FMO DATABASE

FMODB ID: YZV72

Calculation Name: 1SFP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SFP

Chain ID: A

ChEMBL ID:

UniProt ID: P29392

Base Structure: X-ray

Registration Date: 2023-06-22

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	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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-892241.048706
FMO2-HF: Nuclear repulsion	847463.9641
FMO2-HF: Total energy	-44777.084606
FMO2-MP2: Total energy	-44904.209887

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:LEU)

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

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.
-5.361	-0.652	3.859	-2.351	-6.219	-0.014

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.017 / q_NPA : -0.019

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	ARG	1	0.929	0.959	3.790	-0.278	0.978	-0.005	-0.435	-0.817	0.003
4	A	7	ASN	0	-0.010	-0.012	5.960	0.537	0.537	0.000	0.000	0.000	0.000
5	A	8	THR	0	0.060	0.026	8.875	-0.014	-0.014	0.000	0.000	0.000	0.000
6	A	9	ASN	0	-0.007	-0.004	12.066	0.097	0.097	0.000	0.000	0.000	0.000
7	A	10	CYS	0	-0.139	-0.054	14.572	-0.011	-0.011	0.000	0.000	0.000	0.000
8	A	11	GLY	0	0.019	0.008	15.209	0.031	0.031	0.000	0.000	0.000	0.000
9	A	12	GLY	0	-0.016	-0.010	15.215	0.005	0.005	0.000	0.000	0.000	0.000
10	A	13	ILE	0	-0.035	-0.022	14.811	-0.029	-0.029	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.052	-0.017	9.003	0.018	0.018	0.000	0.000	0.000	0.000
12	A	15	LYS	1	0.915	0.946	11.202	0.158	0.158	0.000	0.000	0.000	0.000
13	A	16	GLU	-1	-0.915	-0.940	5.953	0.084	0.084	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.796	-0.887	6.575	-0.311	-0.311	0.000	0.000	0.000	0.000
15	A	18	SER	0	-0.004	-0.008	2.463	-1.891	-1.195	2.117	-0.954	-1.859	-0.011
16	A	19	GLY	0	0.021	0.012	2.356	-1.412	-0.234	0.915	-0.868	-1.225	-0.005
17	A	20	VAL	0	-0.035	-0.016	2.459	-0.326	0.262	0.756	0.108	-1.453	-0.001
18	A	21	ILE	0	-0.019	0.004	4.817	0.039	0.059	-0.001	-0.005	-0.014	0.000
19	A	22	ALA	0	0.003	-0.001	8.542	0.027	0.027	0.000	0.000	0.000	0.000
20	A	23	THR	0	0.001	-0.006	10.330	0.025	0.025	0.000	0.000	0.000	0.000
21	A	24	TYR	0	-0.029	0.014	13.998	0.020	0.020	0.000	0.000	0.000	0.000
22	A	25	TYR	0	0.017	-0.001	15.799	0.009	0.009	0.000	0.000	0.000	0.000
23	A	26	GLY	0	-0.040	-0.022	18.971	0.023	0.023	0.000	0.000	0.000	0.000
24	A	27	PRO	0	0.017	-0.006	21.529	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.914	0.958	20.351	0.146	0.146	0.000	0.000	0.000	0.000
26	A	29	THR	0	0.058	0.024	22.692	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	30	ASN	0	0.011	0.003	22.343	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	32	VAL	0	0.040	0.005	18.016	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	33	TRP	0	0.018	0.009	12.319	0.014	0.014	0.000	0.000	0.000	0.000
30	A	34	THR	0	-0.029	-0.014	14.803	0.008	0.008	0.000	0.000	0.000	0.000
31	A	35	ILE	0	0.000	0.005	10.371	0.008	0.008	0.000	0.000	0.000	0.000
32	A	36	GLN	0	0.002	-0.013	13.172	0.058	0.058	0.000	0.000	0.000	0.000
33	A	37	MET	0	0.005	0.021	8.882	0.024	0.024	0.000	0.000	0.000	0.000
34	A	38	PRO	0	-0.002	-0.014	13.401	0.030	0.030	0.000	0.000	0.000	0.000
35	A	39	PRO	0	0.041	0.005	16.675	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	40	GLU	-1	-0.962	-0.976	19.440	-0.087	-0.087	0.000	0.000	0.000	0.000
37	A	41	TYR	0	-0.061	-0.011	14.316	0.000	0.000	0.000	0.000	0.000	0.000
38	A	42	HIS	0	-0.042	-0.022	15.182	0.020	0.020	0.000	0.000	0.000	0.000
39	A	43	VAL	0	-0.009	-0.004	10.646	-0.044	-0.044	0.000	0.000	0.000	0.000
40	A	44	ARG	1	0.779	0.866	9.758	0.392	0.392	0.000	0.000	0.000	0.000
41	A	45	VAL	0	-0.006	-0.013	9.045	-0.119	-0.119	0.000	0.000	0.000	0.000
42	A	46	SER	0	-0.009	0.006	7.969	0.058	0.058	0.000	0.000	0.000	0.000
43	A	47	ILE	0	-0.014	-0.007	8.938	-0.072	-0.072	0.000	0.000	0.000	0.000
44	A	48	GLN	0	0.018	0.007	9.627	0.067	0.067	0.000	0.000	0.000	0.000
45	A	49	TYR	0	0.030	0.002	11.768	0.047	0.047	0.000	0.000	0.000	0.000
46	A	50	LEU	0	-0.038	-0.011	13.955	-0.034	-0.034	0.000	0.000	0.000	0.000
47	A	51	GLN	0	0.020	0.001	16.299	0.013	0.013	0.000	0.000	0.000	0.000
48	A	52	LEU	0	-0.017	0.014	17.757	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	53	ASN	0	0.067	0.023	21.080	0.017	0.017	0.000	0.000	0.000	0.000
50	A	54	CYS	0	0.019	-0.042	20.549	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	55	ASN	0	-0.035	-0.023	25.922	0.008	0.008	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.892	0.961	26.592	0.110	0.110	0.000	0.000	0.000	0.000
53	A	57	GLU	-1	-0.730	-0.770	21.269	-0.191	-0.191	0.000	0.000	0.000	0.000
54	A	58	SER	0	-0.082	-0.035	21.794	0.006	0.006	0.000	0.000	0.000	0.000
55	A	59	LEU	0	0.048	0.022	14.430	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	60	GLU	-1	-0.948	-0.973	18.857	-0.163	-0.163	0.000	0.000	0.000	0.000
57	A	61	ILE	0	-0.008	0.004	14.413	-0.028	-0.028	0.000	0.000	0.000	0.000
58	A	62	ILE	0	-0.028	-0.023	17.781	0.027	0.027	0.000	0.000	0.000	0.000
59	A	63	ASP	-1	-0.724	-0.800	18.235	-0.228	-0.228	0.000	0.000	0.000	0.000
60	A	64	GLY	0	0.070	0.035	19.144	0.019	0.019	0.000	0.000	0.000	0.000
61	A	65	LEU	0	-0.024	0.006	19.602	-0.019	-0.019	0.000	0.000	0.000	0.000
62	A	66	PRO	0	0.007	-0.019	20.957	0.005	0.005	0.000	0.000	0.000	0.000
63	A	67	GLY	0	0.000	0.000	23.467	0.010	0.010	0.000	0.000	0.000	0.000
64	A	68	SER	0	-0.040	0.004	22.822	0.011	0.011	0.000	0.000	0.000	0.000
65	A	69	PRO	0	0.014	-0.004	24.236	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	70	VAL	0	0.010	0.016	22.451	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	71	LEU	0	-0.025	-0.019	17.940	0.007	0.007	0.000	0.000	0.000	0.000
68	A	72	GLY	0	0.028	0.012	20.939	0.006	0.006	0.000	0.000	0.000	0.000
69	A	73	LYS	1	0.957	0.990	20.612	0.134	0.134	0.000	0.000	0.000	0.000
70	A	74	ILE	0	-0.013	-0.009	16.674	0.013	0.013	0.000	0.000	0.000	0.000
71	A	76	GLU	-1	-0.945	-0.964	20.494	-0.158	-0.158	0.000	0.000	0.000	0.000
72	A	77	GLY	0	0.027	0.015	19.397	0.012	0.012	0.000	0.000	0.000	0.000
73	A	78	SER	0	-0.046	-0.024	16.003	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.024	-0.015	14.343	0.008	0.008	0.000	0.000	0.000	0.000
75	A	80	MET	0	-0.039	0.001	14.385	0.017	0.017	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.810	-0.900	12.172	-0.405	-0.405	0.000	0.000	0.000	0.000
77	A	82	TYR	0	-0.005	-0.009	13.050	0.047	0.047	0.000	0.000	0.000	0.000
78	A	83	ARG	1	0.887	0.938	13.296	0.193	0.193	0.000	0.000	0.000	0.000
79	A	84	SER	0	-0.016	-0.008	15.148	0.013	0.013	0.000	0.000	0.000	0.000
80	A	85	SER	0	-0.045	-0.094	17.059	0.010	0.010	0.000	0.000	0.000	0.000
81	A	86	GLY	0	-0.002	0.002	19.606	0.017	0.017	0.000	0.000	0.000	0.000
82	A	87	SER	0	0.035	0.037	17.084	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	88	ILE	0	-0.073	-0.046	16.100	-0.020	-0.020	0.000	0.000	0.000	0.000
84	A	89	MET	0	0.008	0.025	13.469	0.024	0.024	0.000	0.000	0.000	0.000
85	A	90	THR	0	-0.056	-0.043	15.182	-0.025	-0.025	0.000	0.000	0.000	0.000
86	A	91	VAL	0	0.017	0.019	12.353	0.009	0.009	0.000	0.000	0.000	0.000
87	A	92	LYS	1	0.923	0.967	15.621	0.180	0.180	0.000	0.000	0.000	0.000
88	A	93	TYR	0	-0.022	-0.044	17.075	0.002	0.002	0.000	0.000	0.000	0.000
89	A	94	ILE	0	-0.016	-0.015	18.956	0.011	0.011	0.000	0.000	0.000	0.000
90	A	95	ARG	1	0.864	0.937	22.197	0.140	0.140	0.000	0.000	0.000	0.000
91	A	96	GLU	-1	-0.876	-0.949	24.431	-0.094	-0.094	0.000	0.000	0.000	0.000
92	A	97	PRO	0	-0.017	-0.020	26.982	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	98	GLU	-1	-0.964	-0.977	28.461	-0.075	-0.075	0.000	0.000	0.000	0.000
94	A	99	HIS	0	-0.063	-0.023	23.587	0.014	0.014	0.000	0.000	0.000	0.000
95	A	100	PRO	0	-0.003	0.006	23.536	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	101	ALA	0	0.005	-0.002	18.990	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	102	SER	0	-0.027	-0.062	19.377	0.008	0.008	0.000	0.000	0.000	0.000
98	A	103	PHE	0	-0.033	-0.009	11.215	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	104	TYR	0	0.014	0.001	12.764	0.010	0.010	0.000	0.000	0.000	0.000
100	A	105	GLU	-1	-0.850	-0.933	7.391	-0.792	-0.792	0.000	0.000	0.000	0.000
101	A	106	VAL	0	-0.056	-0.017	9.073	0.065	0.065	0.000	0.000	0.000	0.000
102	A	107	LEU	0	0.011	0.010	3.223	-0.528	-0.163	0.035	-0.074	-0.326	0.000
103	A	108	TYR	0	-0.011	-0.011	4.840	0.249	0.249	0.000	0.000	0.000	0.000
104	A	109	PHE	0	0.003	-0.007	3.256	-1.141	-0.535	0.042	-0.123	-0.525	0.000
105	A	110	GLN	0	0.000	0.014	6.989	0.149	0.149	0.000	0.000	0.000	0.000
106	A	111	ASP	-1	-0.833	-0.874	9.815	-0.322	-0.322	0.000	0.000	0.000	0.000
107	A	112	PRO	0	0.038	-0.013	12.478	0.029	0.029	0.000	0.000	0.000	0.000
108	A	113	GLN	0	-0.055	-0.058	6.593	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	114	ALA	0	-0.042	-0.029	10.354	0.050	0.050	0.000	0.000	0.000	0.000

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