FMO DATABASE

FMODB ID: QVNQY

Calculation Name: 2F9S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2F9S

Chain ID: A

ChEMBL ID:

UniProt ID: P35160

Base Structure: X-ray

Registration Date: 2023-09-22

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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1299874.99196
FMO2-HF: Nuclear repulsion	1245028.344355
FMO2-HF: Total energy	-54846.647604
FMO2-MP2: Total energy	-55004.514942

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:38:GLU)

Summations of interaction energy for fragment #1(A:38: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.
28.984	32.169	0.553	-1.347	-2.39	0.007

Interaction energy analysis for fragmet #1(A:38:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.985 / q_NPA : -1.003

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

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	40	SER	0	-0.019	-0.003	3.507	-2.869	-1.202	0.006	-0.811	-0.863	0.005
4	A	41	ASP	-1	-0.872	-0.930	6.939	27.156	27.156	0.000	0.000	0.000	0.000
5	A	42	ALA	0	0.020	0.025	9.213	-0.873	-0.873	0.000	0.000	0.000	0.000
6	A	43	PRO	0	0.004	0.009	11.633	-0.795	-0.795	0.000	0.000	0.000	0.000
7	A	44	ASN	0	-0.013	-0.004	15.233	0.529	0.529	0.000	0.000	0.000	0.000
8	A	45	PHE	0	0.025	0.008	16.926	-0.560	-0.560	0.000	0.000	0.000	0.000
9	A	46	VAL	0	0.022	-0.003	20.489	0.079	0.079	0.000	0.000	0.000	0.000
10	A	47	LEU	0	-0.010	0.010	22.696	-0.293	-0.293	0.000	0.000	0.000	0.000
11	A	48	GLU	-1	-0.823	-0.903	25.402	9.687	9.687	0.000	0.000	0.000	0.000
12	A	49	ASP	-1	-0.747	-0.858	27.500	10.664	10.664	0.000	0.000	0.000	0.000
13	A	50	THR	0	-0.004	-0.032	28.798	-0.240	-0.240	0.000	0.000	0.000	0.000
14	A	51	ASN	0	-0.108	-0.054	31.909	-0.571	-0.571	0.000	0.000	0.000	0.000
15	A	52	GLY	0	-0.022	0.001	32.319	-0.222	-0.222	0.000	0.000	0.000	0.000
16	A	53	LYS	1	0.866	0.938	27.247	-11.154	-11.154	0.000	0.000	0.000	0.000
17	A	54	ARG	1	0.937	0.969	26.737	-10.413	-10.413	0.000	0.000	0.000	0.000
18	A	55	ILE	0	0.001	-0.004	21.571	0.000	0.000	0.000	0.000	0.000	0.000
19	A	56	GLU	-1	-0.820	-0.895	19.717	13.615	13.615	0.000	0.000	0.000	0.000
20	A	57	LEU	0	-0.011	0.013	13.851	0.261	0.261	0.000	0.000	0.000	0.000
21	A	58	SER	0	-0.007	-0.039	15.311	1.265	1.265	0.000	0.000	0.000	0.000
22	A	59	ASP	-1	-0.896	-0.935	16.362	14.018	14.018	0.000	0.000	0.000	0.000
23	A	60	LEU	0	-0.109	-0.071	16.318	-0.274	-0.274	0.000	0.000	0.000	0.000
24	A	61	LYS	1	0.964	0.976	11.124	-19.384	-19.384	0.000	0.000	0.000	0.000
25	A	62	GLY	0	-0.035	-0.020	12.450	-1.477	-1.477	0.000	0.000	0.000	0.000
26	A	63	LYS	1	0.821	0.929	13.727	-17.571	-17.571	0.000	0.000	0.000	0.000
27	A	64	GLY	0	0.060	0.052	11.184	1.237	1.237	0.000	0.000	0.000	0.000
28	A	65	VAL	0	-0.047	-0.035	11.763	-2.454	-2.454	0.000	0.000	0.000	0.000
29	A	66	PHE	0	0.038	0.005	12.339	1.604	1.604	0.000	0.000	0.000	0.000
30	A	67	LEU	0	0.010	0.011	13.998	-1.587	-1.587	0.000	0.000	0.000	0.000
31	A	68	ASN	0	-0.032	-0.030	15.719	-0.190	-0.190	0.000	0.000	0.000	0.000
32	A	69	PHE	0	0.040	0.023	16.544	-0.813	-0.813	0.000	0.000	0.000	0.000
33	A	70	TRP	0	-0.026	-0.036	20.757	-0.360	-0.360	0.000	0.000	0.000	0.000
34	A	71	GLY	0	0.088	0.035	24.180	-0.170	-0.170	0.000	0.000	0.000	0.000
35	A	72	THR	0	-0.125	-0.108	27.932	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	73	TRP	0	0.020	0.001	28.177	-0.145	-0.145	0.000	0.000	0.000	0.000
37	A	74	CYS	0	-0.062	-0.009	25.938	-0.145	-0.145	0.000	0.000	0.000	0.000
38	A	75	GLU	-1	-0.781	-0.879	28.967	9.798	9.798	0.000	0.000	0.000	0.000
39	A	76	PRO	0	-0.015	-0.017	24.907	0.105	0.105	0.000	0.000	0.000	0.000
40	A	77	CYS	0	0.006	0.027	23.731	0.437	0.437	0.000	0.000	0.000	0.000
41	A	78	LYS	1	0.853	0.917	25.784	-9.371	-9.371	0.000	0.000	0.000	0.000
42	A	79	LYS	1	0.882	0.952	26.714	-11.468	-11.468	0.000	0.000	0.000	0.000
43	A	80	GLU	-1	-0.794	-0.914	21.371	14.986	14.986	0.000	0.000	0.000	0.000
44	A	81	PHE	0	0.042	0.014	23.819	0.257	0.257	0.000	0.000	0.000	0.000
45	A	82	PRO	0	0.004	-0.001	25.799	0.135	0.135	0.000	0.000	0.000	0.000
46	A	83	TYR	0	-0.019	-0.002	23.194	-0.074	-0.074	0.000	0.000	0.000	0.000
47	A	84	MET	0	0.004	0.013	20.204	0.366	0.366	0.000	0.000	0.000	0.000
48	A	85	ALA	0	0.040	0.031	22.575	0.275	0.275	0.000	0.000	0.000	0.000
49	A	86	ASN	0	-0.056	-0.043	25.305	-0.419	-0.419	0.000	0.000	0.000	0.000
50	A	87	GLN	0	0.030	-0.004	19.952	0.535	0.535	0.000	0.000	0.000	0.000
51	A	88	TYR	0	-0.045	-0.045	20.489	0.095	0.095	0.000	0.000	0.000	0.000
52	A	89	LYS	1	0.830	0.912	21.986	-11.320	-11.320	0.000	0.000	0.000	0.000
53	A	90	HIS	0	-0.048	-0.006	19.023	-0.626	-0.626	0.000	0.000	0.000	0.000
54	A	91	PHE	0	0.047	0.022	15.814	0.153	0.153	0.000	0.000	0.000	0.000
55	A	92	LYS	1	0.907	0.966	18.309	-13.172	-13.172	0.000	0.000	0.000	0.000
56	A	93	SER	0	-0.054	-0.034	20.150	0.382	0.382	0.000	0.000	0.000	0.000
57	A	94	GLN	0	-0.018	-0.016	16.402	0.847	0.847	0.000	0.000	0.000	0.000
58	A	95	GLY	0	0.036	0.026	15.679	1.121	1.121	0.000	0.000	0.000	0.000
59	A	96	VAL	0	-0.004	0.001	13.497	1.320	1.320	0.000	0.000	0.000	0.000
60	A	97	GLU	-1	-0.804	-0.877	15.779	13.254	13.254	0.000	0.000	0.000	0.000
61	A	98	ILE	0	0.003	0.006	16.616	1.097	1.097	0.000	0.000	0.000	0.000
62	A	99	VAL	0	-0.014	-0.009	18.107	-0.814	-0.814	0.000	0.000	0.000	0.000
63	A	100	ALA	0	0.009	0.007	19.035	0.527	0.527	0.000	0.000	0.000	0.000
64	A	101	VAL	0	0.016	-0.001	19.798	-0.749	-0.749	0.000	0.000	0.000	0.000
65	A	102	ASN	0	-0.051	-0.043	22.492	-0.129	-0.129	0.000	0.000	0.000	0.000
66	A	103	VAL	0	0.026	-0.001	23.966	-0.044	-0.044	0.000	0.000	0.000	0.000
67	A	104	GLY	0	0.026	0.025	26.557	-0.314	-0.314	0.000	0.000	0.000	0.000
68	A	105	GLU	-1	-0.793	-0.833	29.840	9.681	9.681	0.000	0.000	0.000	0.000
69	A	106	SER	0	0.006	-0.002	31.990	0.079	0.079	0.000	0.000	0.000	0.000
70	A	107	LYS	1	0.916	0.946	32.735	-9.177	-9.177	0.000	0.000	0.000	0.000
71	A	108	ILE	0	-0.019	-0.003	34.578	0.100	0.100	0.000	0.000	0.000	0.000
72	A	109	ALA	0	0.017	0.015	34.483	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	110	VAL	0	0.065	0.032	29.407	0.097	0.097	0.000	0.000	0.000	0.000
74	A	111	HIS	0	-0.012	-0.016	32.113	0.162	0.162	0.000	0.000	0.000	0.000
75	A	112	ASN	0	0.006	-0.012	34.215	0.028	0.028	0.000	0.000	0.000	0.000
76	A	113	PHE	0	0.053	0.045	28.213	-0.124	-0.124	0.000	0.000	0.000	0.000
77	A	114	MET	0	0.025	0.000	28.369	0.052	0.052	0.000	0.000	0.000	0.000
78	A	115	LYS	1	0.878	0.952	31.400	-8.926	-8.926	0.000	0.000	0.000	0.000
79	A	116	SER	0	-0.052	-0.032	34.415	-0.163	-0.163	0.000	0.000	0.000	0.000
80	A	117	TYR	0	-0.014	-0.010	29.802	-0.083	-0.083	0.000	0.000	0.000	0.000
81	A	118	GLY	0	-0.050	-0.005	30.300	0.298	0.298	0.000	0.000	0.000	0.000
82	A	119	VAL	0	-0.037	-0.016	26.470	0.280	0.280	0.000	0.000	0.000	0.000
83	A	120	ASN	0	-0.049	-0.027	26.189	-0.086	-0.086	0.000	0.000	0.000	0.000
84	A	121	PHE	0	0.014	0.013	22.727	0.167	0.167	0.000	0.000	0.000	0.000
85	A	122	PRO	0	-0.025	-0.015	22.253	-0.547	-0.547	0.000	0.000	0.000	0.000
86	A	123	VAL	0	0.020	0.012	23.224	0.418	0.418	0.000	0.000	0.000	0.000
87	A	124	VAL	0	-0.030	-0.021	22.509	-0.372	-0.372	0.000	0.000	0.000	0.000
88	A	125	LEU	0	-0.013	-0.017	25.497	0.043	0.043	0.000	0.000	0.000	0.000
89	A	126	ASP	-1	-0.747	-0.875	24.027	12.372	12.372	0.000	0.000	0.000	0.000
90	A	127	THR	0	-0.049	-0.033	26.172	-0.151	-0.151	0.000	0.000	0.000	0.000
91	A	128	ASP	-1	-0.901	-0.964	28.381	10.310	10.310	0.000	0.000	0.000	0.000
92	A	129	ARG	1	0.826	0.914	25.866	-11.361	-11.361	0.000	0.000	0.000	0.000
93	A	130	GLN	0	0.036	0.036	24.903	0.403	0.403	0.000	0.000	0.000	0.000
94	A	131	VAL	0	-0.019	-0.019	19.495	0.539	0.539	0.000	0.000	0.000	0.000
95	A	132	LEU	0	-0.040	-0.038	19.919	0.702	0.702	0.000	0.000	0.000	0.000
96	A	133	ASP	-1	-0.844	-0.919	20.549	12.429	12.429	0.000	0.000	0.000	0.000
97	A	134	ALA	0	-0.044	-0.012	18.785	0.402	0.402	0.000	0.000	0.000	0.000
98	A	135	TYR	0	-0.101	-0.081	13.046	1.434	1.434	0.000	0.000	0.000	0.000
99	A	136	ASP	-1	-0.946	-0.959	16.430	16.023	16.023	0.000	0.000	0.000	0.000
100	A	137	VAL	0	-0.043	-0.015	17.761	0.276	0.276	0.000	0.000	0.000	0.000
101	A	138	SER	0	0.022	0.005	19.732	-0.887	-0.887	0.000	0.000	0.000	0.000
102	A	139	PRO	0	-0.066	-0.021	20.715	-0.520	-0.520	0.000	0.000	0.000	0.000
103	A	140	LEU	0	0.007	0.027	21.494	0.582	0.582	0.000	0.000	0.000	0.000
104	A	141	PRO	0	-0.012	-0.036	20.480	-0.609	-0.609	0.000	0.000	0.000	0.000
105	A	142	THR	0	0.013	-0.008	15.925	0.349	0.349	0.000	0.000	0.000	0.000
106	A	143	THR	0	-0.011	-0.002	14.045	-0.781	-0.781	0.000	0.000	0.000	0.000
107	A	144	PHE	0	0.011	0.008	11.274	1.231	1.231	0.000	0.000	0.000	0.000
108	A	145	LEU	0	-0.055	-0.021	8.882	-1.219	-1.219	0.000	0.000	0.000	0.000
109	A	146	ILE	0	0.025	0.011	7.829	3.729	3.729	0.000	0.000	0.000	0.000
110	A	147	ASN	0	0.043	0.004	4.779	-6.160	-6.003	-0.001	-0.008	-0.148	0.000
111	A	148	PRO	0	0.043	0.030	7.762	-2.367	-2.367	0.000	0.000	0.000	0.000
112	A	149	GLU	-1	-0.883	-0.938	5.850	35.032	35.032	0.000	0.000	0.000	0.000
113	A	150	GLY	0	-0.081	-0.036	8.174	-1.874	-1.874	0.000	0.000	0.000	0.000
114	A	151	LYS	1	0.827	0.913	3.909	-34.206	-33.934	0.000	-0.054	-0.218	0.000
115	A	152	VAL	0	0.000	-0.008	6.537	1.772	1.772	0.000	0.000	0.000	0.000
116	A	153	VAL	0	0.029	0.008	2.424	-0.289	0.639	0.549	-0.468	-1.008	0.002
117	A	154	LYS	1	0.905	0.964	4.432	-27.201	-27.040	-0.001	-0.006	-0.153	0.000
118	A	155	VAL	0	0.024	0.022	7.744	-1.963	-1.963	0.000	0.000	0.000	0.000
119	A	156	VAL	0	-0.050	-0.026	11.212	0.205	0.205	0.000	0.000	0.000	0.000
120	A	157	THR	0	0.021	0.021	14.481	-0.658	-0.658	0.000	0.000	0.000	0.000
121	A	158	GLY	0	0.003	0.001	17.855	-0.121	-0.121	0.000	0.000	0.000	0.000
122	A	159	THR	0	-0.056	-0.029	19.925	0.363	0.363	0.000	0.000	0.000	0.000
123	A	160	MET	0	-0.026	-0.003	17.271	0.963	0.963	0.000	0.000	0.000	0.000
124	A	161	THR	0	0.008	-0.036	20.293	-0.603	-0.603	0.000	0.000	0.000	0.000
125	A	162	GLU	-1	-0.765	-0.889	20.205	13.625	13.625	0.000	0.000	0.000	0.000
126	A	163	SER	0	-0.006	-0.003	20.008	0.309	0.309	0.000	0.000	0.000	0.000
127	A	164	MET	0	0.020	0.054	16.474	0.356	0.356	0.000	0.000	0.000	0.000
128	A	165	ILE	0	0.015	0.005	15.458	1.361	1.361	0.000	0.000	0.000	0.000
129	A	166	HIS	0	-0.034	-0.027	16.110	1.363	1.363	0.000	0.000	0.000	0.000
130	A	167	ASP	-1	-0.908	-0.955	13.206	21.189	21.189	0.000	0.000	0.000	0.000
131	A	168	TYR	0	-0.053	-0.046	11.487	2.676	2.676	0.000	0.000	0.000	0.000
132	A	169	MET	0	0.003	0.002	11.358	1.552	1.552	0.000	0.000	0.000	0.000
133	A	170	ASN	0	0.000	-0.003	12.576	0.188	0.188	0.000	0.000	0.000	0.000
134	A	171	LEU	0	-0.059	-0.013	5.659	0.256	0.256	0.000	0.000	0.000	0.000
135	A	172	ILE	0	-0.029	-0.012	7.285	4.277	4.277	0.000	0.000	0.000	0.000
136	A	173	LYS	1	0.828	0.919	8.955	-22.494	-22.494	0.000	0.000	0.000	0.000
137	A	174	PRO	0	-0.182	-0.065	10.337	2.343	2.343	0.000	0.000	0.000	0.000
138	A	175	GLY	0	0.157	0.079	10.337	-2.793	-2.793	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:38:GLU)