FMO DATABASE

FMODB ID: 8273Y

Calculation Name: 2PQA-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PQA

Chain ID: A

ChEMBL ID:

UniProt ID: P15927

Base Structure: X-ray

Registration Date: 2023-03-13

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1117146.010287
FMO2-HF: Nuclear repulsion	1065335.023203
FMO2-HF: Total energy	-51810.987084
FMO2-MP2: Total energy	-51960.312862

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:42:ARG)

Summations of interaction energy for fragment #1(A:42:ARG)

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.
-73.468	-71.932	-0.016	-0.738	-0.781	0

Interaction energy analysis for fragmet #1(A:42:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.977 / q_NPA : 0.963

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	44	GLN	0	0.034	0.007	3.876	1.547	3.083	-0.016	-0.738	-0.781
4	A	45	HIS	0	-0.052	-0.004	5.518	1.564	1.564	0.000	0.000	0.000
5	A	46	ILE	0	0.013	-0.009	7.866	-0.281	-0.281	0.000	0.000	0.000
6	A	47	VAL	0	-0.019	-0.001	11.025	0.431	0.431	0.000	0.000	0.000
7	A	48	PRO	0	0.023	0.047	13.537	0.259	0.259	0.000	0.000	0.000
8	A	49	CYS	0	-0.076	-0.054	16.146	-0.423	-0.423	0.000	0.000	0.000
9	A	50	THR	0	0.062	0.016	19.054	0.233	0.233	0.000	0.000	0.000
10	A	51	ILE	0	0.014	-0.011	21.393	-0.638	-0.638	0.000	0.000	0.000
11	A	52	SER	0	0.012	0.003	23.188	-0.400	-0.400	0.000	0.000	0.000
12	A	53	GLN	0	0.027	0.024	19.103	-0.318	-0.318	0.000	0.000	0.000
13	A	54	LEU	0	0.041	0.025	17.262	-0.635	-0.635	0.000	0.000	0.000
14	A	55	LEU	0	-0.038	-0.019	19.658	-0.415	-0.415	0.000	0.000	0.000
15	A	56	SER	0	-0.065	-0.038	20.502	-0.194	-0.194	0.000	0.000	0.000
16	A	57	ALA	0	-0.007	0.007	16.133	-0.222	-0.222	0.000	0.000	0.000
17	A	58	THR	0	-0.011	0.009	16.929	0.164	0.164	0.000	0.000	0.000
18	A	59	LEU	0	-0.004	-0.012	15.079	-0.734	-0.734	0.000	0.000	0.000
19	A	60	VAL	0	-0.035	-0.020	13.428	1.161	1.161	0.000	0.000	0.000
20	A	61	ASP	-1	-0.876	-0.932	11.586	-22.695	-22.695	0.000	0.000	0.000
21	A	62	GLU	-1	-0.957	-0.987	11.480	-21.057	-21.057	0.000	0.000	0.000
22	A	63	VAL	0	-0.064	-0.010	8.335	-0.665	-0.665	0.000	0.000	0.000
23	A	64	PHE	0	-0.012	-0.016	11.664	1.894	1.894	0.000	0.000	0.000
24	A	65	ARG	1	0.842	0.901	8.870	26.161	26.161	0.000	0.000	0.000
25	A	66	ILE	0	0.016	0.005	13.471	1.663	1.663	0.000	0.000	0.000
26	A	67	GLY	0	0.016	0.013	14.449	-0.420	-0.420	0.000	0.000	0.000
27	A	68	ASN	0	-0.023	-0.029	12.537	-0.478	-0.478	0.000	0.000	0.000
28	A	69	VAL	0	-0.017	0.009	8.957	-2.525	-2.525	0.000	0.000	0.000
29	A	70	GLU	-1	-0.807	-0.892	6.834	-36.328	-36.328	0.000	0.000	0.000
30	A	71	ILE	0	-0.043	-0.013	8.301	-1.211	-1.211	0.000	0.000	0.000
31	A	72	SER	0	0.038	0.014	8.047	1.114	1.114	0.000	0.000	0.000
32	A	73	GLN	0	-0.006	-0.020	9.707	2.521	2.521	0.000	0.000	0.000
33	A	74	VAL	0	-0.004	-0.004	12.003	-0.544	-0.544	0.000	0.000	0.000
34	A	75	THR	0	-0.012	-0.018	14.857	0.129	0.129	0.000	0.000	0.000
35	A	76	ILE	0	-0.013	0.002	18.175	-0.103	-0.103	0.000	0.000	0.000
36	A	77	VAL	0	-0.005	-0.002	21.607	0.148	0.148	0.000	0.000	0.000
37	A	78	GLY	0	0.003	0.001	25.167	0.003	0.003	0.000	0.000	0.000
38	A	79	ILE	0	-0.027	0.001	28.185	0.041	0.041	0.000	0.000	0.000
39	A	80	ILE	0	0.008	0.012	30.197	-0.144	-0.144	0.000	0.000	0.000
40	A	81	ARG	1	0.748	0.847	32.129	8.603	8.603	0.000	0.000	0.000
41	A	82	HIS	0	-0.021	-0.009	33.377	0.316	0.316	0.000	0.000	0.000
42	A	83	ALA	0	0.040	0.009	32.742	-0.324	-0.324	0.000	0.000	0.000
43	A	84	GLU	-1	-0.960	-0.962	32.927	-8.576	-8.576	0.000	0.000	0.000
44	A	85	LYS	1	0.979	0.980	32.802	7.566	7.566	0.000	0.000	0.000
45	A	86	ALA	0	0.043	0.031	30.924	0.201	0.201	0.000	0.000	0.000
46	A	87	PRO	0	-0.022	-0.031	32.667	-0.011	-0.011	0.000	0.000	0.000
47	A	88	THR	0	-0.029	-0.009	28.521	0.031	0.031	0.000	0.000	0.000
48	A	89	ASN	0	-0.053	-0.019	26.117	-0.118	-0.118	0.000	0.000	0.000
49	A	90	ILE	0	0.038	0.032	28.531	0.362	0.362	0.000	0.000	0.000
50	A	91	VAL	0	-0.008	-0.010	28.066	-0.503	-0.503	0.000	0.000	0.000
51	A	92	TYR	0	0.062	0.039	27.646	0.454	0.454	0.000	0.000	0.000
52	A	93	LYS	1	0.780	0.883	28.572	9.570	9.570	0.000	0.000	0.000
53	A	94	ILE	0	0.013	0.005	25.854	0.264	0.264	0.000	0.000	0.000
54	A	95	ASP	-1	-0.828	-0.908	28.318	-9.230	-9.230	0.000	0.000	0.000
55	A	96	ASP	-1	-0.708	-0.829	25.394	-11.020	-11.020	0.000	0.000	0.000
56	A	97	MET	0	0.024	-0.001	28.672	-0.116	-0.116	0.000	0.000	0.000
57	A	98	THR	0	-0.082	-0.034	26.671	-0.003	-0.003	0.000	0.000	0.000
58	A	99	ALA	0	-0.043	-0.029	27.222	-0.149	-0.149	0.000	0.000	0.000
59	A	100	ALA	0	0.020	0.020	29.174	0.235	0.235	0.000	0.000	0.000
60	A	101	PRO	0	0.030	0.009	28.705	-0.351	-0.351	0.000	0.000	0.000
61	A	102	MET	0	-0.003	0.027	22.398	-0.115	-0.115	0.000	0.000	0.000
62	A	103	ASP	-1	-0.831	-0.902	26.126	-10.240	-10.240	0.000	0.000	0.000
63	A	104	VAL	0	-0.019	-0.024	22.906	-0.638	-0.638	0.000	0.000	0.000
64	A	105	ARG	1	0.883	0.941	22.920	12.719	12.719	0.000	0.000	0.000
65	A	106	GLN	0	0.030	-0.003	23.440	-1.014	-1.014	0.000	0.000	0.000
66	A	107	TRP	0	-0.015	-0.013	22.357	0.126	0.126	0.000	0.000	0.000
67	A	108	VAL	0	-0.034	-0.020	26.063	-0.087	-0.087	0.000	0.000	0.000
68	A	109	ASP	-1	-0.847	-0.925	29.022	-9.273	-9.273	0.000	0.000	0.000
69	A	110	THR	0	-0.091	-0.084	31.357	0.003	0.003	0.000	0.000	0.000
70	A	111	ASP	-1	-0.927	-0.943	34.499	-7.768	-7.768	0.000	0.000	0.000
71	A	112	ASP	-1	-0.894	-0.921	32.879	-8.655	-8.655	0.000	0.000	0.000
72	A	113	THR	0	-0.171	-0.102	32.985	0.226	0.226	0.000	0.000	0.000
73	A	114	SER	0	-0.134	-0.088	29.376	0.010	0.010	0.000	0.000	0.000
74	A	115	SER	-1	-0.735	-0.834	27.943	-9.922	-9.922	0.000	0.000	0.000
75	A	116	GLU	-1	-0.897	-0.924	28.463	-9.912	-9.912	0.000	0.000	0.000
76	A	117	ASN	0	0.031	0.018	31.655	0.445	0.445	0.000	0.000	0.000
77	A	118	THR	0	-0.122	-0.089	31.301	0.174	0.174	0.000	0.000	0.000
78	A	119	VAL	0	-0.079	-0.049	33.485	0.109	0.109	0.000	0.000	0.000
79	A	120	VAL	0	0.059	0.052	30.357	0.215	0.215	0.000	0.000	0.000
80	A	121	PRO	0	0.033	0.011	33.507	-0.062	-0.062	0.000	0.000	0.000
81	A	122	PRO	0	0.005	-0.007	34.947	-0.182	-0.182	0.000	0.000	0.000
82	A	123	GLU	-1	-0.851	-0.920	35.911	-7.682	-7.682	0.000	0.000	0.000
83	A	124	THR	0	-0.029	-0.017	32.589	0.079	0.079	0.000	0.000	0.000
84	A	125	TYR	0	0.015	-0.004	30.070	-0.167	-0.167	0.000	0.000	0.000
85	A	126	VAL	0	-0.015	-0.009	26.400	0.039	0.039	0.000	0.000	0.000
86	A	127	LYS	1	0.857	0.939	21.138	11.615	11.615	0.000	0.000	0.000
87	A	128	VAL	0	-0.024	-0.014	20.691	0.072	0.072	0.000	0.000	0.000
88	A	129	ALA	0	0.015	0.002	17.336	-0.422	-0.422	0.000	0.000	0.000
89	A	130	GLY	0	0.058	0.020	16.878	0.457	0.457	0.000	0.000	0.000
90	A	131	HIS	0	-0.036	-0.007	12.545	-0.954	-0.954	0.000	0.000	0.000
91	A	132	LEU	0	0.026	0.028	14.668	1.139	1.139	0.000	0.000	0.000
92	A	133	ARG	1	0.849	0.917	14.005	17.200	17.200	0.000	0.000	0.000
93	A	134	SER	0	0.037	0.011	18.350	0.716	0.716	0.000	0.000	0.000
94	A	135	PHE	0	0.029	0.021	20.332	-0.389	-0.389	0.000	0.000	0.000
95	A	136	GLN	0	0.003	-0.006	23.593	0.465	0.465	0.000	0.000	0.000
96	A	137	ASN	0	-0.001	0.002	23.541	-0.084	-0.084	0.000	0.000	0.000
97	A	138	LYS	1	0.899	0.944	24.609	10.716	10.716	0.000	0.000	0.000
98	A	139	LYS	1	0.813	0.889	19.152	14.536	14.536	0.000	0.000	0.000
99	A	140	SER	0	-0.040	-0.007	21.317	0.604	0.604	0.000	0.000	0.000
100	A	141	LEU	0	0.053	0.016	18.440	-0.745	-0.745	0.000	0.000	0.000
101	A	142	VAL	0	-0.052	-0.022	18.444	0.644	0.644	0.000	0.000	0.000
102	A	143	ALA	0	-0.009	0.000	18.509	-0.813	-0.813	0.000	0.000	0.000
103	A	144	PHE	0	-0.020	-0.020	15.868	-0.187	-0.187	0.000	0.000	0.000
104	A	145	LYS	1	0.958	0.981	19.017	13.201	13.201	0.000	0.000	0.000
105	A	146	ILE	0	0.012	0.003	22.104	-0.321	-0.321	0.000	0.000	0.000
106	A	147	MET	0	-0.009	0.000	21.269	0.064	0.064	0.000	0.000	0.000
107	A	148	PRO	0	0.057	0.025	26.667	-0.110	-0.110	0.000	0.000	0.000
108	A	149	LEU	0	-0.048	-0.021	26.650	-0.122	-0.122	0.000	0.000	0.000
109	A	150	GLU	-1	-0.910	-0.955	30.380	-8.154	-8.154	0.000	0.000	0.000
110	A	151	ASP	-1	-0.822	-0.894	31.153	-8.306	-8.306	0.000	0.000	0.000
111	A	152	MET	0	0.009	0.003	30.566	-0.361	-0.361	0.000	0.000	0.000
112	A	153	ASN	0	-0.060	-0.047	30.610	-0.158	-0.158	0.000	0.000	0.000
113	A	154	GLU	-1	-0.837	-0.910	24.434	-11.162	-11.162	0.000	0.000	0.000
114	A	155	PHE	0	-0.011	-0.008	25.958	-0.417	-0.417	0.000	0.000	0.000
115	A	156	THR	0	-0.022	-0.017	27.229	-0.219	-0.219	0.000	0.000	0.000
116	A	157	THR	0	-0.028	-0.024	23.437	-0.137	-0.137	0.000	0.000	0.000
117	A	158	HIS	0	0.060	0.033	20.481	-0.779	-0.779	0.000	0.000	0.000
118	A	159	ILE	0	-0.035	-0.004	22.645	-0.431	-0.431	0.000	0.000	0.000
119	A	160	LEU	0	0.004	-0.001	23.943	-0.248	-0.248	0.000	0.000	0.000
120	A	161	GLU	-1	-0.881	-0.943	19.136	-12.885	-12.885	0.000	0.000	0.000
121	A	162	VAL	0	-0.029	-0.004	18.844	-0.668	-0.668	0.000	0.000	0.000
122	A	163	ILE	0	0.007	-0.001	19.507	-0.496	-0.496	0.000	0.000	0.000
123	A	164	ASN	0	-0.018	-0.015	18.332	-0.094	-0.094	0.000	0.000	0.000
124	A	165	ALA	0	0.020	0.012	15.038	-0.486	-0.486	0.000	0.000	0.000
125	A	166	HIS	0	0.006	-0.021	15.633	-0.842	-0.842	0.000	0.000	0.000
126	A	167	MET	0	-0.042	-0.009	17.683	-0.017	-0.017	0.000	0.000	0.000
127	A	168	VAL	0	-0.028	-0.012	13.137	-0.204	-0.204	0.000	0.000	0.000
128	A	169	LEU	0	-0.013	-0.014	11.549	-0.792	-0.792	0.000	0.000	0.000
129	A	170	SER	0	-0.011	0.006	14.361	-0.532	-0.532	0.000	0.000	0.000
130	A	171	LYS	1	0.911	0.955	16.793	13.387	13.387	0.000	0.000	0.000
131	A	172	ALA	0	-0.043	-0.002	12.423	-0.981	-0.981	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:42:ARG)