FMO DATABASE

FMODB ID: 8J1QY

Calculation Name: 4UF3-A-Xray313

Preferred Name: Bcl-2-like protein 11

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 4UF3

Chain ID: A

ChEMBL ID: CHEMBL5777

UniProt ID: O43521

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	138
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1191094.727325
FMO2-HF: Nuclear repulsion	1135678.37123
FMO2-HF: Total energy	-55416.356094
FMO2-MP2: Total energy	-55578.512813

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:2:ACE )

Summations of interaction energy for fragment #1(A:2:ACE )

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.
0.502	1.364	-0.007	-0.408	-0.446	0

Interaction energy analysis for fragmet #1(A:2:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / 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	4	ALA	0	0.007	0.013	3.823	0.836	1.698	-0.007	-0.408	-0.446
4	A	5	ILE	0	0.049	0.026	5.528	0.104	0.104	0.000	0.000	0.000
5	A	6	GLU	-1	-0.919	-0.952	8.294	-0.337	-0.337	0.000	0.000	0.000
6	A	7	PHE	0	-0.007	-0.017	11.046	0.076	0.076	0.000	0.000	0.000
7	A	8	ASP	-1	-0.875	-0.942	10.308	-0.468	-0.468	0.000	0.000	0.000
8	A	9	GLU	-1	-0.856	-0.930	13.323	-0.051	-0.051	0.000	0.000	0.000
9	A	10	ILE	0	-0.010	0.001	15.994	0.020	0.020	0.000	0.000	0.000
10	A	11	VAL	0	0.030	0.012	16.261	0.019	0.019	0.000	0.000	0.000
11	A	12	LYS	1	0.873	0.922	14.441	0.131	0.131	0.000	0.000	0.000
12	A	13	LYS	1	0.934	0.971	19.290	0.060	0.060	0.000	0.000	0.000
13	A	14	LEU	0	0.010	-0.005	21.559	0.010	0.010	0.000	0.000	0.000
14	A	15	LEU	0	0.010	0.015	20.840	0.008	0.008	0.000	0.000	0.000
15	A	16	ASN	0	0.003	0.001	22.885	0.009	0.009	0.000	0.000	0.000
16	A	17	ILE	0	-0.008	0.009	25.622	0.008	0.008	0.000	0.000	0.000
17	A	18	TYR	0	0.022	0.014	26.670	0.004	0.004	0.000	0.000	0.000
18	A	19	ILE	0	0.048	0.011	27.225	0.005	0.005	0.000	0.000	0.000
19	A	20	ASN	0	-0.051	-0.043	28.910	0.009	0.009	0.000	0.000	0.000
20	A	21	ASP	-1	-0.931	-0.949	31.404	-0.047	-0.047	0.000	0.000	0.000
21	A	22	ILE	0	-0.006	0.001	31.591	0.003	0.003	0.000	0.000	0.000
22	A	23	CYS	0	-0.057	-0.030	32.714	0.002	0.002	0.000	0.000	0.000
23	A	24	THR	0	0.053	0.036	35.549	0.004	0.004	0.000	0.000	0.000
24	A	25	THR	0	-0.060	-0.037	36.745	0.003	0.003	0.000	0.000	0.000
25	A	26	GLY	0	-0.051	-0.032	38.030	0.002	0.002	0.000	0.000	0.000
26	A	27	GLU	-1	-0.915	-0.966	38.606	-0.034	-0.034	0.000	0.000	0.000
27	A	28	LYS	1	0.915	0.947	40.990	0.036	0.036	0.000	0.000	0.000
28	A	29	ARG	1	0.855	0.936	39.099	0.048	0.048	0.000	0.000	0.000
29	A	30	LEU	0	-0.038	-0.014	43.704	0.001	0.001	0.000	0.000	0.000
30	A	31	LEU	0	0.023	0.046	46.118	0.002	0.002	0.000	0.000	0.000
31	A	32	ASN	0	0.015	0.009	48.489	-0.001	-0.001	0.000	0.000	0.000
32	A	33	ASN	0	0.020	-0.028	51.615	-0.001	-0.001	0.000	0.000	0.000
33	A	34	TYR	0	0.031	0.028	53.437	0.000	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.784	-0.904	50.017	-0.023	-0.023	0.000	0.000	0.000
35	A	36	LYS	1	0.893	0.956	47.146	0.030	0.030	0.000	0.000	0.000
36	A	37	SER	0	-0.066	-0.032	50.189	0.000	0.000	0.000	0.000	0.000
37	A	38	ILE	0	0.057	0.028	51.972	0.001	0.001	0.000	0.000	0.000
38	A	39	LEU	0	0.014	0.000	44.527	0.000	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.875	-0.928	48.275	-0.023	-0.023	0.000	0.000	0.000
40	A	41	ARG	1	0.952	0.979	49.653	0.016	0.016	0.000	0.000	0.000
41	A	42	ILE	0	0.016	0.035	47.301	0.001	0.001	0.000	0.000	0.000
