FMO DATABASE

FMODB ID: 5JQLZ

Calculation Name: 2QTP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QTP

Chain ID: A

ChEMBL ID:

UniProt ID: Q5LV76

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	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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1264693.312016
FMO2-HF: Nuclear repulsion	1209219.33926
FMO2-HF: Total energy	-55473.972756
FMO2-MP2: Total energy	-55635.063082

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-217.569	-222.493	34.368	-16.288	-13.157	-0.176

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.825 / q_NPA : 0.873

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	5	ARG	1	0.702	0.815	3.866	29.706	30.930	-0.009	-0.491	-0.724	0.001
4	A	6	LYS	1	0.843	0.889	5.630	23.571	23.571	0.000	0.000	0.000	0.000
5	A	7	ILE	0	0.011	0.007	8.804	-0.762	-0.762	0.000	0.000	0.000	0.000
6	A	8	ALA	0	-0.048	-0.013	11.190	0.499	0.499	0.000	0.000	0.000	0.000
7	A	9	VAL	0	0.001	-0.015	14.876	-0.214	-0.214	0.000	0.000	0.000	0.000
8	A	10	PHE	0	-0.032	0.000	17.189	0.160	0.160	0.000	0.000	0.000	0.000
9	A	11	ILE	0	0.009	-0.008	21.217	-0.060	-0.060	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.925	-0.954	24.437	-9.979	-9.979	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.816	-0.909	27.744	-8.804	-8.804	0.000	0.000	0.000	0.000
12	A	14	THR	0	0.015	0.014	31.212	0.099	0.099	0.000	0.000	0.000	0.000
13	A	15	ARG	1	0.841	0.895	33.601	8.509	8.509	0.000	0.000	0.000	0.000
14	A	16	ILE	0	-0.015	-0.008	36.950	0.233	0.233	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.858	-0.931	36.201	-8.017	-8.017	0.000	0.000	0.000	0.000
16	A	18	DAL	0	-0.021	-0.018	39.167	0.171	0.171	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.021	0.002	41.792	0.152	0.152	0.000	0.000	0.000	0.000
18	A	20	ARG	1	0.857	0.938	39.623	7.310	7.310	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.915	-0.962	41.755	-6.790	-6.790	0.000	0.000	0.000	0.000
20	A	22	ILE	0	-0.091	-0.035	36.866	0.120	0.120	0.000	0.000	0.000	0.000
21	A	23	SER	0	-0.027	0.002	38.788	-0.165	-0.165	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.014	-0.010	36.170	0.184	0.184	0.000	0.000	0.000	0.000
23	A	25	PRO	0	0.001	-0.013	33.887	0.032	0.032	0.000	0.000	0.000	0.000
24	A	26	THR	0	0.059	0.049	32.920	-0.102	-0.102	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.754	0.854	28.541	9.260	9.260	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.852	0.927	25.446	9.837	9.837	0.000	0.000	0.000	0.000
27	A	29	ALA	0	-0.011	-0.005	21.750	-0.023	-0.023	0.000	0.000	0.000	0.000
28	A	30	VAL	0	0.012	0.006	17.989	-0.068	-0.068	0.000	0.000	0.000	0.000
29	A	31	ALA	0	-0.010	0.011	14.998	-0.143	-0.143	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.003	-0.012	12.690	-0.148	-0.148	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.022	0.008	7.735	-0.135	-0.135	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.025	-0.012	7.618	0.838	0.838	0.000	0.000	0.000	0.000
