER	0	-0.020	-0.007	4.478	0.756	0.810	-0.001	-0.011	-0.041	0.000
161	A	200	PRO	0	-0.008	-0.008	3.076	-2.533	-1.216	0.132	-0.501	-0.948	-0.005
162	A	201	ILE	0	0.017	0.017	2.045	-0.846	-2.644	11.049	-3.739	-5.512	-0.002
163	A	202	VAL	0	-0.036	-0.018	3.638	-0.238	-0.074	0.019	0.015	-0.198	0.000
164	A	203	ALA	0	0.026	0.029	6.663	-0.318	-0.318	0.000	0.000	0.000	0.000

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