FMO DATABASE

FMODB ID: G6751

Calculation Name: 1SMX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SMX

Chain ID: A

ChEMBL ID:

UniProt ID: P21513

Base Structure: X-ray

Registration Date: 2023-06-26

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	87
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-570754.251294
FMO2-HF: Nuclear repulsion	537712.535727
FMO2-HF: Total energy	-33041.715567
FMO2-MP2: Total energy	-33140.85782

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:39:ALA)

Summations of interaction energy for fragment #1(A:39:ALA)

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.
-2.513	0.603	-0.015	-1.608	-1.492	0.003

Interaction energy analysis for fragmet #1(A:39:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.026 / q_NPA : 0.012

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	41	ILE	0	0.010	0.009	3.355	-1.189	1.836	-0.014	-1.596	-1.415	0.003
4	A	42	TYR	0	0.009	0.015	4.903	-0.144	-0.053	-0.001	-0.012	-0.077	0.000
5	A	43	LYS	1	0.900	0.945	7.668	0.360	0.360	0.000	0.000	0.000	0.000
6	A	44	GLY	0	0.016	0.008	10.986	-0.036	-0.036	0.000	0.000	0.000	0.000
7	A	45	LYS	1	0.827	0.904	13.490	0.300	0.300	0.000	0.000	0.000	0.000
8	A	46	ILE	0	-0.004	-0.002	17.026	-0.026	-0.026	0.000	0.000	0.000	0.000
9	A	47	THR	0	-0.039	-0.024	19.463	0.033	0.033	0.000	0.000	0.000	0.000
10	A	48	ARG	1	0.887	0.928	22.024	0.224	0.224	0.000	0.000	0.000	0.000
11	A	49	ILE	0	-0.048	-0.003	23.776	-0.021	-0.021	0.000	0.000	0.000	0.000
12	A	50	GLU	-1	-0.833	-0.911	25.858	-0.184	-0.184	0.000	0.000	0.000	0.000
13	A	51	PRO	0	0.012	-0.012	28.003	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	52	SER	0	-0.029	-0.008	30.182	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	53	LEU	0	-0.020	-0.012	27.221	0.001	0.001	0.000	0.000	0.000	0.000
16	A	54	GLU	-1	-0.824	-0.864	27.050	-0.185	-0.185	0.000	0.000	0.000	0.000
17	A	55	ALA	0	0.016	0.006	23.065	-0.016	-0.016	0.000	0.000	0.000	0.000
18	A	56	ALA	0	0.012	0.003	21.142	0.026	0.026	0.000	0.000	0.000	0.000
19	A	57	PHE	0	-0.022	-0.004	20.195	-0.034	-0.034	0.000	0.000	0.000	0.000
20	A	58	VAL	0	-0.001	-0.006	14.998	0.027	0.027	0.000	0.000	0.000	0.000
21	A	59	ASP	-1	-0.814	-0.897	15.153	-0.527	-0.527	0.000	0.000	0.000	0.000
22	A	60	TYR	0	-0.029	-0.036	9.398	0.028	0.028	0.000	0.000	0.000	0.000
23	A	61	GLY	0	0.021	0.016	10.153	-0.156	-0.156	0.000	0.000	0.000	0.000
24	A	62	ALA	0	-0.044	-0.001	11.392	0.000	0.000	0.000	0.000	0.000	0.000
25	A	63	GLU	-1	-0.911	-0.959	12.686	-0.303	-0.303	0.000	0.000	0.000	0.000
26	A	64	ARG	1	0.801	0.910	15.945	0.531	0.531	0.000	0.000	0.000	0.000
27	A	65	HIS	0	0.008	0.000	15.483	-0.060	-0.060	0.000	0.000	0.000	0.000
28	A	66	GLY	0	0.020	0.003	15.302	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	67	PHE	0	-0.072	-0.037	16.229	0.075	0.075	0.000	0.000	0.000	0.000
