FMO DATABASE

FMODB ID: VR981

Calculation Name: 2J4B-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2J4B

Chain ID: A

ChEMBL ID:

UniProt ID: Q8SQS4

Base Structure: X-ray

Registration Date: 2023-06-19

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	-1315765.606111
FMO2-HF: Nuclear repulsion	1260872.201666
FMO2-HF: Total energy	-54893.404445
FMO2-MP2: Total energy	-55057.124803

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:18:GLN)

Summations of interaction energy for fragment #1(A:18:GLN)

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.
-0.65	4.489	0.53	-2.302	-3.368	-0.005

Interaction energy analysis for fragmet #1(A:18:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.063 / q_NPA : 0.030

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

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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	20	GLU	-1	-0.721	-0.840	3.791	-0.912	1.286	-0.011	-1.025	-1.162	0.004
4	A	21	THR	0	0.024	-0.001	2.792	-1.832	0.129	0.527	-0.893	-1.596	-0.009
5	A	22	SER	0	-0.026	-0.023	3.174	0.032	0.943	0.015	-0.377	-0.549	0.000
6	A	23	TYR	0	-0.050	-0.044	5.414	0.733	0.733	0.000	0.000	0.000	0.000
7	A	24	VAL	0	0.036	0.021	7.941	0.175	0.175	0.000	0.000	0.000	0.000
8	A	25	SER	0	-0.011	0.002	7.917	0.161	0.161	0.000	0.000	0.000	0.000
9	A	26	LEU	0	-0.006	-0.006	9.399	0.186	0.186	0.000	0.000	0.000	0.000
10	A	27	LYS	1	0.832	0.917	11.330	0.343	0.343	0.000	0.000	0.000	0.000
11	A	28	THR	0	-0.005	-0.009	12.514	0.110	0.110	0.000	0.000	0.000	0.000
12	A	29	TRP	0	0.023	0.022	13.768	0.066	0.066	0.000	0.000	0.000	0.000
13	A	30	ILE	0	-0.017	-0.012	15.366	0.074	0.074	0.000	0.000	0.000	0.000
14	A	31	GLU	-1	-0.897	-0.952	17.026	-0.232	-0.232	0.000	0.000	0.000	0.000
15	A	32	ASP	-1	-0.891	-0.951	18.074	-0.393	-0.393	0.000	0.000	0.000	0.000
16	A	33	SER	0	-0.118	-0.061	19.756	0.035	0.035	0.000	0.000	0.000	0.000
17	A	34	LEU	0	0.020	-0.006	21.406	0.034	0.034	0.000	0.000	0.000	0.000
18	A	35	ASP	-1	-0.815	-0.915	24.670	-0.219	-0.219	0.000	0.000	0.000	0.000
19	A	36	LEU	0	-0.060	-0.029	26.341	0.007	0.007	0.000	0.000	0.000	0.000
20	A	37	PHE	0	-0.007	-0.019	23.173	0.007	0.007	0.000	0.000	0.000	0.000
21	A	38	LYS	1	0.831	0.925	21.369	0.257	0.257	0.000	0.000	0.000	0.000
22	A	39	ASN	0	-0.043	-0.028	22.545	0.012	0.012	0.000	0.000	0.000	0.000
23	A	40	ASP	-1	-0.816	-0.897	23.512	-0.203	-0.203	0.000	0.000	0.000	0.000
24	A	41	LEU	0	-0.035	-0.013	18.057	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	42	LEU	0	0.042	0.019	18.549	-0.030	-0.030	0.000	0.000	0.000	0.000
