FMO DATABASE

FMODB ID: 63J9Z

Calculation Name: 2QZB-A-Xray316

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QZB

Chain ID: A

ChEMBL ID:

UniProt ID: P76537

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	153
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1390021.261919
FMO2-HF: Nuclear repulsion	1330483.667691
FMO2-HF: Total energy	-59537.594228
FMO2-MP2: Total energy	-59709.167657

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:38:ACE )

Summations of interaction energy for fragment #1(A:38: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.
-2.798	-1.683	-0.003	-0.479	-0.633	0

Interaction energy analysis for fragmet #1(A:38:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.024 / 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].
3	A	40	LYS	1	0.939	0.971	3.863	0.844	1.686	-0.005	-0.397	-0.439
4	A	41	VAL	0	-0.014	0.003	6.942	-0.098	-0.098	0.000	0.000	0.000
5	A	42	SER	0	0.060	0.016	10.326	0.087	0.087	0.000	0.000	0.000
6	A	43	GLU	-1	-0.761	-0.877	12.115	-0.168	-0.168	0.000	0.000	0.000
7	A	44	GLN	0	-0.022	0.010	12.466	-0.023	-0.023	0.000	0.000	0.000
8	A	45	GLY	0	0.021	0.016	13.270	0.009	0.009	0.000	0.000	0.000
9	A	46	VAL	0	-0.016	-0.011	9.171	0.007	0.007	0.000	0.000	0.000
10	A	47	GLY	0	0.016	0.016	6.804	-0.103	-0.103	0.000	0.000	0.000
11	A	48	GLU	-1	-0.858	-0.919	7.563	-0.695	-0.695	0.000	0.000	0.000
12	A	49	LEU	0	-0.096	-0.041	10.297	0.236	0.236	0.000	0.000	0.000
13	A	50	THR	0	0.073	0.028	12.829	0.039	0.039	0.000	0.000	0.000
14	A	51	ALA	0	-0.010	-0.009	15.424	0.034	0.034	0.000	0.000	0.000
15	A	52	SER	0	-0.014	-0.021	18.019	0.035	0.035	0.000	0.000	0.000
16	A	53	THR	0	0.008	0.024	15.240	0.017	0.017	0.000	0.000	0.000
17	A	54	PRO	0	0.041	0.015	18.217	0.019	0.019	0.000	0.000	0.000
18	A	55	LEU	0	-0.015	0.010	19.819	-0.023	-0.023	0.000	0.000	0.000
19	A	56	GLN	0	-0.038	-0.030	20.524	0.036	0.036	0.000	0.000	0.000
20	A	57	GLU	-1	-0.900	-0.939	19.784	-0.204	-0.204	0.000	0.000	0.000
21	A	58	GLN	0	0.070	0.010	18.588	-0.029	-0.029	0.000	0.000	0.000
22	A	59	ALA	0	-0.025	0.007	17.383	-0.019	-0.019	0.000	0.000	0.000
23	A	60	ILE	0	-0.006	-0.007	14.861	-0.044	-0.044	0.000	0.000	0.000
24	A	61	ALA	0	-0.026	-0.016	13.634	-0.075	-0.075	0.000	0.000	0.000
25	A	62	ASP	-1	-0.926	-0.961	13.049	-0.342	-0.342	0.000	0.000	0.000
26	A	63	ALA	0	-0.065	-0.029	11.358	-0.043	-0.043	0.000	0.000	0.000
27	A	64	LEU	0	-0.109	-0.051	9.379	-0.210	-0.210	0.000	0.000	0.000
28	A	65	ASP	-1	-0.893	-0.935	3.915	-2.176	-1.903	0.002	-0.082	-0.194
29	A	66	GLY	0	0.011	-0.004	5.928	-0.235	-0.235	0.000	0.000	0.000
30	A	67	ASP	-1	-0.972	-0.965	8.174	-0.046	-0.046	0.000	0.000	0.000
31	A	68	TYR	0	-0.072	-0.057	8.461	0.009	0.009	0.000	0.000	0.000
32	A	69	ARG	1	0.906	0.950	13.277	0.168	0.168	0.000	0.000	0.000
33	A	70	LEU	0	0.018	0.020	16.282	-0.030	-0.030	0.000	0.000	0.000
34	A	71	ARG	1	0.894	0.960	18.452	0.166	0.166	0.000	0.000	0.000
35	A	72	SER	0	-0.018	-0.020	21.410	-0.013	-0.013	0.000	0.000	0.000
36	A	73	GLY	0	0.031	0.023	24.019	0.013	0.013	0.000	0.000	0.000
37	A	74	MET	0	-0.034	-0.022	26.791	-0.004	-0.004	0.000	0.000	0.000
38	A	75	LYS	1	0.961	0.991	25.904	0.143	0.143	0.000	0.000	0.000
39	A	76	THR	0	0.022	0.021	30.684	-0.002	-0.002	0.000	0.000	0.000
40	A	77	ALA	0	-0.013	-0.021	30.347	-0.003	-0.003	0.000	0.000	0.000
41	A	78	ASN	0	-0.023	-0.009	31.614	0.005	0.005	0.000	0.000	0.000
42	A	79	GLY	0	0.019	0.017	34.944	0.001	0.001	0.000	0.000	0.000
43	A	80	ASN	0	0.001	0.008	34.010	0.001	0.001	0.000	0.000	0.000
44	A	81	VAL	0	0.026	0.011	32.136	-0.001	-0.001	0.000	0.000	0.000
45	A	82	VAL	0	-0.050	-0.028	27.663	-0.003	-0.003	0.000	0.000	0.000
46	A	83	ARG	1	0.882	0.909	24.480	0.166	0.166	0.000	0.000	0.000
47	A	84	PHE	0	-0.035	-0.006	22.593	-0.003	-0.003	0.000	0.000	0.000
48	A	85	PHE	0	0.013	-0.010	19.250	0.013	0.013	0.000	0.000	0.000
49	A	86	GLU	-1	-0.856	-0.926	18.801	-0.165	-0.165	0.000	0.000	0.000
50	A	87	VAL	0	0.034	0.016	12.497	0.019	0.019	0.000	0.000	0.000
51	A	88	MET	0	-0.051	-0.019	15.872	0.012	0.012	0.000	0.000	0.000
52	A	89	LYS	1	0.940	0.954	11.337	0.108	0.108	0.000	0.000	0.000
53	A	90	GLY	0	-0.028	-0.016	14.912	0.029	0.029	0.000	0.000	0.000
54	A	91	ASP	-1	-0.931	-0.965	17.895	-0.082	-0.082	0.000	0.000	0.000
55	A	92	ASN	0	-0.022	-0.004	17.823	0.005	0.005	0.000	0.000	0.000
56	A	93	VAL	0	-0.011	-0.008	17.461	-0.023	-0.023	0.000	0.000	0.000
57	A	94	ALA	0	0.032	0.013	12.371	0.014	0.014	0.000	0.000	0.000
58	A	95	MET	0	0.018	0.002	9.745	-0.010	-0.010	0.000	0.000	0.000
59	A	96	VAL	0	-0.016	0.012	15.201	0.024	0.024	0.000	0.000	0.000
60	A	97	ILE	0	0.024	0.023	14.820	-0.007	-0.007	0.000	0.000	0.000
61	A	98	ASN	0	0.014	-0.024	18.637	0.047	0.047	0.000	0.000	0.000
62	A	99	GLY	0	0.120	0.036	21.061	-0.021	-0.021	0.000	0.000	0.000
63	A	100	ASH	0	-0.073	-0.059	23.483	0.016	0.016	0.000	0.000	0.000
64	A	101	GLN	0	0.034	0.034	26.901	-0.002	-0.002	0.000	0.000	0.000
65	A	102	GLY	0	-0.046	-0.017	26.193	0.004	0.004	0.000	0.000	0.000
66	A	103	THR	0	-0.042	0.006	22.201	-0.015	-0.015	0.000	0.000	0.000
67	A	104	ILE	0	0.038	0.033	16.414	0.021	0.021	0.000	0.000	0.000
68	A	105	SER	0	-0.053	-0.046	20.220	-0.001	-0.001	0.000	0.000	0.000
69	A	106	ARG	1	0.762	0.831	19.655	0.175	0.175	0.000	0.000	0.000
70	A	107	ILE	0	0.000	0.006	13.667	-0.005	-0.005	0.000	0.000	0.000
71	A	108	ASP	-1	-0.791	-0.850	16.768	-0.190	-0.190	0.000	0.000	0.000
72	A	109	VAL	0	0.017	-0.005	11.080	-0.019	-0.019	0.000	0.000	0.000
73	A	110	LEU	0	0.014	-0.022	14.322	0.049	0.049	0.000	0.000	0.000
