FMO DATABASE

FMODB ID: JQ949

Calculation Name: 2F9H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2F9H

Chain ID: A

ChEMBL ID:

UniProt ID: Q831B0

Base Structure: X-ray

Registration Date: 2023-09-23

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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1002120.640649
FMO2-HF: Nuclear repulsion	955733.322609
FMO2-HF: Total energy	-46387.318039
FMO2-MP2: Total energy	-46524.30377

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:3:TRP)

Summations of interaction energy for fragment #1(A:3:TRP)

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.
-29.649	-28.676	19.076	-8.65	-11.398	-0.048

Interaction energy analysis for fragmet #1(A:3:TRP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.002 / q_NPA : -0.003

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	5	MET	0	-0.013	0.015	2.023	-3.215	0.163	5.118	-2.718	-5.778	0.001
4	A	6	GLN	0	-0.074	-0.044	3.854	2.434	2.663	0.006	-0.020	-0.215	0.000
5	A	7	ALA	0	-0.001	0.019	7.375	-0.048	-0.048	0.000	0.000	0.000	0.000
6	A	8	THR	0	-0.031	-0.032	10.410	0.256	0.256	0.000	0.000	0.000	0.000
7	A	9	VAL	0	-0.011	0.004	13.817	0.026	0.026	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.009	-0.013	17.158	0.087	0.087	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.870	-0.921	19.611	-0.568	-0.568	0.000	0.000	0.000	0.000
10	A	12	ILE	0	-0.009	0.001	21.615	-0.068	-0.068	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.011	0.029	24.019	0.054	0.054	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.864	0.908	26.759	0.376	0.376	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.013	-0.011	29.020	0.025	0.025	0.000	0.000	0.000	0.000
14	A	16	ALA	0	-0.043	0.009	23.896	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	17	ILE	0	-0.013	-0.014	22.505	-0.031	-0.031	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.794	-0.864	26.190	-0.343	-0.343	0.000	0.000	0.000	0.000
17	A	19	ASP	-1	-0.867	-0.946	27.895	-0.422	-0.422	0.000	0.000	0.000	0.000
18	A	20	SER	0	-0.092	-0.062	29.092	0.013	0.013	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.922	-0.963	27.572	-0.464	-0.464	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.800	0.906	24.899	0.379	0.379	0.000	0.000	0.000	0.000
21	A	23	MET	0	-0.058	-0.034	23.194	-0.036	-0.036	0.000	0.000	0.000	0.000
22	A	24	ILE	0	0.014	0.002	20.147	0.006	0.006	0.000	0.000	0.000	0.000
23	A	25	ILE	0	0.016	0.019	19.905	-0.084	-0.084	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.001	0.013	14.420	0.000	0.000	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.034	-0.011	18.092	0.057	0.057	0.000	0.000	0.000	0.000
26	A	28	GLY	0	0.055	0.049	16.697	-0.065	-0.065	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.786	-0.914	16.478	-1.115	-1.115	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.087	-0.028	19.273	0.059	0.059	0.000	0.000	0.000	0.000
29	A	31	ALA	0	0.010	0.026	21.680	0.066	0.066	0.000	0.000	0.000	0.000
30	A	32	THR	0	0.014	-0.001	23.620	0.016	0.016	0.000	0.000	0.000	0.000
31	A	33	ASP	-1	-0.820	-0.935	27.219	-0.484	-0.484	0.000	0.000	0.000	0.000
32	A	34	THR	0	-0.072	-0.040	29.381	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	35	LEU	0	0.009	0.000	25.298	0.013	0.013	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.876	0.937	23.966	0.599	0.599	0.000	0.000	0.000	0.000