26	A	43	PRO	0	-0.032	-0.019	19.101	0.003	0.003	0.000	0.000	0.000	0.000
27	A	44	LEU	0	0.011	0.012	14.370	0.027	0.027	0.000	0.000	0.000	0.000
28	A	45	LEU	0	0.023	0.001	13.596	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	46	TYR	0	0.029	0.013	15.083	0.045	0.045	0.000	0.000	0.000	0.000
30	A	47	PRO	0	-0.001	0.002	16.635	0.046	0.046	0.000	0.000	0.000	0.000
31	A	48	LEU	0	0.010	0.009	9.456	0.024	0.024	0.000	0.000	0.000	0.000
32	A	49	PHE	0	-0.006	0.008	11.798	0.011	0.011	0.000	0.000	0.000	0.000
33	A	50	ILE	0	-0.002	0.011	13.010	0.124	0.124	0.000	0.000	0.000	0.000
34	A	51	HIS	0	-0.006	-0.007	12.225	0.095	0.095	0.000	0.000	0.000	0.000
35	A	52	ILE	0	-0.012	0.003	7.561	0.058	0.058	0.000	0.000	0.000	0.000
36	A	53	TYR	0	-0.031	-0.027	9.834	0.330	0.330	0.000	0.000	0.000	0.000
37	A	54	PHE	0	0.017	-0.011	12.377	0.125	0.125	0.000	0.000	0.000	0.000
38	A	55	ASP	-1	-0.768	-0.874	8.751	0.299	0.299	0.000	0.000	0.000	0.000
39	A	56	LEU	0	-0.051	-0.011	6.585	0.255	0.255	0.000	0.000	0.000	0.000
40	A	57	ILE	0	0.004	0.014	10.273	0.081	0.081	0.000	0.000	0.000	0.000
41	A	58	GLN	0	-0.081	-0.035	12.620	-0.077	-0.077	0.000	0.000	0.000	0.000
42	A	59	GLN	0	-0.075	-0.054	6.818	0.490	0.490	0.000	0.000	0.000	0.000
43	A	60	ASN	0	-0.040	-0.022	11.948	0.037	0.037	0.000	0.000	0.000	0.000
44	A	61	LYS	1	0.819	0.909	6.498	-4.524	-4.524	0.000	0.000	0.000	0.000
45	A	62	THR	0	0.010	-0.014	11.830	0.081	0.081	0.000	0.000	0.000	0.000
46	A	63	ASP	-1	-0.854	-0.928	13.741	0.840	0.840	0.000	0.000	0.000	0.000
47	A	64	GLU	-1	-0.763	-0.859	6.842	4.455	4.455	0.000	0.000	0.000	0.000
48	A	65	ALA	0	-0.013	0.002	10.483	-0.109	-0.109	0.000	0.000	0.000	0.000
49	A	66	LYS	1	0.845	0.907	11.929	-0.940	-0.940	0.000	0.000	0.000	0.000
50	A	67	GLU	-1	-0.891	-0.933	11.117	1.398	1.398	0.000	0.000	0.000	0.000
51	A	68	PHE	0	-0.029	-0.018	8.378	-0.192	-0.192	0.000	0.000	0.000	0.000
52	A	69	PHE	0	-0.022	-0.021	11.218	-0.227	-0.227	0.000	0.000	0.000	0.000
53	A	70	GLU	-1	-0.806	-0.919	14.559	0.238	0.238	0.000	0.000	0.000	0.000
54	A	71	LYS	1	0.756	0.893	9.474	-1.490	-1.490	0.000	0.000	0.000	0.000
55	A	72	TYR	0	-0.046	-0.041	9.572	-0.216	-0.216	0.000	0.000	0.000	0.000
56	A	73	ARG	1	0.738	0.836	15.002	-0.331	-0.331	0.000	0.000	0.000	0.000
57	A	74	GLY	0	-0.007	-0.012	18.048	-0.035	-0.035	0.000	0.000	0.000	0.000
58	A	75	ASP	-1	-0.776	-0.860	15.260	-0.119	-0.119	0.000	0.000	0.000	0.000
59	A	76	HIS	1	0.843	0.923	15.496	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	77	TYR	0	0.058	0.041	20.892	0.032	0.032	0.000	0.000	0.000	0.000
61	A	78	ASN	0	0.031	0.017	23.464	0.012	0.012	0.000	0.000	0.000	0.000
62	A	79	LYS	1	0.775	0.877	22.709	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	80	SER	0	0.023	0.002	24.128	0.017	0.017	0.000	0.000	0.000	0.000
64	A	81	GLU	-1	-0.907	-0.938	25.333	0.094	0.094	0.000	0.000	0.000	0.000
65	A	82	GLU	-1	-0.776	-0.876	23.965	0.045	0.045	0.000	0.000	0.000	0.000
66	A	83	ILE	0	-0.053	-0.017	19.113	0.026	0.026	0.000	0.000	0.000	0.000
67	A	84	LYS	1	0.899	0.929	21.985	-0.160	-0.160	0.000	0.000	0.000	0.000
68	A	85	GLN	0	-0.032	-0.009	24.647	0.006	0.006	0.000	0.000	0.000	0.000
69	A	86	PHE	0	0.021	-0.019	19.437	0.024	0.024	0.000	0.000	0.000	0.000
70	A	87	GLU	-1	-0.769	-0.841	20.319	0.274	0.274	0.000	0.000	0.000	0.000
71	A	88	SER	0	-0.076	-0.026	21.316	0.032	0.032	0.000	0.000	0.000	0.000
72	A	89	ILE	0	-0.061	-0.012	19.471	0.000	0.000	0.000	0.000	0.000	0.000
73	A	90	TYR	0	0.006	-0.004	18.116	0.043	0.043	0.000	0.000	0.000	0.000
74	A	91	THR	0	0.024	-0.006	17.820	0.078	0.078	0.000	0.000	0.000	0.000
75	A	92	VAL	0	0.088	0.024	17.213	-0.046	-0.046	0.000	0.000	0.000	0.000
76	A	93	GLN	0	-0.035	-0.013	19.602	-0.039	-0.039	0.000	0.000	0.000	0.000
77	A	94	HIS	0	0.019	0.034	21.589	0.004	0.004	0.000	0.000	0.000	0.000
78	A	95	ILE	0	0.033	0.018	16.888	-0.032	-0.032	0.000	0.000	0.000	0.000
79	A	96	HIS	0	-0.083	-0.055	20.534	-0.053	-0.053	0.000	0.000	0.000	0.000
80	A	97	GLU	-1	-0.856	-0.909	24.211	0.238	0.238	0.000	0.000	0.000	0.000
81	A	98	ASN	0	-0.032	-0.018	24.324	-0.037	-0.037	0.000	0.000	0.000	0.000
82	A	99	ASN	0	0.034	0.000	24.880	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	100	PHE	0	0.022	0.032	23.667	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	101	ALA	0	0.029	0.015	20.755	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	102	TYR	0	0.016	0.013	20.949	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	103	THR	0	-0.032	-0.031	22.499	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	104	PHE	0	-0.009	-0.001	17.619	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	105	LYS	1	0.889	0.953	16.542	-0.261	-0.261	0.000	0.000	0.000	0.000
89	A	106	ASN	0	-0.073	-0.029	18.188	0.002	0.002	0.000	0.000	0.000	0.000
90	A	107	SER	0	-0.004	-0.007	20.952	-0.008	-0.008	0.000	0.000	0.000	0.000
91	A	108	LYS	1	0.777	0.880	19.584	0.152	0.152	0.000	0.000	0.000	0.000
92	A	109	TYR	0	0.021	0.012	19.635	0.023	0.023	0.000	0.000	0.000	0.000
93	A	110	HIS	0	-0.036	-0.028	21.218	-0.025	-0.025	0.000	0.000	0.000	0.000
94	A	111	LEU	0	-0.023	-0.011	18.680	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	112	SER	0	-0.034	-0.020	23.206	0.014	0.014	0.000	0.000	0.000	0.000
96	A	113	MET	0	-0.006	0.009	18.567	-0.017	-0.017	0.000	0.000	0.000	0.000
97	A	114	GLY	0	0.028	0.017	24.773	0.013	0.013	0.000	0.000	0.000	0.000
98	A	115	ARG	1	0.899	0.929	25.107	0.186	0.186	0.000	0.000	0.000	0.000
99	A	116	TYR	0	0.003	0.001	24.597	-0.016	-0.016	0.000	0.000	0.000	0.000
100	A	117	ALA	0	0.066	0.047	22.462	-0.021	-0.021	0.000	0.000	0.000	0.000
101	A	118	PHE	0	0.020	-0.003	20.032	-0.042	-0.042	0.000	0.000	0.000	0.000
102	A	119	ASP	-1	-0.924	-0.965	19.735	-0.370	-0.370	0.000	0.000	0.000	0.000
103	A	120	LEU	0	0.014	0.013	19.925	-0.036	-0.036	0.000	0.000	0.000	0.000
104	A	121	LEU	0	0.008	0.009	14.427	-0.058	-0.058	0.000	0.000	0.000	0.000
105	A	122	ILE	0	-0.018	-0.008	15.249	-0.098	-0.098	0.000	0.000	0.000	0.000
106	A	123	ASN	0	-0.009	-0.010	15.391	-0.069	-0.069	0.000	0.000	0.000	0.000
107	A	124	PHE	0	-0.001	0.007	11.140	-0.089	-0.089	0.000	0.000	0.000	0.000
108	A	125	LEU	0	-0.026	-0.029	10.022	-0.167	-0.167	0.000	0.000	0.000	0.000
109	A	126	GLU	-1	-0.945	-0.972	10.791	-0.694	-0.694	0.000	0.000	0.000	0.000
110	A	127	GLU	-1	-0.884	-0.925	12.933	-0.807	-0.807	0.000	0.000	0.000	0.000
111	A	128	ARG	1	0.816	0.899	9.025	1.034	1.034	0.000	0.000	0.000	0.000
112	A	129	ASN	0	-0.047	-0.018	8.294	-0.287	-0.287	0.000	0.000	0.000	0.000
113	A	130	LEU	0	0.043	0.042	5.609	-0.283	-0.283	0.000	0.000	0.000	0.000
114	A	131	THR	0	-0.019	-0.038	5.644	0.182	0.182	0.000	0.000	0.000	0.000
115	A	132	TYR	0	-0.042	-0.043	4.747	0.121	0.190	-0.001	-0.007	-0.061	0.000
116	A	133	ILE	0	0.043	0.012	6.595	0.352	0.352	0.000	0.000	0.000	0.000
117	A	134	LEU	0	0.049	0.032	9.070	0.256	0.256	0.000	0.000	0.000	0.000
118	A	135	LYS	1	0.877	0.951	9.551	0.248	0.248	0.000	0.000	0.000	0.000
119	A	136	ILE	0	-0.023	-0.011	10.133	0.128	0.128	0.000	0.000	0.000	0.000
120	A	137	LEU	0	0.005	-0.004	12.647	0.094	0.094	0.000	0.000	0.000	0.000
121	A	138	ASN	0	-0.025	-0.015	14.528	0.106	0.106	0.000	0.000	0.000	0.000
122	A	139	GLN	0	-0.029	-0.015	14.371	0.057	0.057	0.000	0.000	0.000	0.000
123	A	140	HIS	0	0.025	0.017	14.112	0.033	0.033	0.000	0.000	0.000	0.000
124	A	141	LEU	0	-0.015	0.015	15.419	0.017	0.017	0.000	0.000	0.000	0.000
125	A	142	ASP	-1	-0.878	-0.926	18.836	-0.125	-0.125	0.000	0.000	0.000	0.000
126	A	143	ILE	0	0.024	0.009	17.824	0.005	0.005	0.000	0.000	0.000	0.000
127	A	144	LYS	1	0.928	0.968	22.521	0.131	0.131	0.000	0.000	0.000	0.000
128	A	145	VAL	0	0.049	0.029	23.793	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	146	TYR	0	-0.031	-0.017	26.271	0.021	0.021	0.000	0.000	0.000	0.000
130	A	147	VAL	0	0.014	-0.010	28.978	-0.016	-0.016	0.000	0.000	0.000	0.000
131	A	148	GLY	0	0.019	0.025	31.276	0.006	0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:GLN)