FMO DATABASE

FMODB ID: QY21Y

Calculation Name: 2BK0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BK0

Chain ID: A

ChEMBL ID:

UniProt ID: P49372

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	153
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1311477.537199
FMO2-HF: Nuclear repulsion	1255438.058983
FMO2-HF: Total energy	-56039.478216
FMO2-MP2: Total energy	-56205.478468

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:GLY)

Summations of interaction energy for fragment #1(A:2: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.
-3.083	-13.47	27.902	-10.493	-7.02	-0.063

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : -0.007

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	4	GLN	0	-0.014	-0.002	3.803	0.365	1.852	-0.015	-0.764	-0.708	0.002
4	A	5	THR	0	-0.002	-0.008	6.726	0.034	0.034	0.000	0.000	0.000	0.000
5	A	6	HIS	0	-0.004	0.002	10.416	0.009	0.009	0.000	0.000	0.000	0.000
6	A	7	VAL	0	-0.014	-0.009	13.606	0.006	0.006	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.027	-0.002	17.129	0.015	0.015	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.867	-0.925	20.426	-0.233	-0.233	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.022	-0.004	23.842	0.009	0.009	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.002	0.007	27.058	0.007	0.007	0.000	0.000	0.000	0.000
11	A	12	SER	0	-0.049	-0.050	30.564	0.001	0.001	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.026	-0.010	33.376	0.006	0.006	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.010	0.000	35.192	0.009	0.009	0.000	0.000	0.000	0.000
14	A	15	SER	0	0.072	0.039	35.140	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.071	0.018	32.111	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.931	-0.960	32.903	-0.101	-0.101	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.886	0.949	34.915	0.104	0.104	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.008	0.003	29.975	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	20	PHE	0	0.024	0.010	27.188	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	21	GLN	0	-0.035	-0.033	30.862	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	22	GLY	0	-0.007	-0.003	32.942	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	23	PHE	0	-0.014	-0.022	25.500	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.064	-0.021	26.555	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	25	ILE	0	-0.064	-0.022	28.654	0.002	0.002	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.829	-0.902	31.810	-0.116	-0.116	0.000	0.000	0.000	0.000
26	A	27	VAL	0	0.029	0.016	27.726	0.003	0.003	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.779	-0.889	29.194	-0.192	-0.192	0.000	0.000	0.000	0.000
28	A	29	THR	0	-0.058	-0.022	31.768	0.010	0.010	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.057	-0.038	33.365	0.006	0.006	0.000	0.000	0.000	0.000
30	A	31	LEU	0	0.046	0.023	27.440	0.002	0.002	0.000	0.000	0.000	0.000
31	A	32	PRO	0	-0.015	-0.001	32.140	0.003	0.003	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.857	0.931	34.635	0.120	0.120	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.042	-0.005	34.077	0.005	0.005	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.018	-0.021	31.801	0.000	0.000	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.009	0.006	32.491	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	37	GLY	0	-0.009	-0.004	33.227	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.027	-0.004	28.461	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.036	-0.022	27.779	-0.018	-0.018	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.826	0.916	28.990	0.178	0.178	0.000	0.000	0.000	0.000
40	A	41	SER	0	-0.011	-0.026	29.355	0.017	0.017	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.001	-0.012	27.584	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.877	-0.905	28.187	-0.132	-0.132	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.013	-0.021	27.576	-0.018	-0.018	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.808	0.922	27.022	0.168	0.168	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.043	0.007	27.315	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.932	-0.959	29.473	-0.117	-0.117	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.036	0.010	29.208	0.002	0.002	0.000	0.000	0.000	0.000
48	A	49	GLY	0	-0.023	-0.004	27.670	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	50	PRO	0	-0.016	-0.019	24.116	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	51	GLY	0	-0.011	0.005	23.076	0.017	0.017	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.061	-0.027	24.022	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.016	-0.012	21.254	-0.026	-0.026	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.826	0.883	22.949	0.233	0.233	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.018	0.012	22.981	-0.027	-0.027	0.000	0.000	0.000	0.000
55	A	56	ILE	0	0.012	0.001	22.706	0.024	0.024	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.000	0.004	24.029	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.003	-0.009	22.101	0.011	0.011	0.000	0.000	0.000	0.000
58	A	59	PRO	0	-0.014	-0.012	26.393	0.013	0.013	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.823	-0.900	28.065	-0.174	-0.174	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.024	0.001	28.682	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	62	GLY	0	-0.001	0.001	26.166	0.003	0.003	0.000	0.000	0.000	0.000
62	A	63	PRO	0	-0.056	-0.035	21.351	0.004	0.004	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.004	0.015	18.326	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.035	-0.018	21.308	0.035	0.035	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.027	-0.038	20.963	0.035	0.035	0.000	0.000	0.000	0.000
66	A	67	MET	0	-0.052	-0.017	18.655	-0.044	-0.044	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.030	-0.032	18.440	0.051	0.051	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.022	-0.007	17.995	-0.057	-0.057	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.886	0.927	14.948	0.393	0.393	0.000	0.000	0.000	0.000
70	A	71	ILE	0	0.022	0.017	19.528	-0.038	-0.038	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.820	-0.886	17.440	-0.344	-0.344	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.011	0.000	20.680	0.033	0.033	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.005	-0.001	23.504	-0.018	-0.018	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.008	-0.001	26.553	0.020	0.020	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.994	0.985	28.641	0.105	0.105	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.903	-0.952	31.819	-0.092	-0.092	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.048	-0.017	28.183	0.003	0.003	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.033	-0.003	29.015	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.029	-0.014	23.312	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	81	PHE	0	-0.011	-0.015	23.598	0.012	0.012	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.829	-0.883	19.051	-0.299	-0.299	0.000	0.000	0.000	0.000
82	A	83	TYR	0	0.015	0.008	18.411	0.040	0.040	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.014	-0.004	14.095	-0.088	-0.088	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.053	-0.022	13.776	0.084	0.084	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.019	-0.029	13.175	-0.110	-0.110	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.833	-0.903	14.767	-0.313	-0.313	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.029	0.025	16.373	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.778	-0.882	16.053	-0.428	-0.428	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.052	0.020	14.400	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.067	-0.022	10.932	-0.088	-0.088	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.041	-0.018	11.441	-0.129	-0.129	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.005	0.012	12.351	0.075	0.075	0.000	0.000	0.000	0.000
93	A	94	PHE	0	0.002	-0.024	6.729	0.149	0.149	0.000	0.000	0.000	0.000
94	A	95	ILE	0	-0.014	0.002	6.605	-0.554	-0.554	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.977	-0.990	6.541	0.017	0.017	0.000	0.000	0.000	0.000
96	A	97	SER	0	-0.006	-0.002	7.838	0.354	0.354	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.027	-0.006	8.657	-0.402	-0.402	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.782	-0.852	10.773	-0.462	-0.462	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.034	-0.028	12.633	-0.085	-0.085	0.000	0.000	0.000	0.000
