FMO DATABASE

FMODB ID: KGZ13

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	OptH
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	-1263025.299998
FMO2-HF: Nuclear repulsion	1207552.239538
FMO2-HF: Total energy	-55473.06046
FMO2-MP2: Total energy	-55634.090358

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.
-219.757	-223.17	33.259	-15.989	-13.858	-0.173

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 : 0.818 / q_NPA : 0.891

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	0.728	0.851	3.878	29.751	31.062	-0.016	-0.581	-0.713	0.001
4	A	6	LYS	1	0.853	0.909	5.905	22.869	22.869	0.000	0.000	0.000	0.000
5	A	7	ILE	0	0.005	0.001	8.965	-0.904	-0.904	0.000	0.000	0.000	0.000
6	A	8	ALA	0	-0.057	-0.017	11.157	0.681	0.681	0.000	0.000	0.000	0.000
7	A	9	VAL	0	-0.006	-0.010	14.804	-0.250	-0.250	0.000	0.000	0.000	0.000
8	A	10	PHE	0	-0.028	-0.004	16.859	0.176	0.176	0.000	0.000	0.000	0.000
9	A	11	ILE	0	0.018	-0.001	21.001	-0.069	-0.069	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.959	-0.972	24.101	-10.151	-10.151	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.939	-0.978	27.425	-8.920	-8.920	0.000	0.000	0.000	0.000
12	A	14	THR	0	0.015	0.022	30.774	0.104	0.104	0.000	0.000	0.000	0.000
13	A	15	ARG	1	0.958	0.965	33.759	8.161	8.161	0.000	0.000	0.000	0.000
14	A	16	ILE	0	-0.022	0.000	37.072	0.226	0.226	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.881	-0.942	35.215	-8.381	-8.381	0.000	0.000	0.000	0.000
16	A	18	DAL	0	-0.031	-0.014	39.143	0.175	0.175	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.025	-0.004	41.943	0.163	0.163	0.000	0.000	0.000	0.000
18	A	20	ARG	1	0.926	0.957	40.701	7.153	7.153	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.931	-0.973	41.472	-6.765	-6.765	0.000	0.000	0.000	0.000
20	A	22	ILE	0	-0.103	-0.040	36.478	0.129	0.129	0.000	0.000	0.000	0.000
21	A	23	SER	0	-0.032	-0.001	38.479	-0.161	-0.161	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.010	-0.015	35.795	0.185	0.185	0.000	0.000	0.000	0.000
23	A	25	PRO	0	0.020	-0.006	33.706	0.015	0.015	0.000	0.000	0.000	0.000
24	A	26	THR	0	0.035	0.040	32.479	-0.113	-0.113	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.833	0.902	27.928	9.361	9.361	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.928	0.982	25.306	9.928	9.928	0.000	0.000	0.000	0.000
27	A	29	ALA	0	0.004	0.001	21.297	-0.042	-0.042	0.000	0.000	0.000	0.000
28	A	30	VAL	0	0.018	0.006	17.515	-0.089	-0.089	0.000	0.000	0.000	0.000
29	A	31	ALA	0	-0.025	0.000	14.361	-0.058	-0.058	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.009	-0.012	12.345	-0.260	-0.260	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.011	0.003	7.368	-0.019	-0.019	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.038	-0.012	7.391	0.551	0.551	0.000	0.000	0.000	0.000
33	A	35	ILE	0	0.016	0.004	3.118	-2.520	-1.858	0.030	-0.191	-0.501	0.000