33	A	35	ILE	0	0.026	0.015	3.513	-2.750	-2.209	0.008	-0.143	-0.407	0.000
34	A	36	GLU	-1	-0.823	-0.885	1.736	-154.709	-161.813	34.369	-15.561	-11.704	-0.177
35	A	37	ASN	0	0.011	-0.009	3.955	-0.541	-0.186	0.001	-0.092	-0.264	0.000
36	A	38	PRO	0	0.042	0.041	5.279	-1.643	-1.643	0.000	0.000	0.000	0.000
37	A	39	PHE	0	0.015	-0.003	6.643	2.033	2.033	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.017	-0.005	8.636	3.047	3.047	0.000	0.000	0.000	0.000
39	A	41	GLY	0	-0.027	-0.015	10.311	-1.040	-1.040	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.792	0.893	7.366	34.153	34.153	0.000	0.000	0.000	0.000
41	A	43	TYR	0	-0.011	0.007	13.995	0.187	0.187	0.000	0.000	0.000	0.000
42	A	44	VAL	0	-0.044	-0.030	13.552	0.082	0.082	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.891	-0.941	16.819	-14.722	-14.722	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.894	-0.915	16.406	-18.043	-18.043	0.000	0.000	0.000	0.000
45	A	47	LEU	0	-0.004	-0.014	13.727	-1.426	-1.426	0.000	0.000	0.000	0.000
46	A	48	THR	0	-0.008	-0.035	12.741	-0.493	-0.493	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.896	-0.946	7.200	-36.355	-36.355	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.025	-0.006	7.499	-1.487	-1.487	0.000	0.000	0.000	0.000
49	A	51	MET	0	-0.037	-0.009	9.525	0.961	0.961	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.889	-0.944	10.054	-18.964	-18.964	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.031	-0.036	4.762	-0.811	-0.751	-0.001	-0.001	-0.058	0.000
52	A	54	GLY	0	0.027	0.002	7.384	0.403	0.403	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.039	-0.010	10.192	1.182	1.182	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.961	-0.969	7.368	-22.126	-22.126	0.000	0.000	0.000	0.000
55	A	57	LEU	0	-0.024	-0.025	5.956	0.686	0.686	0.000	0.000	0.000	0.000
56	A	58	GLY	0	0.021	0.006	9.339	0.888	0.888	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.009	-0.006	12.938	0.887	0.887	0.000	0.000	0.000	0.000
58	A	60	LEU	0	-0.014	0.000	8.776	0.638	0.638	0.000	0.000	0.000	0.000
59	A	61	LEU	0	-0.013	-0.023	10.845	0.556	0.556	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.055	0.028	13.798	0.695	0.695	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.849	-0.915	15.709	-12.100	-12.100	0.000	0.000	0.000	0.000
62	A	64	ARG	1	0.815	0.889	13.776	15.561	15.561	0.000	0.000	0.000	0.000
63	A	65	CYS	0	-0.035	-0.002	16.989	0.389	0.389	0.000	0.000	0.000	0.000
64	A	66	VAL	0	0.008	0.012	19.717	0.473	0.473	0.000	0.000	0.000	0.000
65	A	67	GLN	0	-0.036	-0.027	17.762	0.079	0.079	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.041	-0.014	20.586	0.347	0.347	0.000	0.000	0.000	0.000
67	A	69	LEU	0	0.008	0.005	22.441	0.336	0.336	0.000	0.000	0.000	0.000
68	A	70	GLY	0	-0.014	0.013	24.829	0.425	0.425	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.076	-0.028	25.620	0.389	0.389	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.854	0.902	25.442	8.437	8.437	0.000	0.000	0.000	0.000
71	A	73	PRO	0	0.030	-0.007	22.725	0.102	0.102	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.815	-0.892	24.943	-9.218	-9.218	0.000	0.000	0.000	0.000
73	A	75	GLN	0	-0.022	-0.014	28.249	0.211	0.211	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.012	0.016	25.377	0.079	0.079	0.000	0.000	0.000	0.000
75	A	77	GLU	-1	-0.828	-0.866	27.441	-8.436	-8.436	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.045	-0.027	26.871	0.181	0.181	0.000	0.000	0.000	0.000
77	A	79	TYR	0	-0.038	-0.017	22.044	-0.248	-0.248	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.044	0.017	21.271	0.376	0.376	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.827	0.920	15.658	14.568	14.568	0.000	0.000	0.000	0.000
80	A	82	SER	0	0.018	-0.015	16.344	0.682	0.682	0.000	0.000	0.000	0.000
81	A	83	ALA	0	-0.022	0.003	13.039	-0.903	-0.903	0.000	0.000	0.000	0.000
82	A	84	MET	0	-0.023	0.004	13.641	0.831	0.831	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.018	-0.008	11.643	-1.818	-1.818	0.000	0.000	0.000	0.000
84	A	86	GLY	0	0.007	0.006	11.679	1.343	1.343	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.862	-0.958	13.202	-17.021	-17.021	0.000	0.000	0.000	0.000
86	A	88	ASN	0	-0.065	-0.027	12.741	1.782	1.782	0.000	0.000	0.000	0.000
87	A	89	GLY	0	-0.002	-0.004	12.790	-1.497	-1.497	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.834	-0.926	13.644	-15.456	-15.456	0.000	0.000	0.000	0.000
89	A	91	LEU	0	0.036	0.006	15.194	-0.700	-0.700	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.802	-0.918	16.975	-14.869	-14.869	0.000	0.000	0.000	0.000
91	A	93	HIS	0	0.040	0.038	11.479	-1.229	-1.229	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.021	0.005	12.524	-0.726	-0.726	0.000	0.000	0.000	0.000
93	A	95	ALA	0	-0.022	-0.012	14.318	0.558	0.558	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.003	0.002	13.132	0.458	0.458	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.009	0.002	7.595	0.302	0.302	0.000	0.000	0.000	0.000
96	A	98	LEU	0	-0.054	-0.035	11.857	0.489	0.489	0.000	0.000	0.000	0.000
97	A	99	HIS	0	0.009	0.031	15.229	1.023	1.023	0.000	0.000	0.000	0.000
98	A	100	PRO	0	0.003	0.023	13.234	0.914	0.914	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.914	0.947	16.529	11.784	11.784	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.021	0.021	15.764	0.125	0.125	0.000	0.000	0.000	0.000
101	A	116	LEU	0	0.012	0.006	24.093	0.102	0.102	0.000	0.000	0.000	0.000
102	A	117	VAL	0	-0.042	-0.024	21.015	0.118	0.118	0.000	0.000	0.000	0.000
103	A	118	PRO	0	0.006	0.025	23.110	-0.266	-0.266	0.000	0.000	0.000	0.000
104	A	119	SER	0	-0.027	-0.033	19.016	-0.587	-0.587	0.000	0.000	0.000	0.000
105	A	120	SER	0	-0.023	-0.004	19.666	0.473	0.473	0.000	0.000	0.000	0.000
106	A	121	LYS	1	0.889	0.943	17.806	13.502	13.502	0.000	0.000	0.000	0.000
107	A	122	LYS	1	0.793	0.875	17.562	13.891	13.891	0.000	0.000	0.000	0.000
108	A	123	MET	0	0.028	0.028	15.840	-0.841	-0.841	0.000	0.000	0.000	0.000