100	A	101	HIS	1	0.779	0.847	14.438	0.503	0.503	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.012	-0.004	18.554	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	103	VAL	0	0.002	-0.003	21.848	0.023	0.023	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.010	-0.007	24.450	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	105	VAL	0	-0.007	0.002	27.350	0.010	0.010	0.000	0.000	0.000	0.000
105	A	106	PRO	0	0.008	-0.007	30.120	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.024	-0.029	33.060	0.000	0.000	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.022	-0.020	35.391	0.004	0.004	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.894	-0.931	37.121	-0.102	-0.102	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.019	0.000	38.896	0.002	0.002	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.013	0.017	36.274	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.054	-0.055	31.649	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	113	ILE	0	0.007	-0.002	26.942	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	114	CYS	0	-0.040	-0.013	25.592	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.900	0.945	19.821	0.250	0.250	0.000	0.000	0.000	0.000
115	A	116	THR	0	0.017	0.001	19.526	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.033	-0.030	14.549	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	118	ALA	0	0.037	0.026	13.442	0.018	0.018	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.028	-0.028	8.374	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	120	PHE	0	0.002	0.004	7.503	0.164	0.164	0.000	0.000	0.000	0.000
120	A	121	HIS	0	0.021	0.002	4.575	-1.516	-1.545	-0.001	-0.020	0.052	0.000
121	A	122	THR	0	-0.053	-0.040	2.868	-0.831	0.362	0.426	-0.716	-0.904	-0.005
122	A	123	LYS	1	0.936	0.971	2.240	-2.274	-1.571	2.604	-1.745	-1.561	-0.020
123	A	124	GLY	0	0.003	-0.004	3.670	-1.617	-0.879	0.040	-0.385	-0.393	0.000
124	A	125	ASP	-1	-0.883	-0.951	1.689	6.136	-8.625	24.846	-6.751	-3.333	-0.040
125	A	126	ALA	0	-0.063	-0.016	3.552	-0.349	-0.126	0.003	-0.076	-0.151	0.000
126	A	127	VAL	0	0.023	0.024	4.142	-1.414	-1.355	-0.001	-0.036	-0.022	0.000
127	A	128	VAL	0	-0.022	-0.015	6.864	0.296	0.296	0.000	0.000	0.000	0.000
128	A	129	PRO	0	-0.004	0.004	9.668	0.120	0.120	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.876	-0.940	12.937	-0.438	-0.438	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.888	-0.957	15.392	-0.435	-0.435	0.000	0.000	0.000	0.000
131	A	132	ASN	0	-0.057	-0.038	14.034	-0.015	-0.015	0.000	0.000	0.000	0.000
132	A	133	ILE	0	0.036	0.024	11.172	0.025	0.025	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.812	0.891	15.607	0.352	0.352	0.000	0.000	0.000	0.000
134	A	135	TYR	0	0.006	-0.002	18.952	0.057	0.057	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.044	0.021	17.238	0.040	0.040	0.000	0.000	0.000	0.000
136	A	137	ASN	0	0.041	0.030	18.694	0.012	0.012	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.833	-0.884	21.075	-0.245	-0.245	0.000	0.000	0.000	0.000
138	A	139	GLN	0	-0.022	-0.008	22.220	0.037	0.037	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.029	-0.037	19.588	0.036	0.036	0.000	0.000	0.000	0.000
140	A	141	THR	0	-0.030	-0.022	23.312	0.028	0.028	0.000	0.000	0.000	0.000
141	A	142	ALA	0	-0.025	-0.010	26.016	0.022	0.022	0.000	0.000	0.000	0.000
142	A	143	LEU	0	0.021	0.016	25.334	0.020	0.020	0.000	0.000	0.000	0.000
143	A	144	PHE	0	0.032	0.009	26.798	0.016	0.016	0.000	0.000	0.000	0.000
144	A	145	LYS	1	0.972	0.974	28.655	0.194	0.194	0.000	0.000	0.000	0.000
145	A	146	ALA	0	-0.015	0.009	31.182	0.014	0.014	0.000	0.000	0.000	0.000
146	A	147	LEU	0	0.013	-0.003	29.203	0.013	0.013	0.000	0.000	0.000	0.000
147	A	148	GLU	-1	-0.822	-0.881	32.434	-0.146	-0.146	0.000	0.000	0.000	0.000
148	A	149	ALA	0	-0.011	-0.002	34.226	0.011	0.011	0.000	0.000	0.000	0.000
149	A	150	TYR	0	0.026	0.010	36.335	0.009	0.009	0.000	0.000	0.000	0.000
150	A	151	LEU	0	-0.013	-0.011	33.486	0.009	0.009	0.000	0.000	0.000	0.000
151	A	152	ILE	0	-0.034	-0.017	37.713	0.008	0.008	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.050	-0.009	40.230	0.006	0.006	0.000	0.000	0.000	0.000
153	A	154	ASN	0	-0.043	-0.010	41.031	0.008	0.008	0.000	0.000	0.000	0.000

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