42	A	43	TYR	0	0.018	0.015	41.529	0.000	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.856	0.910	47.234	0.023	0.023	0.000	0.000	0.000
44	A	45	SER	0	-0.020	-0.024	49.962	0.001	0.001	0.000	0.000	0.000
45	A	46	CYS	0	-0.015	-0.013	46.883	0.001	0.001	0.000	0.000	0.000
46	A	47	GLU	-1	-0.871	-0.928	43.933	-0.019	-0.019	0.000	0.000	0.000
47	A	48	TYR	0	-0.056	-0.016	47.669	0.001	0.001	0.000	0.000	0.000
48	A	49	ILE	0	-0.010	-0.013	50.096	0.001	0.001	0.000	0.000	0.000
49	A	50	LYS	1	0.844	0.912	42.316	0.019	0.019	0.000	0.000	0.000
50	A	51	LYS	1	0.938	0.989	47.580	0.016	0.016	0.000	0.000	0.000
51	A	52	ASN	0	-0.086	-0.050	48.962	0.001	0.001	0.000	0.000	0.000
52	A	53	TYR	0	-0.036	0.003	50.817	0.001	0.001	0.000	0.000	0.000
53	A	54	GLU	-1	-0.910	-0.937	45.428	-0.010	-0.010	0.000	0.000	0.000
54	A	55	LEU	0	-0.023	-0.033	47.053	0.001	0.001	0.000	0.000	0.000
55	A	56	ASP	-1	-0.866	-0.943	48.712	-0.003	-0.003	0.000	0.000	0.000
56	A	57	PHE	0	0.044	0.002	45.741	0.001	0.001	0.000	0.000	0.000
57	A	58	ASN	0	-0.020	-0.002	43.268	0.001	0.001	0.000	0.000	0.000
58	A	59	SER	0	-0.019	-0.008	44.646	0.002	0.002	0.000	0.000	0.000
59	A	60	MET	0	-0.034	-0.008	47.062	0.001	0.001	0.000	0.000	0.000
60	A	61	TYR	0	0.002	-0.010	36.679	0.000	0.000	0.000	0.000	0.000
61	A	62	ASN	0	0.008	-0.010	41.764	0.001	0.001	0.000	0.000	0.000
62	A	63	GLN	0	-0.062	-0.017	42.540	0.001	0.001	0.000	0.000	0.000
63	A	64	ILE	0	-0.012	0.002	40.663	0.001	0.001	0.000	0.000	0.000
64	A	65	ASN	0	-0.040	-0.018	36.404	-0.001	-0.001	0.000	0.000	0.000
65	A	66	ILE	0	-0.010	0.015	37.451	0.001	0.001	0.000	0.000	0.000
66	A	67	ASN	0	-0.030	-0.049	34.065	-0.001	-0.001	0.000	0.000	0.000
67	A	68	ASP	-1	-0.952	-0.967	36.978	0.015	0.015	0.000	0.000	0.000
68	A	69	ILE	0	0.012	0.026	39.731	0.000	0.000	0.000	0.000	0.000
69	A	70	THR	0	-0.025	-0.009	38.770	0.000	0.000	0.000	0.000	0.000
70	A	71	THR	0	0.036	-0.005	36.895	-0.001	-0.001	0.000	0.000	0.000
71	A	72	SER	0	-0.005	-0.016	39.767	-0.002	-0.002	0.000	0.000	0.000
72	A	73	ASP	-1	-0.842	-0.885	42.991	0.007	0.007	0.000	0.000	0.000
73	A	74	ILE	0	0.013	0.002	39.107	-0.001	-0.001	0.000	0.000	0.000
74	A	75	LYS	1	0.885	0.950	42.151	0.003	0.003	0.000	0.000	0.000
75	A	76	SER	0	-0.019	-0.029	45.119	-0.001	-0.001	0.000	0.000	0.000
76	A	77	LYS	1	0.985	1.004	46.902	-0.003	-0.003	0.000	0.000	0.000
77	A	78	ILE	0	-0.023	-0.013	44.084	-0.001	-0.001	0.000	0.000	0.000
78	A	79	ILE	0	-0.037	-0.024	48.289	-0.001	-0.001	0.000	0.000	0.000
79	A	80	GLU	-1	-0.892	-0.954	50.420	0.001	0.001	0.000	0.000	0.000
80	A	81	ALA	0	-0.029	-0.011	52.581	0.000	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.001	-0.016	50.755	0.000	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.089	-0.023	53.889	0.000	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.017	-0.003	56.385	0.000	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.782	-0.859	57.937	-0.005	-0.005	0.000	0.000	0.000
85	A	86	SER	0	0.000	-0.002	57.301	-0.001	-0.001	0.000	0.000	0.000
86	A	87	ARG	1	0.830	0.875	58.659	0.004	0.004	0.000	0.000	0.000
87	A	88	PRO	0	0.060	0.030	56.916	0.000	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.025	0.010	55.721	0.000	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.035	0.029	54.793	0.000	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.833	0.946	52.748	0.009	0.009	0.000	0.000	0.000
