FMO DATABASE

FMODB ID: 8N26Y

Calculation Name: 3ILC-A-Xray372

Preferred Name: Bcl-2-like protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3ILC

Chain ID: A

ChEMBL ID: CHEMBL3309112

UniProt ID: Q64373

Base Structure: X-ray

Registration Date: 2023-09-26

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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1423695.203017
FMO2-HF: Nuclear repulsion	1365763.991374
FMO2-HF: Total energy	-57931.211643
FMO2-MP2: Total energy	-58100.244712

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:0:HIS)

Summations of interaction energy for fragment #1(A:0:HIS)

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.
-21.015	-16.182	11.336	-5.597	-10.573	0.023

Interaction energy analysis for fragmet #1(A:0:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.089 / q_NPA : 0.047

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	2	SER	0	-0.005	-0.026	2.066	-15.665	-13.740	10.089	-4.392	-7.623	0.023
4	A	3	GLN	0	-0.053	-0.024	2.287	-4.864	-2.621	1.242	-0.978	-2.507	0.000
5	A	4	SER	0	0.016	-0.010	3.798	-0.737	-0.072	0.005	-0.227	-0.443	0.000
6	A	5	ASN	0	0.001	-0.023	5.910	-0.203	-0.203	0.000	0.000	0.000	0.000
7	A	6	ARG	1	0.898	0.957	6.877	0.019	0.019	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.832	-0.913	7.578	0.005	0.005	0.000	0.000	0.000	0.000
9	A	8	LEU	0	0.026	0.013	9.653	-0.032	-0.032	0.000	0.000	0.000	0.000
10	A	9	VAL	0	-0.044	-0.011	11.554	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	10	VAL	0	-0.010	-0.006	12.376	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	11	ASP	-1	-0.859	-0.894	13.602	0.108	0.108	0.000	0.000	0.000	0.000
13	A	12	PHE	0	0.042	0.020	15.308	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	13	LEU	0	0.008	-0.008	16.573	-0.010	-0.010	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.035	-0.035	17.405	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	15	TYR	0	-0.071	-0.057	19.448	0.003	0.003	0.000	0.000	0.000	0.000
17	A	16	LYS	1	0.804	0.885	21.351	0.011	0.011	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.017	-0.020	21.579	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.015	-0.004	23.961	0.004	0.004	0.000	0.000	0.000	0.000
20	A	19	GLN	0	-0.035	-0.013	25.365	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	20	LYS	1	0.778	0.878	27.263	0.025	0.025	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.010	0.025	28.926	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	22	TYR	0	-0.083	-0.066	27.002	0.000	0.000	0.000	0.000	0.000	0.000
24	A	23	SER	0	0.012	-0.001	26.255	0.011	0.011	0.000	0.000	0.000	0.000
25	A	24	TRP	0	0.062	0.030	20.705	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.014	-0.020	21.011	0.003	0.003	0.000	0.000	0.000	0.000
27	A	26	GLN	0	-0.060	-0.026	19.879	0.013	0.013	0.000	0.000	0.000	0.000
28	A	27	PHE	0	-0.033	-0.020	16.108	-0.034	-0.034	0.000	0.000	0.000	0.000
29	A	28	SER	0	0.001	0.012	15.680	0.043	0.043	0.000	0.000	0.000	0.000