74	A	111	ASP	-1	-0.782	-0.874	9.724	-0.294	-0.294	0.000	0.000	0.000
75	A	112	SER	0	-0.025	-0.029	11.252	-0.030	-0.030	0.000	0.000	0.000
76	A	113	ASP	-1	-0.944	-0.965	7.295	0.089	0.089	0.000	0.000	0.000
77	A	114	ILE	0	-0.039	-0.002	6.628	0.020	0.020	0.000	0.000	0.000
78	A	115	PRO	0	-0.074	-0.031	6.798	0.086	0.086	0.000	0.000	0.000
79	A	116	ALA	0	0.049	0.003	9.204	-0.165	-0.165	0.000	0.000	0.000
80	A	117	ASP	-1	-0.955	-0.985	9.717	-0.093	-0.093	0.000	0.000	0.000
81	A	118	THR	0	-0.004	-0.035	10.904	0.060	0.060	0.000	0.000	0.000
82	A	119	GLY	0	-0.053	-0.026	12.318	0.032	0.032	0.000	0.000	0.000
83	A	120	VAL	0	-0.028	0.005	13.288	0.024	0.024	0.000	0.000	0.000
84	A	121	LYS	1	0.970	0.990	12.325	-0.187	-0.187	0.000	0.000	0.000
85	A	122	ILE	0	0.048	0.025	13.652	0.014	0.014	0.000	0.000	0.000
86	A	123	GLY	0	-0.024	-0.020	15.681	0.029	0.029	0.000	0.000	0.000
87	A	124	THR	0	-0.051	-0.029	16.570	0.020	0.020	0.000	0.000	0.000
88	A	125	PRO	0	0.011	0.001	18.957	-0.016	-0.016	0.000	0.000	0.000
89	A	126	PHE	0	0.041	0.002	22.764	-0.001	-0.001	0.000	0.000	0.000
90	A	127	SER	0	-0.046	-0.025	24.751	0.002	0.002	0.000	0.000	0.000
91	A	128	ASP	-1	-0.897	-0.938	21.425	0.051	0.051	0.000	0.000	0.000
92	A	129	LEU	0	-0.081	-0.038	19.388	0.001	0.001	0.000	0.000	0.000
93	A	130	TYR	0	-0.024	-0.023	22.895	-0.004	-0.004	0.000	0.000	0.000
94	A	131	SER	0	-0.031	-0.014	26.871	0.002	0.002	0.000	0.000	0.000
95	A	132	LYS	1	0.925	0.957	30.174	0.014	0.014	0.000	0.000	0.000
96	A	133	ALA	0	0.087	0.033	30.066	-0.003	-0.003	0.000	0.000	0.000
97	A	134	PHE	0	-0.044	-0.035	30.992	-0.004	-0.004	0.000	0.000	0.000
98	A	135	GLY	0	0.018	0.025	32.245	0.001	0.001	0.000	0.000	0.000
99	A	136	ASN	0	-0.004	-0.011	27.171	-0.006	-0.006	0.000	0.000	0.000
100	A	150	CYS	0	-0.122	-0.037	23.826	0.003	0.003	0.000	0.000	0.000
101	A	138	GLN	0	-0.007	-0.024	28.718	0.008	0.008	0.000	0.000	0.000
102	A	139	LYS	1	0.870	0.960	29.005	0.042	0.042	0.000	0.000	0.000
103	A	140	ALA	0	0.005	0.006	26.485	-0.003	-0.003	0.000	0.000	0.000
104	A	141	ASP	-1	-0.815	-0.893	25.869	-0.114	-0.114	0.000	0.000	0.000
105	A	142	GLY	0	0.018	0.004	25.953	0.001	0.001	0.000	0.000	0.000
106	A	143	ASP	-1	-0.827	-0.888	22.749	-0.130	-0.130	0.000	0.000	0.000
107	A	144	ASP	-1	-0.930	-0.940	25.698	-0.063	-0.063	0.000	0.000	0.000
108	A	145	ASN	0	-0.034	-0.032	28.565	0.011	0.011	0.000	0.000	0.000
109	A	146	ARG	1	0.767	0.865	29.056	0.038	0.038	0.000	0.000	0.000
110	A	147	ALA	0	0.098	0.060	25.423	-0.004	-0.004	0.000	0.000	0.000
111	A	148	VAL	0	-0.065	-0.025	26.608	0.001	0.001	0.000	0.000	0.000
112	A	149	GLU	-1	-0.779	-0.890	23.420	-0.116	-0.116	0.000	0.000	0.000
113	A	151	LYS	1	0.976	0.998	22.647	0.051	0.051	0.000	0.000	0.000
114	A	152	ALA	0	0.006	0.016	18.785	0.014	0.014	0.000	0.000	0.000
115	A	153	GLU	-1	-0.919	-0.969	20.721	-0.033	-0.033	0.000	0.000	0.000
116	A	154	GLY	0	-0.004	-0.001	20.708	-0.001	-0.001	0.000	0.000	0.000
117	A	155	SER	0	-0.074	-0.048	18.119	-0.011	-0.011	0.000	0.000	0.000
118	A	156	GLN	0	-0.064	-0.041	20.436	-0.001	-0.001	0.000	0.000	0.000
119	A	157	HIS	1	0.826	0.923	18.019	0.173	0.173	0.000	0.000	0.000
120	A	158	ILE	0	0.034	0.031	14.277	-0.019	-0.019	0.000	0.000	0.000
121	A	159	SER	0	-0.047	-0.022	18.274	0.034	0.034	0.000	0.000	0.000
122	A	160	TYR	0	0.050	0.053	16.019	-0.023	-0.023	0.000	0.000	0.000
123	A	161	GLN	0	-0.004	-0.016	20.113	0.013	0.013	0.000	0.000	0.000
124	A	162	PHE	0	-0.005	0.009	21.250	0.002	0.002	0.000	0.000	0.000
125	A	163	SER	0	0.029	-0.014	23.648	-0.001	-0.001	0.000	0.000	0.000
126	A	164	GLY	0	0.033	-0.002	25.594	0.007	0.007	0.000	0.000	0.000
127	A	165	GLU	-1	-0.928	-0.957	28.229	-0.011	-0.011	0.000	0.000	0.000
128	A	166	TRP	0	-0.006	-0.011	31.670	-0.002	-0.002	0.000	0.000	0.000
129	A	167	ARG	1	0.895	0.953	34.055	0.012	0.012	0.000	0.000	0.000
130	A	168	GLY	0	0.008	0.012	37.250	-0.001	-0.001	0.000	0.000	0.000
131	A	169	PRO	0	0.023	-0.011	39.357	-0.001	-0.001	0.000	0.000	0.000
132	A	170	GLU	-1	-0.806	-0.884	36.698	-0.034	-0.034	0.000	0.000	0.000
133	A	171	GLY	0	-0.016	-0.007	36.724	-0.003	-0.003	0.000	0.000	0.000
134	A	172	LEU	0	-0.023	-0.018	37.198	-0.002	-0.002	0.000	0.000	0.000
135	A	173	MET	0	0.002	0.002	31.714	-0.002	-0.002	0.000	0.000	0.000
136	A	174	PRO	0	-0.009	0.010	32.327	0.003	0.003	0.000	0.000	0.000
137	A	175	SER	0	0.019	0.003	34.197	-0.001	-0.001	0.000	0.000	0.000
138	A	176	ASP	-1	-0.739	-0.894	33.138	-0.016	-0.016	0.000	0.000	0.000
139	A	177	ASP	-1	-0.944	-0.971	33.025	0.000	0.000	0.000	0.000	0.000
140	A	178	THR	0	-0.100	-0.041	32.465	0.003	0.003	0.000	0.000	0.000
141	A	179	LEU	0	0.007	-0.003	29.210	0.001	0.001	0.000	0.000	0.000
142	A	180	LYS	1	0.959	1.005	28.529	-0.007	-0.007	0.000	0.000	0.000
143	A	181	ASN	0	-0.019	-0.022	27.864	0.007	0.007	0.000	0.000	0.000
144	A	182	TRP	0	-0.055	-0.019	26.102	-0.002	-0.002	0.000	0.000	0.000
145	A	183	LYS	1	0.952	0.982	21.231	-0.011	-0.011	0.000	0.000	0.000
146	A	184	VAL	0	-0.019	0.015	17.063	-0.008	-0.008	0.000	0.000	0.000
147	A	185	SER	0	0.018	0.004	19.044	0.009	0.009	0.000	0.000	0.000
148	A	186	LYS	1	0.812	0.902	17.369	0.130	0.130	0.000	0.000	0.000
149	A	187	ILE	0	-0.005	0.011	12.800	0.030	0.030	0.000	0.000	0.000
150	A	188	ILE	0	-0.043	-0.012	16.118	-0.035	-0.035	0.000	0.000	0.000
151	A	189	TRP	0	0.010	-0.001	15.099	0.007	0.007	0.000	0.000	0.000
152	A	190	ARG	1	0.779	0.854	17.197	0.140	0.140	0.000	0.000	0.000
153	A	191	ARG	0	0.003	0.006	20.300	0.036	0.036	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:38:ACE )