109	A	124	GLY	0	0.001	-0.010	16.692	0.905	0.905	0.000	0.000	0.000	0.000
110	A	125	SER	0	-0.002	-0.002	15.991	-1.156	-1.156	0.000	0.000	0.000	0.000
111	A	126	PRO	0	-0.044	-0.038	14.316	0.306	0.306	0.000	0.000	0.000	0.000
112	A	127	GLY	0	-0.008	0.017	16.411	0.947	0.947	0.000	0.000	0.000	0.000
113	A	128	GLN	0	0.040	0.034	18.511	0.721	0.721	0.000	0.000	0.000	0.000
114	A	129	VAL	0	-0.005	-0.005	18.918	-0.584	-0.584	0.000	0.000	0.000	0.000
115	A	130	LEU	0	-0.039	-0.010	15.638	0.024	0.024	0.000	0.000	0.000	0.000
116	A	131	ASP	-1	-0.814	-0.902	19.596	-11.772	-11.772	0.000	0.000	0.000	0.000
117	A	132	VAL	0	-0.022	0.004	18.603	-0.619	-0.619	0.000	0.000	0.000	0.000
118	A	133	PRO	0	0.031	0.029	21.130	0.431	0.431	0.000	0.000	0.000	0.000
119	A	134	LEU	0	0.000	-0.012	22.977	-0.339	-0.339	0.000	0.000	0.000	0.000
120	A	135	GLY	0	-0.018	-0.022	25.548	0.341	0.341	0.000	0.000	0.000	0.000
121	A	136	HIS	0	-0.032	-0.007	27.520	0.085	0.085	0.000	0.000	0.000	0.000
122	A	146	PHE	0	-0.080	-0.058	27.785	0.073	0.073	0.000	0.000	0.000	0.000
123	A	147	ASP	-1	-0.772	-0.865	28.921	-9.593	-9.593	0.000	0.000	0.000	0.000
124	A	148	GLY	0	0.027	-0.006	25.518	-0.296	-0.296	0.000	0.000	0.000	0.000
125	A	149	ILE	0	-0.009	0.005	22.010	0.270	0.270	0.000	0.000	0.000	0.000
126	A	150	GLU	-1	-0.913	-0.951	22.567	-11.651	-11.651	0.000	0.000	0.000	0.000
127	A	151	VAL	0	-0.011	0.001	17.111	-0.110	-0.110	0.000	0.000	0.000	0.000
128	A	152	ARG	1	0.902	0.941	17.877	13.312	13.312	0.000	0.000	0.000	0.000
129	A	153	LEU	0	0.033	0.009	13.112	0.093	0.093	0.000	0.000	0.000	0.000
130	A	154	ASN	0	-0.036	-0.025	16.406	-0.502	-0.502	0.000	0.000	0.000	0.000
131	A	155	ASP	-1	-0.787	-0.866	12.462	-21.164	-21.164	0.000	0.000	0.000	0.000
132	A	156	ALA	0	-0.029	0.007	11.485	-2.090	-2.090	0.000	0.000	0.000	0.000
133	A	157	PRO	0	0.072	0.047	11.246	1.216	1.216	0.000	0.000	0.000	0.000
134	A	158	ARG	1	0.907	0.921	7.502	33.662	33.662	0.000	0.000	0.000	0.000
135	A	159	ALA	0	0.035	0.012	11.426	-0.807	-0.807	0.000	0.000	0.000	0.000
136	A	160	ASN	0	0.010	0.004	6.377	4.450	4.450	0.000	0.000	0.000	0.000
137	A	161	GLU	-1	-0.756	-0.834	6.511	-38.159	-38.159	0.000	0.000	0.000	0.000
138	A	162	ILE	0	0.029	0.010	7.438	2.832	2.832	0.000	0.000	0.000	0.000
139	A	163	MET	0	-0.045	0.002	8.358	-1.854	-1.854	0.000	0.000	0.000	0.000
140	A	164	VAL	0	0.022	-0.001	9.276	1.216	1.216	0.000	0.000	0.000	0.000
141	A	165	ALA	0	0.015	0.003	11.678	-0.180	-0.180	0.000	0.000	0.000	0.000
142	A	166	VAL	0	-0.002	-0.007	14.107	0.252	0.252	0.000	0.000	0.000	0.000
143	A	167	ALA	0	0.017	0.004	16.649	-0.057	-0.057	0.000	0.000	0.000	0.000
144	A	168	VAL	0	-0.007	-0.015	20.266	0.115	0.115	0.000	0.000	0.000	0.000
145	A	169	THR	0	0.025	0.013	23.215	-0.081	-0.081	0.000	0.000	0.000	0.000
146	A	170	ASP	-1	-0.852	-0.920	26.935	-9.060	-9.060	0.000	0.000	0.000	0.000
147	A	171	SER	0	-0.019	-0.036	29.600	0.280	0.280	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)