30	A	82	PRO	0	0.071	0.016	11.449	0.015	0.015	0.000	0.000	0.000	0.000
31	A	83	MET	0	-0.007	0.010	8.576	-0.086	-0.086	0.000	0.000	0.000	0.000
32	A	84	ALA	0	0.007	0.003	11.103	-0.034	-0.034	0.000	0.000	0.000	0.000
33	A	85	ALA	0	0.038	0.022	14.508	-0.031	-0.031	0.000	0.000	0.000	0.000
34	A	86	VAL	0	0.014	0.013	11.973	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	87	LYS	1	0.825	0.903	10.913	-0.196	-0.196	0.000	0.000	0.000	0.000
36	A	88	GLN	0	-0.041	-0.029	15.348	-0.028	-0.028	0.000	0.000	0.000	0.000
37	A	89	ALA	0	0.075	0.034	18.443	-0.022	-0.022	0.000	0.000	0.000	0.000
38	A	90	LEU	0	-0.017	-0.005	15.355	-0.024	-0.024	0.000	0.000	0.000	0.000
39	A	91	ARG	1	0.776	0.863	17.100	-0.137	-0.137	0.000	0.000	0.000	0.000
40	A	92	GLU	-1	-0.832	-0.894	20.754	0.091	0.091	0.000	0.000	0.000	0.000
41	A	93	ALA	0	0.008	0.009	21.698	-0.014	-0.014	0.000	0.000	0.000	0.000
42	A	94	GLY	0	-0.011	-0.012	22.528	-0.017	-0.017	0.000	0.000	0.000	0.000
43	A	95	ASP	-1	-0.759	-0.850	23.827	0.011	0.011	0.000	0.000	0.000	0.000
44	A	96	GLU	-1	-0.793	-0.847	26.644	0.005	0.005	0.000	0.000	0.000	0.000
45	A	97	PHE	0	0.020	0.005	25.986	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	98	GLU	-1	-0.808	-0.883	25.569	-0.040	-0.040	0.000	0.000	0.000	0.000
47	A	99	LEU	0	-0.034	-0.015	29.453	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	100	ARG	1	0.766	0.841	28.723	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	101	ALA	0	-0.033	-0.023	29.754	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	102	ARG	1	0.893	0.965	31.751	0.018	0.018	0.000	0.000	0.000	0.000
51	A	103	ARG	1	0.862	0.919	29.362	0.090	0.090	0.000	0.000	0.000	0.000
52	A	104	ALA	0	0.018	0.005	29.962	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	105	PHE	0	0.010	-0.011	25.247	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	106	SER	0	0.050	0.033	29.639	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	107	ASP	-1	-0.833	-0.880	30.637	-0.119	-0.119	0.000	0.000	0.000	0.000
56	A	108	LEU	0	0.077	0.045	24.479	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	109	THR	0	-0.023	-0.021	27.291	-0.017	-0.017	0.000	0.000	0.000	0.000
58	A	110	SER	0	-0.041	-0.018	29.042	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	111	GLN	0	-0.043	-0.038	28.824	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	112	LEU	0	-0.045	-0.022	23.055	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	113	HIS	1	0.820	0.907	27.490	0.194	0.194	0.000	0.000	0.000	0.000
62	A	114	ILE	0	-0.010	0.014	23.138	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	115	THR	0	0.087	0.028	27.256	0.014	0.014	0.000	0.000	0.000	0.000
64	A	116	PRO	0	0.050	0.004	26.249	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	117	GLY	0	0.007	0.019	26.152	-0.017	-0.017	0.000	0.000	0.000	0.000
66	A	118	THR	0	-0.026	0.004	23.737	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	119	ALA	0	0.048	0.011	21.509	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	120	TYR	0	0.035	0.010	13.816	0.053	0.053	0.000	0.000	0.000	0.000