91	A	92	LEU	0	0.011	0.013	50.905	0.000	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.019	0.019	50.569	-0.001	-0.001	0.000	0.000	0.000
93	A	94	THR	0	0.023	0.011	48.386	0.000	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.011	-0.010	45.673	0.000	0.000	0.000	0.000	0.000
95	A	96	SER	0	0.010	-0.023	45.722	-0.001	-0.001	0.000	0.000	0.000
96	A	97	PHE	0	0.004	0.017	44.828	-0.001	-0.001	0.000	0.000	0.000
97	A	98	ILE	0	0.010	-0.001	42.016	0.000	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.066	-0.030	41.393	-0.001	-0.001	0.000	0.000	0.000
99	A	100	LEU	0	0.039	0.008	40.771	-0.001	-0.001	0.000	0.000	0.000
100	A	101	ILE	0	-0.030	-0.014	38.278	0.000	0.000	0.000	0.000	0.000
101	A	102	ALA	0	-0.033	-0.028	36.904	0.000	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.908	-0.958	35.736	-0.021	-0.021	0.000	0.000	0.000
103	A	104	LYS	1	0.909	0.972	35.687	0.008	0.008	0.000	0.000	0.000
104	A	105	TRP	0	-0.051	-0.026	32.993	0.002	0.002	0.000	0.000	0.000
105	A	106	GLY	0	0.063	0.028	31.170	-0.002	-0.002	0.000	0.000	0.000
106	A	107	GLU	-1	-0.965	-0.979	26.207	-0.022	-0.022	0.000	0.000	0.000
107	A	108	LYS	1	0.857	0.948	26.867	0.003	0.003	0.000	0.000	0.000
108	A	109	ASN	0	0.019	0.000	27.594	-0.007	-0.007	0.000	0.000	0.000
109	A	110	ARG	1	1.094	1.042	29.207	0.041	0.041	0.000	0.000	0.000
110	A	111	ALA	0	-0.002	-0.010	31.100	0.002	0.002	0.000	0.000	0.000
111	A	112	LYS	1	0.944	0.970	29.691	-0.001	-0.001	0.000	0.000	0.000
112	A	113	ILE	0	0.010	0.028	33.798	0.002	0.002	0.000	0.000	0.000
113	A	114	MET	0	-0.029	-0.022	35.476	0.000	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.914	-0.955	35.024	-0.003	-0.003	0.000	0.000	0.000
115	A	116	ILE	0	-0.022	-0.007	38.384	0.002	0.002	0.000	0.000	0.000
116	A	117	LEU	0	0.004	0.000	40.604	0.000	0.000	0.000	0.000	0.000
117	A	118	SER	0	0.001	-0.021	40.596	0.000	0.000	0.000	0.000	0.000
118	A	119	ASN	0	-0.038	-0.006	42.633	0.002	0.002	0.000	0.000	0.000
119	A	120	GLU	-1	-0.809	-0.923	45.058	-0.005	-0.005	0.000	0.000	0.000
120	A	121	ILE	0	-0.025	-0.003	45.232	0.000	0.000	0.000	0.000	0.000
121	A	122	VAL	0	0.024	0.003	45.450	0.000	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.909	-0.947	47.678	-0.012	-0.012	0.000	0.000	0.000
123	A	124	LYS	1	0.917	0.976	50.415	0.006	0.006	0.000	0.000	0.000
124	A	125	ILE	0	-0.035	-0.034	48.457	0.000	0.000	0.000	0.000	0.000
125	A	126	SER	0	0.012	0.001	50.125	-0.001	-0.001	0.000	0.000	0.000
126	A	127	ASN	0	-0.050	-0.020	52.857	0.000	0.000	0.000	0.000	0.000
127	A	128	ASN	0	-0.053	-0.037	56.024	0.000	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.094	0.047	55.900	0.000	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.958	0.978	56.551	0.011	0.011	0.000	0.000	0.000
130	A	131	ASP	-1	-0.808	-0.903	59.546	-0.009	-0.009	0.000	0.000	0.000
131	A	132	PHE	0	-0.082	-0.038	51.756	0.000	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.002	-0.014	54.683	0.000	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.891	-0.944	57.045	-0.012	-0.012	0.000	0.000	0.000
134	A	135	PHE	0	-0.071	-0.038	56.788	0.000	0.000	0.000	0.000	0.000
135	A	136	ILE	0	0.002	0.001	53.654	0.000	0.000	0.000	0.000	0.000
136	A	137	ASP	-1	-0.947	-0.981	56.944	-0.016	-0.016	0.000	0.000	0.000
137	A	138	ARG	1	0.845	0.911	58.577	0.013	0.013	0.000	0.000	0.000
138	A	139	NME	0	0.003	0.030	60.390	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ACE )