35	A	37	GLN	0	-0.108	-0.048	25.972	0.003	0.003	0.000	0.000	0.000	0.000
36	A	38	HIS	0	0.029	-0.001	26.564	0.012	0.012	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.025	0.027	21.464	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	40	VAL	0	0.010	0.011	18.314	0.041	0.041	0.000	0.000	0.000	0.000
39	A	41	ILE	0	-0.041	-0.021	18.962	-0.068	-0.068	0.000	0.000	0.000	0.000
40	A	42	GLN	0	0.010	0.001	12.648	-0.218	-0.218	0.000	0.000	0.000	0.000
41	A	43	SER	0	0.001	-0.003	13.863	-0.033	-0.033	0.000	0.000	0.000	0.000
42	A	44	PHE	0	0.005	-0.026	6.253	0.006	0.006	0.000	0.000	0.000	0.000
43	A	45	PRO	0	-0.034	-0.031	8.001	0.104	0.104	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.835	-0.927	2.562	-21.183	-17.691	0.405	-2.022	-1.875	-0.027
45	A	47	LYS	1	0.857	0.936	6.872	1.303	1.303	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.908	-0.952	9.113	-2.035	-2.035	0.000	0.000	0.000	0.000
47	A	49	GLN	0	-0.067	-0.056	5.532	1.061	1.061	0.000	0.000	0.000	0.000
48	A	50	VAL	0	-0.040	-0.002	5.998	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	51	THR	0	-0.044	-0.025	6.652	0.925	0.925	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.017	-0.006	7.523	-0.225	-0.225	0.000	0.000	0.000	0.000
51	A	53	ALA	0	-0.001	-0.007	9.115	0.399	0.399	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.893	-0.955	10.374	-0.637	-0.637	0.000	0.000	0.000	0.000
53	A	55	GLY	0	-0.050	-0.016	11.145	0.106	0.106	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.808	-0.901	6.951	-2.155	-2.155	0.000	0.000	0.000	0.000
55	A	57	HIS	0	-0.017	-0.015	7.395	0.441	0.441	0.000	0.000	0.000	0.000
56	A	58	LEU	0	0.008	0.014	8.457	-0.631	-0.631	0.000	0.000	0.000	0.000
57	A	59	LYS	1	0.854	0.930	10.526	1.275	1.275	0.000	0.000	0.000	0.000
58	A	60	ILE	0	0.028	0.017	12.108	-0.181	-0.181	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.071	0.043	15.031	0.173	0.173	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.967	-0.993	16.180	-0.593	-0.593	0.000	0.000	0.000	0.000
61	A	63	THR	0	-0.028	-0.015	17.081	0.115	0.115	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.066	-0.039	11.048	-0.269	-0.269	0.000	0.000	0.000	0.000
63	A	65	TYR	0	-0.026	-0.026	13.176	0.131	0.131	0.000	0.000	0.000	0.000
64	A	66	THR	0	-0.014	-0.008	12.163	-0.142	-0.142	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.007	-0.011	10.037	0.092	0.092	0.000	0.000	0.000	0.000
66	A	68	THR	0	-0.021	-0.027	13.383	0.072	0.072	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.862	0.923	16.091	0.507	0.507	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.030	0.000	12.661	-0.104	-0.104	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.021	0.027	16.130	0.099	0.099	0.000	0.000	0.000	0.000
70	A	72	SER	0	0.001	-0.025	17.564	-0.079	-0.079	0.000	0.000	0.000	0.000
71	A	73	PHE	0	-0.060	-0.036	18.636	0.024	0.024	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.040	0.043	15.461	-0.045	-0.045	0.000	0.000	0.000	0.000
73	A	75	ASN	0	0.053	0.031	11.512	-0.346	-0.346	0.000	0.000	0.000	0.000
74	A	76	SER	0	0.029	0.020	13.247	-0.123	-0.123	0.000	0.000	0.000	0.000
75	A	77	ASN	0	-0.053	-0.040	15.796	0.032	0.032	0.000	0.000	0.000	0.000
76	A	78	LEU	0	0.009	0.018	10.873	-0.028	-0.028	0.000	0.000	0.000	0.000
77	A	79	GLN	0	0.003	-0.010	10.687	0.149	0.149	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.053	-0.013	12.649	0.032	0.032	0.000	0.000	0.000	0.000