69	A	121	GLN	0	0.051	0.020	18.782	0.007	0.007	0.000	0.000	0.000	0.000
70	A	122	SER	0	0.018	0.011	20.476	0.016	0.016	0.000	0.000	0.000	0.000
71	A	123	PHE	0	0.031	0.008	16.645	0.030	0.030	0.000	0.000	0.000	0.000
72	A	124	GLU	-1	-0.854	-0.898	16.470	-0.580	-0.580	0.000	0.000	0.000	0.000
73	A	125	GLN	0	-0.023	-0.021	19.182	0.030	0.030	0.000	0.000	0.000	0.000
74	A	126	VAL	0	-0.004	0.002	22.618	0.024	0.024	0.000	0.000	0.000	0.000
75	A	127	VAL	0	0.017	0.003	17.913	0.032	0.032	0.000	0.000	0.000	0.000
76	A	128	ASN	0	0.003	0.007	19.020	0.009	0.009	0.000	0.000	0.000	0.000
77	A	129	GLU	-1	-0.832	-0.890	21.312	-0.180	-0.180	0.000	0.000	0.000	0.000
78	A	130	LEU	0	-0.086	-0.038	21.098	0.025	0.025	0.000	0.000	0.000	0.000
79	A	131	PHE	0	-0.009	-0.027	17.933	0.022	0.022	0.000	0.000	0.000	0.000
80	A	132	ARG	1	0.876	0.951	21.559	0.161	0.161	0.000	0.000	0.000	0.000
81	A	133	ASP	-1	-0.856	-0.907	24.307	-0.140	-0.140	0.000	0.000	0.000	0.000
82	A	134	GLY	0	0.012	0.009	20.873	0.021	0.021	0.000	0.000	0.000	0.000
83	A	135	VAL	0	-0.013	-0.002	15.671	0.008	0.008	0.000	0.000	0.000	0.000
84	A	136	ASN	0	0.011	0.003	19.036	0.029	0.029	0.000	0.000	0.000	0.000
85	A	137	TRP	0	0.112	0.048	14.598	-0.045	-0.045	0.000	0.000	0.000	0.000
86	A	138	GLY	0	0.035	0.032	19.633	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	139	ARG	1	0.768	0.867	20.611	0.117	0.117	0.000	0.000	0.000	0.000
88	A	140	ILE	0	0.018	0.019	15.122	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	141	VAL	0	0.019	0.009	18.048	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	142	ALA	0	-0.022	-0.003	20.578	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	143	PHE	0	-0.008	-0.008	14.351	-0.024	-0.024	0.000	0.000	0.000	0.000
92	A	144	PHE	0	0.004	-0.002	13.378	-0.023	-0.023	0.000	0.000	0.000	0.000
93	A	145	SER	0	-0.018	-0.022	19.229	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	146	PHE	0	-0.028	-0.009	21.304	-0.007	-0.007	0.000	0.000	0.000	0.000
95	A	147	GLY	0	0.035	-0.005	20.003	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	148	GLY	0	0.041	0.006	21.070	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	149	ALA	0	0.005	0.005	22.385	0.002	0.002	0.000	0.000	0.000	0.000
98	A	150	LEU	0	-0.009	0.001	22.226	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	151	CYS	0	-0.088	-0.032	21.131	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	152	VAL	0	0.035	0.012	23.875	0.003	0.003	0.000	0.000	0.000	0.000
101	A	153	GLU	-1	-0.806	-0.899	27.067	-0.147	-0.147	0.000	0.000	0.000	0.000
102	A	154	SER	0	-0.060	-0.056	25.718	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	155	VAL	0	-0.039	-0.018	26.354	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	156	ASP	-1	-0.822	-0.877	28.921	-0.074	-0.074	0.000	0.000	0.000	0.000
105	A	157	LYS	1	0.740	0.861	29.198	0.162	0.162	0.000	0.000	0.000	0.000
