FMO DATABASE

FMODB ID: JL369

Calculation Name: 2FSD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FSD

Chain ID: A

ChEMBL ID:

UniProt ID: O80120

Base Structure: X-ray

Registration Date: 2023-06-21

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	110
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-763245.798347
FMO2-HF: Nuclear repulsion	723603.022847
FMO2-HF: Total energy	-39642.7755
FMO2-MP2: Total energy	-39759.844689

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:4:ASP)

Summations of interaction energy for fragment #1(A:4:ASP)

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.
-107.572	-97.566	10.745	-9.734	-11.018	0.09

Interaction energy analysis for fragmet #1(A:4:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.867 / q_NPA : -0.937

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	6	PRO	0	0.036	0.007	3.805	0.514	2.100	-0.018	-0.638	-0.930	0.005
4	A	7	TRP	0	-0.030	-0.027	5.681	-0.676	-0.676	0.000	0.000	0.000	0.000
5	A	8	THR	0	-0.030	-0.012	8.795	-1.217	-1.217	0.000	0.000	0.000	0.000
6	A	9	ASP	-1	-0.916	-0.953	11.232	17.817	17.817	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.055	-0.026	13.405	0.385	0.385	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.020	0.002	15.650	-0.767	-0.767	0.000	0.000	0.000	0.000
9	A	12	ARG	1	0.862	0.918	18.736	-13.475	-13.475	0.000	0.000	0.000	0.000
10	A	13	ALA	0	-0.008	0.007	21.707	-0.294	-0.294	0.000	0.000	0.000	0.000
11	A	14	SER	0	0.059	0.002	24.283	-0.077	-0.077	0.000	0.000	0.000	0.000
12	A	15	GLY	0	-0.028	-0.013	27.929	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	16	VAL	0	-0.057	-0.002	23.737	-0.157	-0.157	0.000	0.000	0.000	0.000
14	A	17	GLY	0	-0.013	-0.002	27.070	-0.111	-0.111	0.000	0.000	0.000	0.000
15	A	18	SER	0	0.013	-0.006	25.222	0.458	0.458	0.000	0.000	0.000	0.000
16	A	19	THR	0	0.002	0.007	24.592	0.400	0.400	0.000	0.000	0.000	0.000
17	A	20	GLY	0	0.079	0.038	23.496	0.135	0.135	0.000	0.000	0.000	0.000
18	A	21	ILE	0	-0.051	-0.030	17.067	0.169	0.169	0.000	0.000	0.000	0.000
19	A	22	LEU	0	0.059	0.021	16.935	-0.069	-0.069	0.000	0.000	0.000	0.000
20	A	23	GLN	0	0.043	0.027	12.621	-0.169	-0.169	0.000	0.000	0.000	0.000
21	A	24	ALA	0	0.020	0.002	10.049	-0.296	-0.296	0.000	0.000	0.000	0.000
22	A	25	ARG	1	0.933	0.977	6.172	-37.603	-37.603	0.000	0.000	0.000	0.000
23	A	26	ILE	0	0.002	-0.005	2.992	-4.796	-3.340	0.139	-0.569	-1.026	0.003
24	A	27	ILE	0	-0.005	-0.007	2.566	0.224	5.075	4.474	-4.725	-4.601	0.017
25	A	28	ASN	0	-0.014	-0.014	1.994	-29.288	-27.857	6.137	-3.382	-4.186	0.062
26	A	29	GLY	0	0.035	0.025	3.752	-14.548	-13.866	0.013	-0.420	-0.275	0.003
27	A	30	VAL	0	-0.007	0.016	5.600	-8.509	-8.509	0.000	0.000	0.000	0.000
28	A	31	ILE	0	-0.003	0.010	6.574	5.761	5.761	0.000	0.000	0.000	0.000
29	A	32	TYR	0	-0.028	-0.021	7.382	-5.475	-5.475	0.000	0.000	0.000	0.000
30	A	33	VAL	0	0.014	-0.008	10.403	0.450	0.450	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.856	0.935	13.128	-21.598	-21.598	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.046	0.011	16.060	0.072	0.072	0.000	0.000	0.000	0.000
33	A	36	ASN	0	-0.067	-0.037	19.277	-0.726	-0.726	0.000	0.000	0.000	0.000
34	A	37	SER	0	0.067	0.022	21.727	-0.295	-0.295	0.000	0.000	0.000	0.000
35	A	38	ILE	0	-0.016	0.007	20.053	-0.145	-0.145	0.000	0.000	0.000	0.000
36	A	39	PRO	0	-0.019	0.012	24.601	-0.266	-0.266	0.000	0.000	0.000	0.000
37	A	40	VAL	0	0.016	0.009	25.736	0.246	0.246	0.000	0.000	0.000	0.000
38	A	41	PRO	0	0.024	0.007	28.374	-0.357	-0.357	0.000	0.000	0.000	0.000
39	A	42	ASN	0	-0.005	-0.011	31.343	0.230	0.230	0.000	0.000	0.000	0.000
40	A	43	VAL	0	0.004	0.029	30.032	0.031	0.031	0.000	0.000	0.000	0.000
41	A	44	ALA	0	0.037	0.020	33.326	-0.142	-0.142	0.000	0.000	0.000	0.000
42	A	45	PRO	0	-0.001	-0.013	34.600	0.267	0.267	0.000	0.000	0.000	0.000
43	A	46	ASN	0	-0.018	-0.022	33.567	0.000	0.000	0.000	0.000	0.000	0.000
44	A	47	PHE	0	-0.027	0.013	33.025	0.068	0.068	0.000	0.000	0.000	0.000
45	A	48	ILE	0	-0.008	-0.018	26.525	0.212	0.212	0.000	0.000	0.000	0.000
46	A	49	VAL	0	0.005	0.010	27.423	-0.221	-0.221	0.000	0.000	0.000	0.000
47	A	50	PRO	0	0.014	0.001	24.444	0.464	0.464	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.007	0.007	21.624	-0.320	-0.320	0.000	0.000	0.000	0.000
49	A	52	GLY	0	0.021	0.000	19.124	-0.149	-0.149	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.002	0.007	17.619	0.063	0.063	0.000	0.000	0.000	0.000
51	A	54	PHE	0	0.055	0.007	11.870	0.560	0.560	0.000	0.000	0.000	0.000
52	A	55	PRO	0	0.009	0.008	11.849	-0.686	-0.686	0.000	0.000	0.000	0.000
53	A	56	PRO	0	0.045	0.003	11.944	1.390	1.390	0.000	0.000	0.000	0.000
54	A	57	ALA	0	-0.027	0.002	8.301	0.388	0.388	0.000	0.000	0.000	0.000
55	A	58	PHE	0	-0.023	-0.019	7.501	2.884	2.884	0.000	0.000	0.000	0.000
56	A	59	GLY	0	0.000	0.022	8.677	1.079	1.079	0.000	0.000	0.000	0.000
57	A	60	THR	0	0.032	-0.002	11.076	-1.046	-1.046	0.000	0.000	0.000	0.000
58	A	61	ASN	0	-0.011	0.008	9.448	-1.299	-1.299	0.000	0.000	0.000	0.000
59	A	62	LEU	0	-0.002	0.003	10.300	1.460	1.460	0.000	0.000	0.000	0.000
60	A	63	PRO	0	0.047	0.026	12.247	-1.430	-1.430	0.000	0.000	0.000	0.000
61	A	64	GLN	0	0.003	-0.008	15.384	-0.402	-0.402	0.000	0.000	0.000	0.000
62	A	65	PHE	0	-0.078	-0.043	15.621	-0.139	-0.139	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.827	-0.909	20.551	13.092	13.092	0.000	0.000	0.000	0.000
64	A	67	SER	0	-0.043	-0.029	20.547	0.204	0.204	0.000	0.000	0.000	0.000
65	A	68	SER	0	0.009	0.001	22.869	-0.454	-0.454	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.020	0.010	23.104	0.760	0.760	0.000	0.000	0.000	0.000
67	A	70	THR	0	-0.079	-0.022	24.710	-0.534	-0.534	0.000	0.000	0.000	0.000
68	A	71	PHE	0	0.021	0.004	27.097	0.245	0.245	0.000	0.000	0.000	0.000
69	A	72	TYR	0	0.024	0.012	29.883	-0.269	-0.269	0.000	0.000	0.000	0.000
70	A	73	SER	0	0.031	0.017	31.638	0.039	0.039	0.000	0.000	0.000	0.000
71	A	74	HIS	0	0.029	0.009	34.682	-0.015	-0.015	0.000	0.000	0.000	0.000
72	A	75	GLY	0	0.050	0.038	35.727	-0.184	-0.184	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.073	-0.039	35.923	-0.133	-0.133	0.000	0.000	0.000	0.000
74	A	77	LEU	0	0.000	-0.010	29.718	0.191	0.191	0.000	0.000	0.000	0.000
75	A	78	SER	0	0.011	-0.002	32.151	-0.236	-0.236	0.000	0.000	0.000	0.000
76	A	79	LEU	0	0.025	0.020	28.975	0.352	0.352	0.000	0.000	0.000	0.000
77	A	80	SER	0	-0.006	-0.006	26.221	-0.204	-0.204	0.000	0.000	0.000	0.000
78	A	81	LEU	0	0.007	0.011	25.490	0.124	0.124	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.033	-0.027	19.964	-0.088	-0.088	0.000	0.000	0.000	0.000
80	A	83	ASN	0	0.033	0.014	22.178	0.615	0.615	0.000	0.000	0.000	0.000
81	A	84	MET	0	-0.002	0.012	13.149	0.317	0.317	0.000	0.000	0.000	0.000
82	A	85	SER	0	0.052	0.011	17.536	-0.486	-0.486	0.000	0.000	0.000	0.000
83	A	86	PRO	0	0.018	-0.007	15.463	0.623	0.623	0.000	0.000	0.000	0.000
84	A	87	SER	0	-0.005	-0.001	16.546	0.339	0.339	0.000	0.000	0.000	0.000
85	A	88	GLY	0	-0.050	-0.008	16.677	-0.432	-0.432	0.000	0.000	0.000	0.000
86	A	89	ILE	0	-0.013	0.000	16.147	0.271	0.271	0.000	0.000	0.000	0.000
87	A	90	ALA	0	-0.013	-0.011	19.310	-0.545	-0.545	0.000	0.000	0.000	0.000
88	A	91	VAL	0	-0.007	-0.005	23.090	0.252	0.252	0.000	0.000	0.000	0.000
89	A	92	GLY	0	0.062	0.030	25.636	-0.383	-0.383	0.000	0.000	0.000	0.000
90	A	93	ASN	0	-0.049	-0.045	28.644	0.207	0.207	0.000	0.000	0.000	0.000
91	A	94	PRO	0	0.006	0.010	30.474	-0.252	-0.252	0.000	0.000	0.000	0.000
92	A	95	ASN	0	-0.045	-0.020	33.153	-0.320	-0.320	0.000	0.000	0.000	0.000
93	A	96	ASN	0	0.022	0.000	36.153	0.055	0.055	0.000	0.000	0.000	0.000
94	A	97	THR	0	0.042	0.026	38.614	-0.213	-0.213	0.000	0.000	0.000	0.000
95	A	98	SER	0	-0.029	-0.038	37.087	0.292	0.292	0.000	0.000	0.000	0.000
96	A	99	MET	0	-0.075	-0.008	33.004	-0.047	-0.047	0.000	0.000	0.000	0.000
97	A	100	ASN	0	0.095	0.054	34.137	0.339	0.339	0.000	0.000	0.000	0.000
98	A	101	GLY	0	0.020	0.005	34.499	-0.056	-0.056	0.000	0.000	0.000	0.000
99	A	102	LYS	1	0.836	0.930	31.027	-9.025	-9.025	0.000	0.000	0.000	0.000
100	A	103	THR	0	-0.014	0.002	27.447	0.193	0.193	0.000	0.000	0.000	0.000
101	A	104	ILE	0	0.011	-0.014	23.046	-0.179	-0.179	0.000	0.000	0.000	0.000
102	A	105	SER	0	-0.003	0.001	22.681	0.456	0.456	0.000	0.000	0.000	0.000
103	A	106	PHE	0	0.022	0.000	16.986	-0.517	-0.517	0.000	0.000	0.000	0.000
104	A	107	ALA	0	-0.001	-0.009	16.889	0.561	0.561	0.000	0.000	0.000	0.000
105	A	108	LEU	0	-0.014	0.013	14.175	-0.624	-0.624	0.000	0.000	0.000	0.000
106	A	109	SER	0	-0.015	-0.023	11.782	1.708	1.708	0.000	0.000	0.000	0.000
107	A	110	ALA	0	0.033	0.028	11.961	-1.912	-1.912	0.000	0.000	0.000	0.000
108	A	111	PRO	0	0.015	0.009	10.033	2.626	2.626	0.000	0.000	0.000	0.000
109	A	112	LEU	0	-0.022	-0.012	6.368	-1.623	-1.623	0.000	0.000	0.000	0.000
110	A	113	LEU	0	-0.044	-0.019	10.658	-1.672	-1.672	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASP)