FMO DATABASE

FMODB ID: QV7JY

Calculation Name: 2JH2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2JH2

Chain ID: A

ChEMBL ID:

UniProt ID: Q0TR53

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	133
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1056311.212716
FMO2-HF: Nuclear repulsion	1007621.809178
FMO2-HF: Total energy	-48689.403538
FMO2-MP2: Total energy	-48834.532167

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:7:GLU)

Summations of interaction energy for fragment #1(A:7:GLU)

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.
182.196	185.383	0.085	-1.289	-1.982	0.002

Interaction energy analysis for fragmet #1(A:7:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.992 / q_NPA : -1.001

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	9	THR	0	-0.006	0.003	3.405	-1.392	0.616	0.013	-0.820	-1.201	0.002
4	A	10	GLY	0	0.069	0.027	5.587	-1.097	-1.097	0.000	0.000	0.000	0.000
5	A	11	SER	0	-0.041	-0.013	9.347	0.425	0.425	0.000	0.000	0.000	0.000
6	A	12	VAL	0	0.012	0.012	12.635	-0.243	-0.243	0.000	0.000	0.000	0.000
7	A	13	SER	0	-0.052	-0.019	16.101	-0.033	-0.033	0.000	0.000	0.000	0.000
8	A	14	LEU	0	-0.003	-0.015	19.243	-0.160	-0.160	0.000	0.000	0.000	0.000
9	A	15	GLU	-1	-0.951	-0.975	22.586	10.493	10.493	0.000	0.000	0.000	0.000
10	A	16	ALA	0	0.064	0.029	26.021	-0.181	-0.181	0.000	0.000	0.000	0.000
11	A	17	LEU	0	0.032	0.018	29.415	0.070	0.070	0.000	0.000	0.000	0.000
12	A	18	GLU	-1	-0.867	-0.925	30.143	10.107	10.107	0.000	0.000	0.000	0.000
13	A	19	GLU	-1	-0.953	-0.981	33.209	7.851	7.851	0.000	0.000	0.000	0.000
14	A	20	VAL	0	-0.005	0.012	36.049	0.005	0.005	0.000	0.000	0.000	0.000
15	A	21	GLN	0	-0.038	-0.011	38.218	-0.061	-0.061	0.000	0.000	0.000	0.000
16	A	22	VAL	0	0.012	-0.007	41.164	0.079	0.079	0.000	0.000	0.000	0.000
17	A	23	GLY	0	-0.033	-0.008	42.194	-0.155	-0.155	0.000	0.000	0.000	0.000
18	A	24	GLU	-1	-0.951	-0.976	40.028	7.346	7.346	0.000	0.000	0.000	0.000
19	A	25	ASN	0	-0.002	-0.010	36.805	-0.016	-0.016	0.000	0.000	0.000	0.000
20	A	26	LEU	0	0.034	0.014	31.788	0.001	0.001	0.000	0.000	0.000	0.000
21	A	27	GLU	-1	-0.891	-0.944	31.545	8.975	8.975	0.000	0.000	0.000	0.000
22	A	28	VAL	0	-0.037	-0.017	26.154	0.189	0.189	0.000	0.000	0.000	0.000
23	A	29	GLY	0	0.072	0.030	26.404	0.080	0.080	0.000	0.000	0.000	0.000
24	A	30	VAL	0	-0.042	-0.013	20.592	0.368	0.368	0.000	0.000	0.000	0.000
25	A	31	GLY	0	0.074	0.026	20.111	-0.280	-0.280	0.000	0.000	0.000	0.000
26	A	32	ILE	0	0.013	0.029	13.895	0.480	0.480	0.000	0.000	0.000	0.000
27	A	33	ASP	-1	-0.871	-0.927	15.303	16.070	16.070	0.000	0.000	0.000	0.000