106	A	158	GLU	-1	-0.855	-0.918	31.544	-0.094	-0.094	0.000	0.000	0.000	0.000
107	A	159	MET	0	-0.085	-0.017	28.424	-0.015	-0.015	0.000	0.000	0.000	0.000
108	A	160	GLN	0	0.034	0.002	26.444	-0.016	-0.016	0.000	0.000	0.000	0.000
109	A	161	VAL	0	-0.019	-0.013	24.233	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	162	LEU	0	-0.032	-0.019	22.786	-0.030	-0.030	0.000	0.000	0.000	0.000
111	A	163	VAL	0	0.014	0.029	20.376	-0.028	-0.028	0.000	0.000	0.000	0.000
112	A	164	SER	0	0.040	0.011	17.871	-0.012	-0.012	0.000	0.000	0.000	0.000
113	A	165	ARG	1	0.840	0.919	16.949	0.278	0.278	0.000	0.000	0.000	0.000
114	A	166	ILE	0	0.033	0.014	17.344	-0.070	-0.070	0.000	0.000	0.000	0.000
115	A	167	ALA	0	0.070	0.032	14.954	-0.032	-0.032	0.000	0.000	0.000	0.000
116	A	168	SER	0	-0.042	-0.024	13.068	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	169	TRP	0	-0.033	-0.011	12.749	-0.116	-0.116	0.000	0.000	0.000	0.000
118	A	170	MET	0	0.011	0.040	14.114	-0.071	-0.071	0.000	0.000	0.000	0.000
119	A	171	ALA	0	0.031	0.019	9.705	0.003	0.003	0.000	0.000	0.000	0.000
120	A	172	THR	0	-0.065	-0.033	9.383	-0.198	-0.198	0.000	0.000	0.000	0.000
121	A	173	TYR	0	0.016	-0.027	10.247	-0.167	-0.167	0.000	0.000	0.000	0.000
122	A	174	LEU	0	-0.021	0.005	9.626	-0.030	-0.030	0.000	0.000	0.000	0.000
123	A	175	ASN	0	-0.005	-0.013	5.405	0.541	0.541	0.000	0.000	0.000	0.000
124	A	176	ASP	-1	-0.882	-0.915	7.561	-1.508	-1.508	0.000	0.000	0.000	0.000
125	A	177	HIS	1	0.765	0.847	9.887	0.891	0.891	0.000	0.000	0.000	0.000
126	A	178	LEU	0	-0.039	-0.004	11.333	0.111	0.111	0.000	0.000	0.000	0.000
127	A	179	GLU	-1	-0.776	-0.873	5.866	0.956	0.956	0.000	0.000	0.000	0.000
128	A	180	PRO	0	0.005	-0.003	8.863	0.196	0.196	0.000	0.000	0.000	0.000
129	A	181	TRP	0	0.048	0.026	10.421	0.130	0.130	0.000	0.000	0.000	0.000
130	A	182	ILE	0	0.006	0.004	10.710	0.054	0.054	0.000	0.000	0.000	0.000
131	A	183	GLN	0	-0.070	-0.052	8.063	0.135	0.135	0.000	0.000	0.000	0.000
132	A	184	GLU	-1	-0.945	-0.958	11.333	0.019	0.019	0.000	0.000	0.000	0.000
133	A	185	ASN	0	-0.119	-0.064	14.512	0.000	0.000	0.000	0.000	0.000	0.000
134	A	186	GLY	0	0.053	0.023	15.222	-0.007	-0.007	0.000	0.000	0.000	0.000
135	A	187	GLY	0	0.007	0.006	12.039	0.085	0.085	0.000	0.000	0.000	0.000
136	A	188	TRP	0	-0.030	-0.058	9.793	-0.190	-0.190	0.000	0.000	0.000	0.000
137	A	189	ASP	-1	-0.906	-0.946	12.468	0.601	0.601	0.000	0.000	0.000	0.000
138	A	190	THR	0	0.028	0.017	14.878	-0.052	-0.052	0.000	0.000	0.000	0.000
139	A	191	PHE	0	-0.056	-0.018	16.250	-0.054	-0.054	0.000	0.000	0.000	0.000
140	A	192	VAL	0	-0.009	-0.020	15.967	-0.037	-0.037	0.000	0.000	0.000	0.000
141	A	193	ASP	-1	-0.886	-0.942	18.567	0.264	0.264	0.000	0.000	0.000	0.000
142	A	194	LEU	0	-0.097	-0.046	21.062	-0.029	-0.029	0.000	0.000	0.000	0.000
143	A	195	TYR	0	-0.065	-0.034	21.021	-0.034	-0.034	0.000	0.000	0.000	0.000
144	A	196	GLY	0	-0.041	-0.001	20.994	-0.009	-0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:HIS)