FMO DATABASE

FMODB ID: 72RJK

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1110478.420846
FMO2-HF: Nuclear repulsion	1060731.064012
FMO2-HF: Total energy	-49747.356834
FMO2-MP2: Total energy	-49891.148721

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.
-47.061	-53.644	38.668	-17.515	-14.573	-0.075

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 : 0.000 / q_NPA : -0.033

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	0.077	0.026	3.011	-3.707	-0.653	0.242	-1.478	-1.819	0.008
4	A	11	GLU	-1	-0.833	-0.882	1.715	-42.604	-53.611	38.412	-15.605	-11.801	-0.083
5	A	12	LEU	0	-0.057	-0.033	3.297	-0.177	0.801	0.014	-0.365	-0.628	0.000
6	A	13	LEU	0	0.019	0.015	5.001	0.113	0.240	-0.001	-0.010	-0.116	0.000
7	A	14	THR	0	-0.005	0.011	7.229	-0.040	-0.040	0.000	0.000	0.000	0.000
8	A	15	TRP	0	-0.034	-0.014	7.572	0.009	0.009	0.000	0.000	0.000	0.000
9	A	16	LEU	0	0.017	-0.004	9.017	0.111	0.111	0.000	0.000	0.000	0.000
10	A	17	ASN	0	-0.022	-0.012	11.051	0.036	0.036	0.000	0.000	0.000	0.000
11	A	18	GLY	0	0.035	0.028	12.460	0.019	0.019	0.000	0.000	0.000	0.000
12	A	19	LEU	0	-0.039	-0.013	13.295	0.027	0.027	0.000	0.000	0.000	0.000
13	A	20	LEU	0	-0.026	-0.029	14.991	0.030	0.030	0.000	0.000	0.000	0.000
14	A	21	ASN	0	0.001	-0.012	16.766	0.024	0.024	0.000	0.000	0.000	0.000
15	A	22	LEU	0	-0.065	-0.016	15.086	0.033	0.033	0.000	0.000	0.000	0.000
16	A	23	ASN	0	0.022	-0.014	15.675	-0.012	-0.012	0.000	0.000	0.000	0.000
17	A	24	TYR	0	-0.002	-0.003	12.894	0.027	0.027	0.000	0.000	0.000	0.000
18	A	25	LYS	1	0.914	0.948	12.082	-0.252	-0.252	0.000	0.000	0.000	0.000
19	A	26	LYS	1	0.929	0.957	10.210	-0.339	-0.339	0.000	0.000	0.000	0.000
20	A	27	ILE	0	0.009	0.012	6.436	-0.063	-0.063	0.000	0.000	0.000	0.000
21	A	28	GLU	-1	-0.847	-0.944	9.930	0.732	0.732	0.000	0.000	0.000	0.000
22	A	29	GLU	-1	-0.796	-0.885	13.092	0.331	0.331	0.000	0.000	0.000	0.000
23	A	30	CYS	0	-0.054	-0.029	12.116	-0.072	-0.072	0.000	0.000	0.000	0.000
24	A	31	GLY	0	0.041	0.021	14.595	-0.024	-0.024	0.000	0.000	0.000	0.000
25	A	32	THR	0	0.017	0.027	16.608	-0.036	-0.036	0.000	0.000	0.000	0.000
26	A	33	GLY	0	0.024	0.014	18.129	-0.030	-0.030	0.000	0.000	0.000	0.000
27	A	34	ALA	0	0.004	0.010	19.401	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	35	ALA	0	0.051	0.019	15.035	-0.022	-0.022	0.000	0.000	0.000	0.000
29	A	36	TYR	0	-0.011	-0.046	12.704	-0.012	-0.012	0.000	0.000	0.000	0.000
30	A	37	CYS	0	-0.029	-0.006	16.850	-0.026	-0.026	0.000	0.000	0.000	0.000
31	A	38	GLN	0	0.016	0.008	18.881	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	39	ILE	0	-0.008	0.017	12.863	-0.023	-0.023	0.000	0.000	0.000	0.000
33	A	40	MET	0	-0.001	0.018	17.116	-0.023	-0.023	0.000	0.000	0.000	0.000
34	A	41	ASP	-1	-0.769	-0.856	19.810	0.008	0.008	0.000	0.000	0.000	0.000
35	A	42	SER	0	-0.048	-0.048	18.354	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	43	ILE	0	-0.041	-0.011	16.912	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	44	TYR	0	-0.050	-0.062	20.950	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	45	GLY	0	0.026	0.032	24.049	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.781	-0.879	25.982	0.043	0.043	0.000	0.000	0.000	0.000