28	A	34	GLU	-1	-0.914	-0.965	9.517	26.019	26.019	0.000	0.000	0.000	0.000
29	A	35	LEU	0	0.019	-0.005	8.775	-0.060	-0.060	0.000	0.000	0.000	0.000
30	A	36	VAL	0	-0.005	0.015	5.399	-0.229	-0.229	0.000	0.000	0.000	0.000
31	A	37	ASN	0	-0.090	-0.075	2.845	-4.535	-3.356	0.072	-0.469	-0.781	0.000
32	A	38	ALA	0	-0.018	-0.011	6.467	0.515	0.515	0.000	0.000	0.000	0.000
33	A	39	GLU	-1	-0.872	-0.925	9.040	18.727	18.727	0.000	0.000	0.000	0.000
34	A	40	ALA	0	0.012	0.013	12.632	0.261	0.261	0.000	0.000	0.000	0.000
35	A	41	PHE	0	0.006	0.009	14.355	-0.854	-0.854	0.000	0.000	0.000	0.000
36	A	42	ALA	0	-0.034	-0.024	16.224	-1.073	-1.073	0.000	0.000	0.000	0.000
37	A	43	TYR	0	-0.009	-0.020	15.843	1.184	1.184	0.000	0.000	0.000	0.000
38	A	44	ASP	-1	-0.821	-0.881	16.910	13.077	13.077	0.000	0.000	0.000	0.000
39	A	45	PHE	0	0.062	0.032	17.303	0.779	0.779	0.000	0.000	0.000	0.000
40	A	46	THR	0	-0.019	-0.015	19.530	-0.689	-0.689	0.000	0.000	0.000	0.000
41	A	47	LEU	0	0.043	0.031	22.119	0.338	0.338	0.000	0.000	0.000	0.000
42	A	48	ASN	0	-0.060	-0.048	22.790	-0.561	-0.561	0.000	0.000	0.000	0.000
43	A	49	TYR	0	0.014	0.015	26.496	0.030	0.030	0.000	0.000	0.000	0.000
44	A	50	ASP	-1	-0.830	-0.919	29.754	8.433	8.433	0.000	0.000	0.000	0.000
45	A	51	GLU	-1	-0.860	-0.944	32.888	8.454	8.454	0.000	0.000	0.000	0.000
46	A	52	ASN	0	-0.134	-0.058	35.170	-0.415	-0.415	0.000	0.000	0.000	0.000
47	A	53	ALA	0	-0.041	-0.004	35.491	-0.210	-0.210	0.000	0.000	0.000	0.000
48	A	54	PHE	0	0.005	-0.017	33.181	-0.079	-0.079	0.000	0.000	0.000	0.000
49	A	55	GLU	-1	-0.894	-0.939	36.195	7.515	7.515	0.000	0.000	0.000	0.000
50	A	56	TYR	0	-0.068	-0.037	30.930	0.021	0.021	0.000	0.000	0.000	0.000
51	A	57	VAL	0	-0.016	0.000	34.500	-0.219	-0.219	0.000	0.000	0.000	0.000
52	A	58	GLU	-1	-0.950	-0.986	33.878	8.132	8.132	0.000	0.000	0.000	0.000
53	A	59	ALA	0	-0.047	-0.032	28.603	0.200	0.200	0.000	0.000	0.000	0.000
54	A	60	ILE	0	0.012	0.022	30.417	-0.128	-0.128	0.000	0.000	0.000	0.000
55	A	61	SER	0	-0.026	-0.026	28.068	0.297	0.297	0.000	0.000	0.000	0.000
56	A	62	ASP	-1	-0.822	-0.922	27.542	9.856	9.856	0.000	0.000	0.000	0.000
57	A	63	ASP	-1	-0.953	-0.979	28.999	9.927	9.927	0.000	0.000	0.000	0.000
58	A	64	GLY	0	-0.010	0.017	27.868	-0.210	-0.210	0.000	0.000	0.000	0.000
59	A	65	VAL	0	-0.052	-0.031	23.393	0.244	0.244	0.000	0.000	0.000	0.000
60	A	66	PHE	0	-0.036	-0.023	25.297	-0.584	-0.584	0.000	0.000	0.000	0.000
61	A	67	VAL	0	0.058	0.026	25.104	0.504	0.504	0.000	0.000	0.000	0.000
62	A	68	ASN	0	-0.065	-0.025	26.231	-0.302	-0.302	0.000	0.000	0.000	0.000
63	A	69	ALA	0	0.056	0.035	26.547	0.384	0.384	0.000	0.000	0.000	0.000
64	A	70	LYS	1	0.935	0.959	28.259	-9.720	-9.720	0.000	0.000	0.000	0.000
65	A	71	LYS	1	0.890	0.940	28.840	-8.007	-8.007	0.000	0.000	0.000	0.000
66	A	72	ILE	0	-0.114	-0.054	26.730	-0.165	-0.165	0.000	0.000	0.000	0.000
67	A	73	GLU	-1	-0.887	-0.945	29.802	9.421	9.421	0.000	0.000	0.000	0.000
68	A	74	ASP	-1	-0.866	-0.921	31.983	8.269	8.269	0.000	0.000	0.000	0.000
69	A	75	GLY	0	0.084	0.041	31.496	0.044	0.044	0.000	0.000	0.000	0.000
70	A	76	LYS	1	0.833	0.922	25.783	-10.226	-10.226	0.000	0.000	0.000	0.000
71	A	77	VAL	0	-0.004	-0.006	27.168	-0.282	-0.282	0.000	0.000	0.000	0.000
72	A	78	ARG	1	0.714	0.848	18.171	-13.457	-13.457	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.024	-0.028	23.188	-0.525	-0.525	0.000	0.000	0.000	0.000
74	A	80	LEU	0	-0.030	-0.002	21.668	0.603	0.603	0.000	0.000	0.000	0.000
75	A	81	VAL	0	0.039	0.000	20.921	-0.503	-0.503	0.000	0.000	0.000	0.000
76	A	82	SER	0	0.004	0.005	20.347	0.615	0.615	0.000	0.000	0.000	0.000
77	A	83	SER	0	0.009	-0.016	21.007	-0.776	-0.776	0.000	0.000	0.000	0.000
78	A	84	LEU	0	-0.059	-0.032	22.672	-0.166	-0.166	0.000	0.000	0.000	0.000
79	A	85	THR	0	-0.019	-0.015	25.013	-0.263	-0.263	0.000	0.000	0.000	0.000
80	A	86	GLY	0	-0.043	-0.009	22.566	-0.169	-0.169	0.000	0.000	0.000	0.000
81	A	87	GLU	-1	-0.947	-0.962	21.573	13.213	13.213	0.000	0.000	0.000	0.000
82	A	88	PRO	0	-0.005	0.008	16.623	-0.172	-0.172	0.000	0.000	0.000	0.000
83	A	89	LEU	0	-0.048	-0.036	17.674	-0.641	-0.641	0.000	0.000	0.000	0.000
84	A	90	PRO	0	0.009	0.028	17.500	0.953	0.953	0.000	0.000	0.000	0.000
85	A	91	ALA	0	-0.008	-0.010	15.553	0.008	0.008	0.000	0.000	0.000	0.000
86	A	92	LYS	1	0.730	0.830	16.457	-17.105	-17.105	0.000	0.000	0.000	0.000
87	A	93	GLU	-1	-0.928	-0.963	19.833	11.867	11.867	0.000	0.000	0.000	0.000
88	A	94	VAL	0	-0.053	-0.003	22.021	0.468	0.468	0.000	0.000	0.000	0.000
89	A	95	LEU	0	-0.032	-0.001	19.300	-0.148	-0.148	0.000	0.000	0.000	0.000
90	A	96	ALA	0	-0.016	-0.031	23.795	-0.406	-0.406	0.000	0.000	0.000	0.000
91	A	97	LYS	1	0.847	0.941	25.645	-9.430	-9.430	0.000	0.000	0.000	0.000
92	A	98	VAL	0	-0.042	-0.039	26.605	-0.207	-0.207	0.000	0.000	0.000	0.000
93	A	99	VAL	0	0.005	0.010	29.357	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	100	LEU	0	-0.021	-0.013	30.216	-0.061	-0.061	0.000	0.000	0.000	0.000
95	A	101	ARG	1	0.864	0.939	34.287	-7.395	-7.395	0.000	0.000	0.000	0.000
96	A	102	ALA	0	-0.015	0.007	37.835	0.064	0.064	0.000	0.000	0.000	0.000
97	A	103	GLU	-1	-0.862	-0.941	38.934	6.977	6.977	0.000	0.000	0.000	0.000
98	A	104	ALA	0	-0.059	-0.033	40.247	-0.244	-0.244	0.000	0.000	0.000	0.000
99	A	105	LYS	1	0.895	0.946	40.127	-6.674	-6.674	0.000	0.000	0.000	0.000
100	A	106	ALA	0	-0.008	0.000	37.180	-0.025	-0.025	0.000	0.000	0.000	0.000
101	A	107	GLU	-1	-0.950	-0.968	37.370	7.791	7.791	0.000	0.000	0.000	0.000
102	A	108	GLY	0	-0.025	-0.010	33.193	0.053	0.053	0.000	0.000	0.000	0.000
103	A	109	SER	0	-0.008	0.004	32.298	0.272	0.272	0.000	0.000	0.000	0.000
104	A	110	ASN	0	-0.035	-0.044	25.632	0.062	0.062	0.000	0.000	0.000	0.000
105	A	111	LEU	0	0.007	0.007	26.808	-0.166	-0.166	0.000	0.000	0.000	0.000
106	A	112	SER	0	0.043	0.015	22.270	0.299	0.299	0.000	0.000	0.000	0.000
107	A	113	VAL	0	0.000	0.017	18.806	-0.323	-0.323	0.000	0.000	0.000	0.000
108	A	114	THR	0	0.015	0.005	18.309	0.543	0.543	0.000	0.000	0.000	0.000
109	A	115	ASN	0	-0.052	-0.038	16.635	-0.430	-0.430	0.000	0.000	0.000	0.000
110	A	116	SER	0	0.056	0.034	14.591	-0.628	-0.628	0.000	0.000	0.000	0.000
111	A	117	SER	0	-0.028	-0.002	12.525	1.098	1.098	0.000	0.000	0.000	0.000
112	A	118	VAL	0	0.048	0.013	10.673	-1.105	-1.105	0.000	0.000	0.000	0.000
113	A	119	GLY	0	-0.004	0.008	11.878	1.042	1.042	0.000	0.000	0.000	0.000
114	A	120	ASP	-1	-0.705	-0.853	9.186	23.848	23.848	0.000	0.000	0.000	0.000
115	A	121	GLY	0	-0.002	-0.007	12.386	-1.013	-1.013	0.000	0.000	0.000	0.000
116	A	122	GLU	-1	-1.023	-1.007	10.205	23.110	23.110	0.000	0.000	0.000	0.000
117	A	123	GLY	0	-0.047	-0.012	13.621	-0.866	-0.866	0.000	0.000	0.000	0.000
118	A	124	LEU	0	-0.095	-0.042	8.546	-0.285	-0.285	0.000	0.000	0.000	0.000
119	A	125	VAL	0	0.011	-0.003	11.117	-0.063	-0.063	0.000	0.000	0.000	0.000
120	A	126	HIS	1	0.812	0.883	6.195	-27.641	-27.641	0.000	0.000	0.000	0.000
121	A	127	GLU	-1	-0.920	-0.955	8.943	18.531	18.531	0.000	0.000	0.000	0.000
122	A	128	ILE	0	-0.050	-0.011	8.420	2.170	2.170	0.000	0.000	0.000	0.000
123	A	129	ALA	0	-0.031	-0.020	10.442	-1.348	-1.348	0.000	0.000	0.000	0.000
124	A	130	GLY	0	0.056	0.022	12.396	-0.446	-0.446	0.000	0.000	0.000	0.000
125	A	131	THR	0	-0.047	-0.030	16.090	0.333	0.333	0.000	0.000	0.000	0.000
126	A	132	GLU	-1	-0.904	-0.955	18.851	12.090	12.090	0.000	0.000	0.000	0.000
127	A	133	LYS	1	0.822	0.912	22.591	-10.308	-10.308	0.000	0.000	0.000	0.000
128	A	134	THR	0	-0.004	0.004	25.828	-0.070	-0.070	0.000	0.000	0.000	0.000
129	A	135	VAL	0	-0.050	-0.019	29.518	0.037	0.037	0.000	0.000	0.000	0.000
130	A	136	ASN	0	-0.006	-0.002	32.576	0.054	0.054	0.000	0.000	0.000	0.000
131	A	137	ILE	0	0.009	0.013	36.220	-0.022	-0.022	0.000	0.000	0.000	0.000
132	A	138	ILE	0	0.032	-0.004	38.795	-0.195	-0.195	0.000	0.000	0.000	0.000
133	A	139	GLU	-1	-0.978	-0.992	42.146	6.383	6.383	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLU)