FMO DATABASE

FMODB ID: V5QZ1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-892869.917427
FMO2-HF: Nuclear repulsion	848092.065622
FMO2-HF: Total energy	-44777.851805
FMO2-MP2: Total energy	-44904.944303

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.
-6.188	-0.417	3.878	-2.682	-6.971	-0.01

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 : -0.019 / q_NPA : -0.018

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	0.885	0.924	3.790	-0.366	0.957	-0.003	-0.481	-0.840	0.003
4	A	7	ASN	0	-0.012	-0.017	5.854	0.540	0.540	0.000	0.000	0.000	0.000
5	A	8	THR	0	0.054	0.024	8.792	-0.017	-0.017	0.000	0.000	0.000	0.000
6	A	9	ASN	0	-0.001	0.001	11.964	0.089	0.089	0.000	0.000	0.000	0.000
7	A	10	CYS	0	-0.136	-0.058	14.491	-0.010	-0.010	0.000	0.000	0.000	0.000
8	A	11	GLY	0	0.014	0.002	15.145	0.032	0.032	0.000	0.000	0.000	0.000
9	A	12	GLY	0	-0.020	-0.012	15.186	0.005	0.005	0.000	0.000	0.000	0.000
10	A	13	ILE	0	-0.035	-0.020	14.795	-0.029	-0.029	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.037	-0.009	9.028	0.023	0.023	0.000	0.000	0.000	0.000
12	A	15	LYS	1	0.908	0.931	11.170	0.148	0.148	0.000	0.000	0.000	0.000
13	A	16	GLU	-1	-0.927	-0.940	5.952	0.025	0.025	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.784	-0.899	6.672	-0.316	-0.316	0.000	0.000	0.000	0.000
15	A	18	SER	0	0.018	0.002	2.654	-1.747	-0.493	1.167	-0.848	-1.574	-0.005
16	A	19	GLY	0	0.009	0.011	2.382	-1.381	-0.133	0.935	-0.832	-1.351	-0.005
17	A	20	VAL	0	-0.041	-0.020	2.406	-0.707	-0.091	1.626	-0.261	-1.981	-0.003
18	A	21	ILE	0	-0.001	0.012	4.733	0.048	0.076	-0.001	-0.008	-0.020	0.000
19	A	22	ALA	0	0.001	-0.001	8.457	0.029	0.029	0.000	0.000	0.000	0.000
20	A	23	THR	0	-0.001	-0.005	10.315	0.024	0.024	0.000	0.000	0.000	0.000
21	A	24	TYR	0	-0.034	0.007	13.975	0.018	0.018	0.000	0.000	0.000	0.000
22	A	25	TYR	0	0.016	-0.007	15.379	0.009	0.009	0.000	0.000	0.000	0.000
23	A	26	GLY	0	-0.034	-0.015	18.935	0.023	0.023	0.000	0.000	0.000	0.000
24	A	27	PRO	0	0.025	-0.002	21.500	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.918	0.964	20.424	0.146	0.146	0.000	0.000	0.000	0.000
26	A	29	THR	0	0.055	0.026	22.596	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	30	ASN	0	0.006	0.006	22.201	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	32	VAL	0	0.046	0.015	17.987	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	33	TRP	0	0.020	0.014	12.394	0.016	0.016	0.000	0.000	0.000	0.000
30	A	34	THR	0	-0.029	-0.022	14.773	0.007	0.007	0.000	0.000	0.000	0.000
31	A	35	ILE	0	0.007	0.010	10.102	0.008	0.008	0.000	0.000	0.000	0.000
32	A	36	GLN	0	0.008	-0.001	13.121	0.054	0.054	0.000	0.000	0.000	0.000
33	A	37	MET	0	-0.001	0.022	8.459	0.029	0.029	0.000	0.000	0.000	0.000
34	A	38	PRO	0	0.009	-0.006	13.352	0.027	0.027	0.000	0.000	0.000	0.000
35	A	39	PRO	0	0.043	0.007	16.570	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	40	GLU	-1	-0.978	-0.982	19.277	-0.081	-0.081	0.000	0.000	0.000	0.000
37	A	41	TYR	0	-0.054	-0.011	13.941	0.005	0.005	0.000	0.000	0.000	0.000
38	A	42	HIS	0	-0.039	-0.029	14.955	0.021	0.021	0.000	0.000	0.000	0.000
39	A	43	VAL	0	-0.010	-0.009	10.701	-0.041	-0.041	0.000	0.000	0.000	0.000
40	A	44	ARG	1	0.782	0.872	9.586	0.386	0.386	0.000	0.000	0.000	0.000
41	A	45	VAL	0	-0.016	-0.025	8.960	-0.118	-0.118	0.000	0.000	0.000	0.000
42	A	46	SER	0	-0.007	-0.004	8.016	0.057	0.057	0.000	0.000	0.000	0.000
43	A	47	ILE	0	-0.015	-0.004	8.740	-0.071	-0.071	0.000	0.000	0.000	0.000
44	A	48	GLN	0	0.011	0.006	9.411	0.072	0.072	0.000	0.000	0.000	0.000
45	A	49	TYR	0	0.034	0.001	11.625	0.046	0.046	0.000	0.000	0.000	0.000
46	A	50	LEU	0	-0.049	-0.012	13.741	-0.035	-0.035	0.000	0.000	0.000	0.000
47	A	51	GLN	0	-0.012	-0.023	16.075	0.016	0.016	0.000	0.000	0.000	0.000
48	A	52	LEU	0	-0.031	0.008	17.513	0.000	0.000	0.000	0.000	0.000	0.000
49	A	53	ASN	0	0.038	0.011	20.823	0.017	0.017	0.000	0.000	0.000	0.000
50	A	54	CYS	0	0.005	-0.027	20.261	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	55	ASN	0	-0.061	-0.029	25.665	0.009	0.009	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.961	0.988	26.674	0.104	0.104	0.000	0.000	0.000	0.000
53	A	57	GLU	-1	-0.727	-0.805	21.090	-0.190	-0.190	0.000	0.000	0.000	0.000
54	A	58	SER	0	-0.068	-0.031	21.489	0.005	0.005	0.000	0.000	0.000	0.000
55	A	59	LEU	0	0.045	0.023	14.021	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	60	GLU	-1	-0.835	-0.896	18.519	-0.155	-0.155	0.000	0.000	0.000	0.000
57	A	61	ILE	0	0.024	0.023	14.083	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	62	ILE	0	-0.037	-0.030	17.529	0.028	0.028	0.000	0.000	0.000	0.000
59	A	63	ASP	-1	-0.737	-0.829	18.025	-0.226	-0.226	0.000	0.000	0.000	0.000
60	A	64	GLY	0	0.059	0.030	18.952	0.019	0.019	0.000	0.000	0.000	0.000
61	A	65	LEU	0	-0.020	0.007	19.388	-0.019	-0.019	0.000	0.000	0.000	0.000
62	A	66	PRO	0	0.025	0.007	20.871	0.005	0.005	0.000	0.000	0.000	0.000
63	A	67	GLY	0	-0.004	-0.001	23.216	0.010	0.010	0.000	0.000	0.000	0.000
64	A	68	SER	0	-0.050	-0.019	22.574	0.011	0.011	0.000	0.000	0.000	0.000
65	A	69	PRO	0	0.020	-0.003	24.210	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	70	VAL	0	-0.003	0.005	22.048	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	71	LEU	0	-0.014	-0.010	17.694	0.008	0.008	0.000	0.000	0.000	0.000
68	A	72	GLY	0	0.017	0.004	20.720	0.006	0.006	0.000	0.000	0.000	0.000
69	A	73	LYS	1	0.853	0.926	20.357	0.142	0.142	0.000	0.000	0.000	0.000
70	A	74	ILE	0	0.001	0.001	16.228	0.014	0.014	0.000	0.000	0.000	0.000
71	A	76	GLU	-1	-0.884	-0.943	20.230	-0.159	-0.159	0.000	0.000	0.000	0.000
72	A	77	GLY	0	0.023	0.017	19.191	0.012	0.012	0.000	0.000	0.000	0.000
73	A	78	SER	0	-0.025	-0.014	15.842	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.043	-0.022	14.198	0.009	0.009	0.000	0.000	0.000	0.000
75	A	80	MET	0	-0.027	0.006	14.258	0.019	0.019	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.793	-0.891	11.825	-0.418	-0.418	0.000	0.000	0.000	0.000
77	A	82	TYR	0	-0.005	-0.010	12.952	0.039	0.039	0.000	0.000	0.000	0.000
78	A	83	ARG	1	0.867	0.932	13.219	0.185	0.185	0.000	0.000	0.000	0.000
79	A	84	SER	0	0.003	0.007	15.085	0.010	0.010	0.000	0.000	0.000	0.000
80	A	85	SER	0	-0.061	-0.067	16.974	0.012	0.012	0.000	0.000	0.000	0.000
81	A	86	GLY	0	0.027	0.014	19.527	0.017	0.017	0.000	0.000	0.000	0.000
82	A	87	SER	0	0.022	0.022	16.846	-0.017	-0.017	0.000	0.000	0.000	0.000
83	A	88	ILE	0	-0.071	-0.044	15.877	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	89	MET	0	0.005	0.028	13.546	0.024	0.024	0.000	0.000	0.000	0.000
85	A	90	THR	0	-0.055	-0.038	14.961	-0.024	-0.024	0.000	0.000	0.000	0.000
86	A	91	VAL	0	0.013	0.020	11.959	0.010	0.010	0.000	0.000	0.000	0.000
87	A	92	LYS	1	0.862	0.922	15.323	0.179	0.179	0.000	0.000	0.000	0.000
88	A	93	TYR	0	-0.016	-0.030	16.974	0.001	0.001	0.000	0.000	0.000	0.000
89	A	94	ILE	0	-0.026	-0.018	18.880	0.011	0.011	0.000	0.000	0.000	0.000
90	A	95	ARG	1	0.876	0.948	21.771	0.137	0.137	0.000	0.000	0.000	0.000
91	A	96	GLU	-1	-0.867	-0.943	24.338	-0.095	-0.095	0.000	0.000	0.000	0.000
92	A	97	PRO	0	-0.023	-0.024	26.970	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	98	GLU	-1	-0.966	-0.982	28.441	-0.074	-0.074	0.000	0.000	0.000	0.000
94	A	99	HIS	0	-0.074	-0.035	23.580	0.014	0.014	0.000	0.000	0.000	0.000
95	A	100	PRO	0	-0.012	-0.001	23.452	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	101	ALA	0	0.006	-0.006	18.982	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	102	SER	0	-0.017	-0.032	19.324	0.007	0.007	0.000	0.000	0.000	0.000
98	A	103	PHE	0	-0.038	-0.017	10.878	-0.016	-0.016	0.000	0.000	0.000	0.000
99	A	104	TYR	0	0.004	-0.005	12.829	0.011	0.011	0.000	0.000	0.000	0.000
100	A	105	GLU	-1	-0.838	-0.911	6.979	-0.863	-0.863	0.000	0.000	0.000	0.000
101	A	106	VAL	0	-0.030	-0.013	8.760	0.068	0.068	0.000	0.000	0.000	0.000
102	A	107	LEU	0	0.015	0.015	3.193	-0.571	-0.169	0.035	-0.078	-0.359	0.000
103	A	108	TYR	0	-0.010	-0.012	4.612	0.098	0.208	-0.001	-0.007	-0.102	0.000
104	A	109	PHE	0	0.012	-0.009	2.949	-1.323	-0.533	0.120	-0.167	-0.744	0.000
105	A	110	GLN	0	-0.025	-0.005	7.012	0.167	0.167	0.000	0.000	0.000	0.000
106	A	111	ASP	-1	-0.841	-0.861	9.642	-0.307	-0.307	0.000	0.000	0.000	0.000
107	A	112	PRO	0	0.038	-0.009	12.342	0.027	0.027	0.000	0.000	0.000	0.000
108	A	113	GLN	0	-0.035	-0.052	6.143	-0.050	-0.050	0.000	0.000	0.000	0.000
109	A	114	ALA	0	-0.050	-0.028	10.395	0.048	0.048	0.000	0.000	0.000	0.000

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