40	A	47	LEU	0	-0.023	-0.013	23.182	0.009	0.009	0.000	0.000	0.000	0.000
41	A	48	PRO	0	-0.024	0.000	26.698	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	49	MET	0	0.093	0.042	22.713	0.013	0.013	0.000	0.000	0.000	0.000
43	A	50	ASN	0	-0.045	-0.020	27.089	0.006	0.006	0.000	0.000	0.000	0.000
44	A	51	ARG	1	0.911	0.942	29.521	-0.057	-0.057	0.000	0.000	0.000	0.000
45	A	52	VAL	0	0.020	0.042	23.046	0.008	0.008	0.000	0.000	0.000	0.000
46	A	53	LYS	1	0.940	0.977	26.018	-0.105	-0.105	0.000	0.000	0.000	0.000
47	A	54	PHE	0	0.024	-0.018	19.186	0.016	0.016	0.000	0.000	0.000	0.000
48	A	55	ASN	0	-0.034	-0.018	22.165	0.019	0.019	0.000	0.000	0.000	0.000
49	A	56	ALA	0	0.011	0.014	23.779	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	57	THR	0	0.014	0.001	23.551	0.016	0.016	0.000	0.000	0.000	0.000
51	A	58	ALA	0	0.011	0.017	25.448	0.008	0.008	0.000	0.000	0.000	0.000
52	A	59	GLU	-1	-0.876	-0.946	24.665	0.210	0.210	0.000	0.000	0.000	0.000
53	A	60	TYR	0	0.009	-0.009	26.061	0.003	0.003	0.000	0.000	0.000	0.000
54	A	61	GLU	-1	-0.914	-0.972	26.973	0.124	0.124	0.000	0.000	0.000	0.000
55	A	62	PHE	0	0.051	0.018	22.138	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	63	GLN	0	-0.002	-0.001	24.097	0.005	0.005	0.000	0.000	0.000	0.000
57	A	64	THR	0	-0.028	-0.005	26.241	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	65	ASN	0	-0.015	-0.011	22.589	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	66	TYR	0	0.020	-0.022	18.106	0.001	0.001	0.000	0.000	0.000	0.000
60	A	67	LYS	1	0.979	1.005	23.624	-0.133	-0.133	0.000	0.000	0.000	0.000
61	A	68	ILE	0	-0.027	-0.003	24.959	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	69	LEU	0	0.008	-0.006	18.802	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	70	GLN	0	-0.002	-0.014	23.173	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	71	SER	0	-0.010	-0.006	25.007	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	72	CYS	0	-0.094	-0.013	23.734	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	73	PHE	0	0.031	-0.009	18.352	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	74	SER	0	-0.007	0.012	24.420	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.842	0.914	27.291	-0.068	-0.068	0.000	0.000	0.000	0.000
69	A	76	HIS	1	0.815	0.889	25.306	-0.056	-0.056	0.000	0.000	0.000	0.000
70	A	77	GLY	0	0.048	0.045	26.915	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	78	ILE	0	-0.085	-0.043	20.747	0.003	0.003	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.872	-0.950	23.875	0.109	0.109	0.000	0.000	0.000	0.000
73	A	80	LYS	1	0.800	0.922	15.707	-0.371	-0.371	0.000	0.000	0.000	0.000
74	A	81	THR	0	0.024	0.012	19.523	0.003	0.003	0.000	0.000	0.000	0.000
75	A	82	VAL	0	0.030	0.007	18.883	0.038	0.038	0.000	0.000	0.000	0.000
76	A	83	TYR	0	0.013	0.011	17.940	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	84	VAL	0	0.068	0.029	19.560	0.031	0.031	0.000	0.000	0.000	0.000
78	A	85	ASP	-1	-0.884	-0.953	20.887	0.278	0.278	0.000	0.000	0.000	0.000
79	A	86	LYS	1	0.907	0.963	17.309	-0.295	-0.295	0.000	0.000	0.000	0.000
80	A	87	LEU	0	-0.031	-0.005	14.675	0.032	0.032	0.000	0.000	0.000	0.000
81	A	88	ILE	0	0.023	0.014	17.283	0.014	0.014	0.000	0.000	0.000	0.000
82	A	89	ARG	1	0.946	0.978	19.278	-0.283	-0.283	0.000	0.000	0.000	0.000
83	A	90	CYS	0	-0.055	-0.013	16.141	0.001	0.001	0.000	0.000	0.000	0.000
84	A	91	LYS	1	0.967	1.004	14.032	-0.470	-0.470	0.000	0.000	0.000	0.000
85	A	92	PHE	0	0.023	0.005	5.469	0.094	0.094	0.000	0.000	0.000	0.000
86	A	93	GLN	0	-0.034	-0.027	8.178	0.138	0.138	0.000	0.000	0.000	0.000
87	A	94	ASP	-1	-0.807	-0.918	10.144	0.668	0.668	0.000	0.000	0.000	0.000
88	A	95	ASN	0	0.014	0.005	11.696	-0.052	-0.052	0.000	0.000	0.000	0.000
89	A	96	LEU	0	-0.048	-0.001	3.901	-0.089	0.049	0.002	-0.033	-0.107	0.000
90	A	97	GLU	-1	-0.841	-0.926	7.912	1.072	1.072	0.000	0.000	0.000	0.000
91	A	98	PHE	0	-0.033	-0.007	9.620	-0.109	-0.109	0.000	0.000	0.000	0.000
92	A	99	LEU	0	0.046	0.018	7.723	-0.106	-0.106	0.000	0.000	0.000	0.000
93	A	100	GLN	0	-0.048	-0.027	4.382	-1.352	-1.225	-0.001	-0.024	-0.102	0.000
94	A	101	TRP	0	0.060	0.020	8.215	-0.239	-0.239	0.000	0.000	0.000	0.000
95	A	102	LEU	0	0.032	0.013	11.830	-0.131	-0.131	0.000	0.000	0.000	0.000
96	A	103	LYS	1	0.913	0.981	6.456	1.291	1.291	0.000	0.000	0.000	0.000
97	A	104	LYS	1	0.881	0.944	6.590	-0.844	-0.844	0.000	0.000	0.000	0.000
98	A	105	HIS	0	-0.003	0.029	12.266	-0.073	-0.073	0.000	0.000	0.000	0.000
99	A	106	TRP	0	0.092	0.006	13.194	-0.053	-0.053	0.000	0.000	0.000	0.000
100	A	107	ILE	0	-0.042	-0.021	10.488	-0.032	-0.032	0.000	0.000	0.000	0.000
101	A	108	ARG	1	0.931	0.968	14.827	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	109	HIS	1	0.867	0.918	17.729	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.800	0.939	18.003	0.113	0.113	0.000	0.000	0.000	0.000
104	A	111	ASP	-1	-0.795	-0.850	19.816	-0.090	-0.090	0.000	0.000	0.000	0.000
105	A	112	GLU	-1	-0.872	-0.958	22.175	-0.123	-0.123	0.000	0.000	0.000	0.000
106	A	113	SER	0	-0.105	-0.057	24.548	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	114	VAL	0	0.022	0.012	23.599	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	115	TYR	0	-0.037	-0.056	20.351	0.020	0.020	0.000	0.000	0.000	0.000
109	A	116	ASP	-1	-0.829	-0.913	22.498	-0.051	-0.051	0.000	0.000	0.000	0.000
110	A	117	PRO	0	0.002	-0.015	19.821	0.018	0.018	0.000	0.000	0.000	0.000
111	A	118	ASP	-1	-0.780	-0.876	22.172	0.004	0.004	0.000	0.000	0.000	0.000
112	A	119	ALA	0	0.043	0.029	24.530	0.013	0.013	0.000	0.000	0.000	0.000
113	A	120	ARG	1	0.808	0.899	24.417	0.000	0.000	0.000	0.000	0.000	0.000
114	A	121	ARG	1	0.747	0.875	19.821	-0.023	-0.023	0.000	0.000	0.000	0.000
115	A	122	LYS	1	0.880	0.937	26.106	-0.028	-0.028	0.000	0.000	0.000	0.000
116	A	123	TYR	0	0.038	0.011	26.840	0.005	0.005	0.000	0.000	0.000	0.000
117	A	124	ARG	1	0.854	0.933	23.894	-0.056	-0.056	0.000	0.000	0.000	0.000

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