79	A	81	ILE	0	-0.028	-0.015	16.156	0.025	0.025	0.000	0.000	0.000	0.000
80	A	82	ALA	0	0.015	0.015	13.418	0.021	0.021	0.000	0.000	0.000	0.000
81	A	83	HIS	0	-0.077	-0.041	14.466	0.090	0.090	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.022	-0.024	15.262	-0.079	-0.079	0.000	0.000	0.000	0.000
83	A	85	THR	0	0.006	0.003	17.362	0.040	0.040	0.000	0.000	0.000	0.000
84	A	86	LEU	0	-0.013	0.005	14.756	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	87	ILE	0	0.020	-0.001	18.667	0.086	0.086	0.000	0.000	0.000	0.000
86	A	88	PHE	0	-0.033	-0.007	18.299	-0.035	-0.035	0.000	0.000	0.000	0.000
87	A	89	ALA	0	0.053	0.001	21.793	0.058	0.058	0.000	0.000	0.000	0.000
88	A	90	ASP	-1	-0.901	-0.942	22.214	-0.417	-0.417	0.000	0.000	0.000	0.000
89	A	91	ALA	0	-0.004	-0.003	21.140	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	92	PRO	0	-0.026	-0.005	23.222	0.033	0.033	0.000	0.000	0.000	0.000
91	A	93	THR	0	-0.010	-0.023	25.649	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.935	-0.959	27.764	-0.219	-0.219	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.761	-0.879	23.249	-0.387	-0.387	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.988	-0.975	26.338	-0.284	-0.284	0.000	0.000	0.000	0.000
95	A	97	ASP	-1	-0.945	-0.987	28.362	-0.307	-0.307	0.000	0.000	0.000	0.000
96	A	98	VAL	0	-0.118	-0.039	21.639	-0.040	-0.040	0.000	0.000	0.000	0.000
97	A	99	ILE	0	0.006	-0.001	22.417	0.001	0.001	0.000	0.000	0.000	0.000
98	A	100	ARG	1	0.988	0.975	21.722	0.376	0.376	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.018	0.007	18.927	-0.011	-0.011	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.043	0.017	18.406	-0.091	-0.091	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.003	0.003	13.498	-0.030	-0.030	0.000	0.000	0.000	0.000
102	A	104	TYR	0	0.045	0.028	16.598	0.013	0.013	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.011	0.004	14.023	-0.088	-0.088	0.000	0.000	0.000	0.000
104	A	106	THR	0	0.035	0.018	16.770	0.108	0.108	0.000	0.000	0.000	0.000
105	A	107	PRO	0	0.019	-0.005	16.813	-0.056	-0.056	0.000	0.000	0.000	0.000
106	A	108	HIS	0	-0.044	-0.024	20.166	-0.044	-0.044	0.000	0.000	0.000	0.000
107	A	109	GLN	0	-0.038	0.000	22.290	0.021	0.021	0.000	0.000	0.000	0.000
108	A	110	LEU	0	0.066	0.043	21.663	-0.060	-0.060	0.000	0.000	0.000	0.000
109	A	111	PRO	0	-0.012	0.017	18.696	0.039	0.039	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.890	0.944	21.004	0.500	0.500	0.000	0.000	0.000	0.000
111	A	113	ILE	0	0.007	0.003	18.521	-0.056	-0.056	0.000	0.000	0.000	0.000
112	A	114	THR	0	-0.032	-0.029	20.709	0.073	0.073	0.000	0.000	0.000	0.000
113	A	115	ILE	0	0.027	0.003	20.475	-0.074	-0.074	0.000	0.000	0.000	0.000
114	A	116	GLY	0	0.008	0.010	18.205	0.065	0.065	0.000	0.000	0.000	0.000
115	A	117	THR	0	-0.052	-0.019	16.506	-0.017	-0.017	0.000	0.000	0.000	0.000
116	A	118	THR	0	0.029	0.017	11.948	0.006	0.006	0.000	0.000	0.000	0.000
117	A	119	ILE	0	-0.022	-0.019	10.780	0.210	0.210	0.000	0.000	0.000	0.000
118	A	120	ASP	-1	-0.825	-0.902	7.937	-2.983	-2.983	0.000	0.000	0.000	0.000
119	A	121	TYR	0	0.030	-0.007	5.595	0.665	0.665	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.062	-0.035	4.205	-2.092	-1.890	-0.001	-0.074	-0.126	0.000
121	A	123	VAL	0	0.044	0.041	1.841	-0.184	-6.512	13.548	-3.816	-3.404	-0.022

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:TRP)