FMO DATABASE

FMODB ID: 2J1KR

Calculation Name: 2QJX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QJX

Chain ID: A

ChEMBL ID:

UniProt ID: P40013

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:

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	117
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1110223.394908
FMO2-HF: Nuclear repulsion	1060475.559886
FMO2-HF: Total energy	-49747.835022
FMO2-MP2: Total energy	-49891.60127

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:8:SER)

Summations of interaction energy for fragment #1(A:8:SER)

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.
-58.886	-58.583	30.846	-17.242	-13.906	-0.087

Interaction energy analysis for fragmet #1(A:8:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.047

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	10	THR	0	0.075	0.031	2.926	-3.648	-0.496	0.306	-1.538	-1.919	0.009
4	A	11	GLU	-1	-0.815	-0.851	1.665	-54.085	-58.568	30.502	-15.187	-10.831	-0.096
5	A	12	LEU	0	-0.071	-0.042	3.043	0.114	1.237	0.036	-0.397	-0.762	0.000
6	A	13	LEU	0	0.021	0.009	4.992	0.101	0.236	-0.001	-0.012	-0.122	0.000
7	A	14	THR	0	-0.007	-0.002	6.987	-0.007	-0.007	0.000	0.000	0.000	0.000
8	A	15	TRP	0	-0.024	-0.018	7.489	0.022	0.022	0.000	0.000	0.000	0.000
9	A	16	LEU	0	0.021	0.003	9.012	0.118	0.118	0.000	0.000	0.000	0.000
10	A	17	ASN	0	-0.024	-0.015	11.044	0.047	0.047	0.000	0.000	0.000	0.000
11	A	18	GLY	0	0.039	0.031	12.455	0.021	0.021	0.000	0.000	0.000	0.000
12	A	19	LEU	0	-0.026	-0.005	13.293	0.030	0.030	0.000	0.000	0.000	0.000
13	A	20	LEU	0	-0.038	-0.034	14.988	0.031	0.031	0.000	0.000	0.000	0.000
14	A	21	ASN	0	0.000	0.002	16.762	0.025	0.025	0.000	0.000	0.000	0.000
15	A	22	LEU	0	-0.043	-0.006	15.046	0.036	0.036	0.000	0.000	0.000	0.000
16	A	23	ASN	0	0.030	-0.005	15.635	-0.019	-0.019	0.000	0.000	0.000	0.000
17	A	24	TYR	0	0.005	0.003	12.830	0.028	0.028	0.000	0.000	0.000	0.000
18	A	25	LYS	1	0.892	0.933	12.016	-0.221	-0.221	0.000	0.000	0.000	0.000
19	A	26	LYS	1	0.844	0.906	10.249	-0.407	-0.407	0.000	0.000	0.000	0.000
20	A	27	ILE	0	0.011	0.011	6.485	-0.061	-0.061	0.000	0.000	0.000	0.000
21	A	28	GLU	-1	-0.798	-0.901	9.944	0.758	0.758	0.000	0.000	0.000	0.000
22	A	29	GLU	-1	-0.765	-0.871	13.106	0.343	0.343	0.000	0.000	0.000	0.000
23	A	30	CYS	0	-0.058	-0.031	12.084	-0.072	-0.072	0.000	0.000	0.000	0.000
24	A	31	GLY	0	0.040	0.013	14.600	-0.023	-0.023	0.000	0.000	0.000	0.000
25	A	32	THR	0	0.017	0.024	16.614	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	33	GLY	0	0.019	0.011	18.131	-0.032	-0.032	0.000	0.000	0.000	0.000
27	A	34	ALA	0	0.014	0.018	19.388	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	35	ALA	0	0.055	0.020	15.021	-0.022	-0.022	0.000	0.000	0.000	0.000
29	A	36	TYR	0	-0.016	-0.045	12.631	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	37	CYS	0	-0.048	-0.013	16.840	-0.025	-0.025	0.000	0.000	0.000	0.000
31	A	38	GLN	0	0.022	0.002	18.942	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	39	ILE	0	-0.011	0.018	12.988	-0.022	-0.022	0.000	0.000	0.000	0.000
33	A	40	MET	0	-0.001	0.002	17.110	-0.021	-0.021	0.000	0.000	0.000	0.000
34	A	41	ASP	-1	-0.772	-0.845	19.808	0.019	0.019	0.000	0.000	0.000	0.000
35	A	42	SER	0	-0.041	-0.033	18.325	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	43	ILE	0	-0.038	-0.010	16.838	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	44	TYR	0	-0.037	-0.045	21.059	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	45	GLY	0	0.039	0.040	24.048	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.770	-0.856	25.979	0.059	0.059	0.000	0.000	0.000	0.000
40	A	47	LEU	0	-0.003	0.001	23.194	0.010	0.010	0.000	0.000	0.000	0.000
41	A	48	PRO	0	-0.011	0.006	26.692	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	49	MET	0	0.086	0.032	22.700	0.014	0.014	0.000	0.000	0.000	0.000
43	A	50	ASN	0	-0.033	-0.015	27.059	0.003	0.003	0.000	0.000	0.000	0.000
44	A	51	ARG	1	0.928	0.953	29.531	-0.068	-0.068	0.000	0.000	0.000	0.000
45	A	52	VAL	0	0.009	0.035	23.033	0.009	0.009	0.000	0.000	0.000	0.000
46	A	53	LYS	1	0.929	0.970	26.000	-0.117	-0.117	0.000	0.000	0.000	0.000
47	A	54	PHE	0	0.021	-0.019	18.837	0.016	0.016	0.000	0.000	0.000	0.000
48	A	55	ASN	0	-0.014	-0.006	22.152	0.020	0.020	0.000	0.000	0.000	0.000
49	A	56	ALA	0	-0.002	0.012	23.774	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	57	THR	0	-0.019	-0.018	23.551	0.016	0.016	0.000	0.000	0.000	0.000
51	A	58	ALA	0	-0.003	0.007	25.460	0.008	0.008	0.000	0.000	0.000	0.000
52	A	59	GLU	-1	-0.878	-0.947	24.127	0.225	0.225	0.000	0.000	0.000	0.000
53	A	60	TYR	0	0.025	-0.001	26.069	0.002	0.002	0.000	0.000	0.000	0.000
54	A	61	GLU	-1	-0.846	-0.941	26.710	0.138	0.138	0.000	0.000	0.000	0.000
55	A	62	PHE	0	0.043	0.013	22.043	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	63	GLN	0	-0.004	0.002	24.098	0.003	0.003	0.000	0.000	0.000	0.000
57	A	64	THR	0	-0.027	-0.009	26.242	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	65	ASN	0	-0.014	-0.007	22.554	-0.027	-0.027	0.000	0.000	0.000	0.000
59	A	66	TYR	0	0.028	-0.018	18.145	0.004	0.004	0.000	0.000	0.000	0.000
60	A	67	LYS	1	0.963	0.996	23.619	-0.151	-0.151	0.000	0.000	0.000	0.000
61	A	68	ILE	0	-0.017	0.012	24.980	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	69	LEU	0	0.013	-0.005	18.816	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	70	GLN	0	-0.022	-0.021	23.164	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	71	SER	0	-0.018	-0.019	24.998	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	72	CYS	0	-0.096	-0.025	23.306	-0.014	-0.014	0.000	0.000	0.000	0.000
66	A	73	PHE	0	0.031	-0.007	18.245	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	74	SER	0	-0.003	0.013	24.415	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.832	0.898	27.127	-0.084	-0.084	0.000	0.000	0.000	0.000
69	A	76	HIS	1	0.796	0.877	25.010	-0.076	-0.076	0.000	0.000	0.000	0.000
70	A	77	GLY	0	0.057	0.050	26.914	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	78	ILE	0	-0.089	-0.045	20.758	0.005	0.005	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.868	-0.942	23.827	0.139	0.139	0.000	0.000	0.000	0.000
73	A	80	LYS	1	0.792	0.917	15.786	-0.426	-0.426	0.000	0.000	0.000	0.000
74	A	81	THR	0	0.046	0.017	19.543	0.003	0.003	0.000	0.000	0.000	0.000
75	A	82	VAL	0	0.027	0.004	18.868	0.043	0.043	0.000	0.000	0.000	0.000
76	A	83	TYR	0	0.016	0.016	17.827	-0.025	-0.025	0.000	0.000	0.000	0.000
77	A	84	VAL	0	0.066	0.028	19.556	0.032	0.032	0.000	0.000	0.000	0.000
78	A	85	ASP	-1	-0.827	-0.906	20.887	0.312	0.312	0.000	0.000	0.000	0.000
79	A	86	LYS	1	0.849	0.915	17.288	-0.321	-0.321	0.000	0.000	0.000	0.000
80	A	87	LEU	0	-0.040	-0.011	14.688	0.034	0.034	0.000	0.000	0.000	0.000
81	A	88	ILE	0	0.027	0.018	17.284	0.014	0.014	0.000	0.000	0.000	0.000
82	A	89	ARG	1	0.949	0.980	19.279	-0.303	-0.303	0.000	0.000	0.000	0.000
83	A	90	CYS	0	-0.063	-0.010	16.134	0.000	0.000	0.000	0.000	0.000	0.000
84	A	91	LYS	1	0.889	0.942	14.249	-0.557	-0.557	0.000	0.000	0.000	0.000
85	A	92	PHE	0	0.040	0.007	5.490	0.086	0.086	0.000	0.000	0.000	0.000
86	A	93	GLN	0	-0.028	-0.037	8.314	0.181	0.181	0.000	0.000	0.000	0.000
87	A	94	ASP	-1	-0.764	-0.872	10.143	0.747	0.747	0.000	0.000	0.000	0.000
88	A	95	ASN	0	0.017	0.006	11.696	-0.049	-0.049	0.000	0.000	0.000	0.000
89	A	96	LEU	0	-0.027	0.004	3.817	-0.106	0.054	0.003	-0.043	-0.121	0.000
90	A	97	GLU	-1	-0.845	-0.912	7.901	1.197	1.197	0.000	0.000	0.000	0.000
91	A	98	PHE	0	-0.039	-0.012	9.608	-0.104	-0.104	0.000	0.000	0.000	0.000
92	A	99	LEU	0	0.044	0.019	7.809	-0.109	-0.109	0.000	0.000	0.000	0.000
93	A	100	GLN	0	-0.035	-0.018	4.051	-1.660	-1.444	0.000	-0.065	-0.151	0.000
94	A	101	TRP	0	0.023	0.000	8.211	-0.243	-0.243	0.000	0.000	0.000	0.000
95	A	102	LEU	0	0.031	0.012	11.828	-0.137	-0.137	0.000	0.000	0.000	0.000
96	A	103	LYS	1	0.912	0.983	5.966	1.204	1.204	0.000	0.000	0.000	0.000
97	A	104	LYS	1	0.911	0.956	7.439	-1.171	-1.171	0.000	0.000	0.000	0.000
98	A	105	HIS	0	-0.017	0.016	12.270	-0.093	-0.093	0.000	0.000	0.000	0.000
99	A	106	TRP	0	0.065	-0.002	13.500	-0.055	-0.055	0.000	0.000	0.000	0.000
100	A	107	ILE	0	-0.040	-0.021	10.423	-0.034	-0.034	0.000	0.000	0.000	0.000
101	A	108	ARG	1	0.935	0.972	14.833	-0.048	-0.048	0.000	0.000	0.000	0.000
102	A	109	HIS	1	0.878	0.929	17.735	-0.042	-0.042	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.756	0.884	18.071	0.097	0.097	0.000	0.000	0.000	0.000
104	A	111	ASP	-1	-0.751	-0.834	19.819	-0.078	-0.078	0.000	0.000	0.000	0.000
105	A	112	GLU	-1	-0.881	-0.942	22.180	-0.115	-0.115	0.000	0.000	0.000	0.000
106	A	113	SER	0	-0.092	-0.047	24.553	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	114	VAL	0	0.016	0.014	23.601	-0.010	-0.010	0.000	0.000	0.000	0.000
108	A	115	TYR	0	-0.029	-0.043	20.382	0.021	0.021	0.000	0.000	0.000	0.000
109	A	116	ASP	-1	-0.817	-0.900	22.497	-0.052	-0.052	0.000	0.000	0.000	0.000
110	A	117	PRO	0	0.003	-0.016	19.673	0.018	0.018	0.000	0.000	0.000	0.000
111	A	118	ASP	-1	-0.765	-0.861	22.166	0.007	0.007	0.000	0.000	0.000	0.000
112	A	119	ALA	0	0.028	0.017	24.523	0.014	0.014	0.000	0.000	0.000	0.000
113	A	120	ARG	1	0.781	0.862	24.456	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	121	ARG	1	0.717	0.849	19.618	-0.020	-0.020	0.000	0.000	0.000	0.000
115	A	122	LYS	1	0.852	0.922	26.097	-0.032	-0.032	0.000	0.000	0.000	0.000
116	A	123	TYR	0	0.061	0.021	26.801	0.006	0.006	0.000	0.000	0.000	0.000
117	A	124	ARG	1	0.823	0.925	24.353	-0.055	-0.055	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:SER)