34	A	36	GLU	-1	-0.831	-0.901	1.811	-146.527	-152.465	33.240	-15.082	-12.221	-0.173
35	A	37	ASN	0	-0.016	-0.019	3.734	-0.774	-0.222	0.005	-0.135	-0.423	-0.001
36	A	38	PRO	0	0.039	0.031	5.199	-2.777	-2.777	0.000	0.000	0.000	0.000
37	A	39	PHE	0	-0.006	-0.020	5.982	2.161	2.161	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.012	0.007	7.983	3.324	3.324	0.000	0.000	0.000	0.000
39	A	41	GLY	0	-0.052	-0.031	9.590	-1.318	-1.318	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.870	0.947	8.173	32.985	32.985	0.000	0.000	0.000	0.000
41	A	43	TYR	0	0.036	0.029	13.206	0.216	0.216	0.000	0.000	0.000	0.000
42	A	44	VAL	0	-0.043	-0.027	12.767	0.233	0.233	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.900	-0.956	15.945	-14.687	-14.687	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.892	-0.904	16.505	-18.323	-18.323	0.000	0.000	0.000	0.000
45	A	47	LEU	0	-0.026	-0.028	13.629	-1.611	-1.611	0.000	0.000	0.000	0.000
46	A	48	THR	0	0.013	-0.026	13.199	-0.433	-0.433	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.920	-0.956	6.695	-39.936	-39.936	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.029	-0.026	7.498	-1.445	-1.445	0.000	0.000	0.000	0.000
49	A	51	MET	0	-0.044	-0.011	9.901	0.902	0.902	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.903	-0.950	10.191	-19.586	-19.586	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.014	-0.014	4.803	-1.040	-1.040	0.000	0.000	0.000	0.000
52	A	54	GLY	0	0.008	-0.006	7.401	0.552	0.552	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.044	-0.017	9.989	1.244	1.244	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.945	-0.965	7.350	-22.721	-22.721	0.000	0.000	0.000	0.000
55	A	57	LEU	0	-0.013	-0.015	5.995	0.748	0.748	0.000	0.000	0.000	0.000
56	A	58	GLY	0	0.013	0.007	9.135	0.976	0.976	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.002	0.004	12.662	0.948	0.948	0.000	0.000	0.000	0.000
58	A	60	LEU	0	-0.002	0.006	8.404	0.618	0.618	0.000	0.000	0.000	0.000
59	A	61	LEU	0	-0.032	-0.040	10.370	0.626	0.626	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.024	0.003	13.336	0.729	0.729	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.896	-0.950	15.436	-11.941	-11.941	0.000	0.000	0.000	0.000
62	A	64	ARG	1	0.905	0.949	13.163	16.134	16.134	0.000	0.000	0.000	0.000
63	A	65	CYS	0	-0.047	-0.004	16.664	0.511	0.511	0.000	0.000	0.000	0.000
64	A	66	VAL	0	0.016	0.016	19.246	0.466	0.466	0.000	0.000	0.000	0.000
65	A	67	GLN	0	-0.020	-0.016	17.913	0.019	0.019	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.062	-0.023	20.222	0.322	0.322	0.000	0.000	0.000	0.000
67	A	69	LEU	0	-0.015	-0.007	22.072	0.354	0.354	0.000	0.000	0.000	0.000
68	A	70	GLY	0	-0.013	0.012	24.396	0.425	0.425	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.052	-0.012	25.215	0.376	0.376	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.834	0.893	25.108	8.463	8.463	0.000	0.000	0.000	0.000
71	A	73	PRO	0	0.052	0.000	22.562	0.086	0.086	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.832	-0.904	24.793	-9.272	-9.272	0.000	0.000	0.000	0.000
73	A	75	GLN	0	-0.046	-0.034	28.086	0.152	0.152	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.007	0.019	25.104	0.063	0.063	0.000	0.000	0.000	0.000
75	A	77	GLU	-1	-0.851	-0.871	27.170	-8.540	-8.540	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.019	-0.009	26.592	0.111	0.111	0.000	0.000	0.000	0.000
77	A	79	TYR	0	-0.014	-0.014	21.629	-0.242	-0.242	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.014	0.004	21.083	0.374	0.374	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.851	0.950	16.218	14.386	14.386	0.000	0.000	0.000	0.000
80	A	82	SER	0	0.037	0.021	16.392	0.682	0.682	0.000	0.000	0.000	0.000
81	A	83	ALA	0	-0.013	0.002	12.658	-0.840	-0.840	0.000	0.000	0.000	0.000
82	A	84	MET	0	-0.033	0.003	13.355	0.869	0.869	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.030	-0.020	11.785	-1.896	-1.896	0.000	0.000	0.000	0.000
84	A	86	GLY	0	0.022	0.011	11.474	1.463	1.463	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.866	-0.966	13.027	-17.406	-17.406	0.000	0.000	0.000	0.000
86	A	88	ASN	0	-0.087	-0.037	12.184	1.829	1.829	0.000	0.000	0.000	0.000
87	A	89	GLY	0	-0.004	-0.003	12.792	-1.292	-1.292	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.849	-0.913	13.519	-17.071	-17.071	0.000	0.000	0.000	0.000
89	A	91	LEU	0	0.034	-0.003	14.935	-0.682	-0.682	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.908	-0.970	16.716	-16.052	-16.052	0.000	0.000	0.000	0.000
91	A	93	HIS	0	0.089	0.043	11.382	-1.236	-1.236	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.011	0.009	12.512	-0.674	-0.674	0.000	0.000	0.000	0.000
93	A	95	ALA	0	-0.059	-0.044	14.021	0.496	0.496	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.002	0.014	13.284	0.524	0.524	0.000	0.000	0.000	0.000
95	A	97	ILE	0	0.013	0.006	7.694	0.348	0.348	0.000	0.000	0.000	0.000
96	A	98	LEU	0	-0.069	-0.043	11.968	0.596	0.596	0.000	0.000	0.000	0.000
97	A	99	HIS	0	-0.006	0.005	15.057	1.015	1.015	0.000	0.000	0.000	0.000
98	A	100	PRO	0	0.005	0.027	13.354	1.088	1.088	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.927	0.956	16.592	11.877	11.877	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.001	0.003	15.757	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	116	LEU	0	-0.010	-0.021	23.663	0.061	0.061	0.000	0.000	0.000	0.000
102	A	117	VAL	0	-0.027	-0.005	20.676	0.178	0.178	0.000	0.000	0.000	0.000
103	A	118	PRO	0	0.003	0.035	23.091	-0.271	-0.271	0.000	0.000	0.000	0.000
104	A	119	SER	0	-0.003	-0.020	19.158	-0.570	-0.570	0.000	0.000	0.000	0.000
105	A	120	SER	0	-0.047	-0.027	19.794	0.470	0.470	0.000	0.000	0.000	0.000
106	A	121	LYS	1	0.986	0.990	17.585	13.562	13.562	0.000	0.000	0.000	0.000
107	A	122	LYS	1	0.899	0.953	17.221	14.377	14.377	0.000	0.000	0.000	0.000
108	A	123	MET	0	0.075	0.059	15.603	-0.867	-0.867	0.000	0.000	0.000	0.000
109	A	124	GLY	0	-0.035	-0.035	16.382	0.999	0.999	0.000	0.000	0.000	0.000
110	A	125	SER	0	0.043	0.023	16.015	-0.896	-0.896	0.000	0.000	0.000	0.000
111	A	126	PRO	0	-0.041	-0.037	14.233	0.243	0.243	0.000	0.000	0.000	0.000
112	A	127	GLY	0	-0.033	0.001	16.253	0.959	0.959	0.000	0.000	0.000	0.000
113	A	128	GLN	0	0.028	0.014	18.402	0.808	0.808	0.000	0.000	0.000	0.000
114	A	129	VAL	0	0.009	0.001	18.589	-0.713	-0.713	0.000	0.000	0.000	0.000
115	A	130	LEU	0	-0.064	-0.019	15.557	0.079	0.079	0.000	0.000	0.000	0.000
116	A	131	ASP	-1	-0.874	-0.951	19.609	-11.412	-11.412	0.000	0.000	0.000	0.000
117	A	132	VAL	0	-0.079	-0.040	18.822	-0.459	-0.459	0.000	0.000	0.000	0.000
118	A	133	PRO	0	0.018	0.020	21.128	0.480	0.480	0.000	0.000	0.000	0.000
119	A	134	LEU	0	0.017	0.002	23.121	-0.326	-0.326	0.000	0.000	0.000	0.000
120	A	135	GLY	0	-0.036	-0.021	25.601	0.365	0.365	0.000	0.000	0.000	0.000
121	A	136	HIS	0	0.007	0.006	27.305	0.036	0.036	0.000	0.000	0.000	0.000
122	A	146	PHE	0	-0.091	-0.065	27.884	0.070	0.070	0.000	0.000	0.000	0.000
123	A	147	ASP	-1	-0.809	-0.884	29.251	-9.534	-9.534	0.000	0.000	0.000	0.000
124	A	148	GLY	0	0.011	-0.022	25.707	-0.294	-0.294	0.000	0.000	0.000	0.000
125	A	149	ILE	0	-0.004	0.002	21.954	0.254	0.254	0.000	0.000	0.000	0.000
126	A	150	GLU	-1	-0.897	-0.934	22.603	-11.718	-11.718	0.000	0.000	0.000	0.000
127	A	151	VAL	0	-0.017	0.000	17.170	-0.107	-0.107	0.000	0.000	0.000	0.000
128	A	152	ARG	1	0.917	0.951	17.827	13.578	13.578	0.000	0.000	0.000	0.000
129	A	153	LEU	0	0.046	0.011	12.973	0.013	0.013	0.000	0.000	0.000	0.000
130	A	154	ASN	0	-0.054	-0.036	16.664	-0.600	-0.600	0.000	0.000	0.000	0.000
131	A	155	ASP	-1	-0.801	-0.886	13.124	-20.827	-20.827	0.000	0.000	0.000	0.000
132	A	156	ALA	0	-0.022	0.014	11.241	-1.908	-1.908	0.000	0.000	0.000	0.000
133	A	157	PRO	0	0.042	0.024	11.041	1.339	1.339	0.000	0.000	0.000	0.000
134	A	158	ARG	1	0.954	0.951	8.208	31.448	31.448	0.000	0.000	0.000	0.000
135	A	159	ALA	0	0.028	0.011	11.040	-0.895	-0.895	0.000	0.000	0.000	0.000
136	A	160	ASN	0	0.007	-0.005	5.990	4.492	4.492	0.000	0.000	0.000	0.000
137	A	161	GLU	-1	-0.754	-0.853	6.238	-38.295	-38.295	0.000	0.000	0.000	0.000
138	A	162	ILE	0	0.035	0.016	7.056	3.133	3.133	0.000	0.000	0.000	0.000
139	A	163	MET	0	-0.044	-0.009	7.974	-1.832	-1.832	0.000	0.000	0.000	0.000
140	A	164	VAL	0	0.015	0.006	9.140	1.580	1.580	0.000	0.000	0.000	0.000
141	A	165	ALA	0	0.017	0.003	11.761	-0.064	-0.064	0.000	0.000	0.000	0.000
142	A	166	VAL	0	0.005	-0.001	14.059	0.277	0.277	0.000	0.000	0.000	0.000
143	A	167	ALA	0	0.028	0.010	16.511	-0.031	-0.031	0.000	0.000	0.000	0.000
144	A	168	VAL	0	-0.012	-0.017	20.087	0.064	0.064	0.000	0.000	0.000	0.000
145	A	169	THR	0	0.018	0.011	22.879	-0.108	-0.108	0.000	0.000	0.000	0.000
146	A	170	ASP	-1	-0.861	-0.940	26.492	-9.104	-9.104	0.000	0.000	0.000	0.000
147	A	171	SER	0	-0.055	-0.056	29.023	0.315	0.315	0.000	0.000	0.000	0.000

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