30	A	68	LEU	0	0.027	0.017	16.092	-0.051	-0.051	0.000	0.000	0.000	0.000
31	A	69	PRO	0	0.001	-0.009	18.774	0.047	0.047	0.000	0.000	0.000	0.000
32	A	70	LEU	0	0.070	0.023	21.009	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	71	LYS	1	0.805	0.876	21.011	0.326	0.326	0.000	0.000	0.000	0.000
34	A	72	GLU	-1	-0.810	-0.855	17.560	-0.373	-0.373	0.000	0.000	0.000	0.000
35	A	73	ILE	0	-0.022	0.018	17.927	-0.033	-0.033	0.000	0.000	0.000	0.000
36	A	74	ALA	0	0.013	0.018	18.158	0.029	0.029	0.000	0.000	0.000	0.000
37	A	75	ARG	1	0.967	0.956	20.129	0.144	0.144	0.000	0.000	0.000	0.000
38	A	76	GLU	-1	-0.872	-0.931	18.604	-0.146	-0.146	0.000	0.000	0.000	0.000
39	A	77	TYR	0	-0.015	-0.013	14.866	0.003	0.003	0.000	0.000	0.000	0.000
40	A	78	PHE	0	-0.068	-0.030	21.686	0.002	0.002	0.000	0.000	0.000	0.000
41	A	79	PRO	0	-0.011	0.007	25.326	0.009	0.009	0.000	0.000	0.000	0.000
42	A	80	ALA	0	0.010	0.006	27.883	0.012	0.012	0.000	0.000	0.000	0.000
43	A	81	ASN	0	-0.030	-0.011	29.534	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	82	TYR	0	-0.007	-0.024	29.129	0.008	0.008	0.000	0.000	0.000	0.000
45	A	83	SER	0	-0.020	-0.014	32.659	0.007	0.007	0.000	0.000	0.000	0.000
46	A	84	ALA	0	-0.006	-0.005	33.218	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	85	HIS	0	-0.014	0.001	33.896	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	86	GLY	0	0.020	0.012	34.410	0.001	0.001	0.000	0.000	0.000	0.000
49	A	87	ARG	1	0.799	0.857	28.624	0.153	0.153	0.000	0.000	0.000	0.000
50	A	88	PRO	0	0.002	0.018	28.752	0.006	0.006	0.000	0.000	0.000	0.000
51	A	89	ASN	0	0.091	0.036	30.306	-0.019	-0.019	0.000	0.000	0.000	0.000
52	A	90	ILE	0	0.025	0.021	23.161	0.003	0.003	0.000	0.000	0.000	0.000
53	A	91	LYS	1	0.859	0.923	26.845	0.163	0.163	0.000	0.000	0.000	0.000
54	A	92	ASP	-1	-0.909	-0.929	29.210	-0.114	-0.114	0.000	0.000	0.000	0.000
55	A	93	VAL	0	-0.085	-0.039	23.787	0.007	0.007	0.000	0.000	0.000	0.000
56	A	94	LEU	0	0.016	0.008	20.728	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	95	ARG	1	0.957	0.970	23.755	0.138	0.138	0.000	0.000	0.000	0.000
58	A	96	GLU	-1	-0.789	-0.918	23.306	-0.200	-0.200	0.000	0.000	0.000	0.000
59	A	97	GLY	0	-0.023	-0.010	21.837	0.018	0.018	0.000	0.000	0.000	0.000
60	A	98	GLN	0	0.022	0.015	19.913	0.002	0.002	0.000	0.000	0.000	0.000
61	A	99	GLU	-1	-0.859	-0.920	15.466	-0.237	-0.237	0.000	0.000	0.000	0.000
62	A	100	VAL	0	-0.001	0.003	14.868	0.039	0.039	0.000	0.000	0.000	0.000
63	A	101	ILE	0	-0.005	-0.002	9.794	-0.056	-0.056	0.000	0.000	0.000	0.000
64	A	102	VAL	0	-0.012	-0.016	10.363	0.043	0.043	0.000	0.000	0.000	0.000
65	A	103	GLN	0	0.080	0.059	8.134	-0.183	-0.183	0.000	0.000	0.000	0.000
66	A	104	ILE	0	-0.002	-0.010	7.753	0.342	0.342	0.000	0.000	0.000	0.000
67	A	105	ASP	-1	-0.835	-0.901	9.934	-0.665	-0.665	0.000	0.000	0.000	0.000
68	A	106	LYS	1	0.739	0.850	12.702	0.689	0.689	0.000	0.000	0.000	0.000
69	A	107	GLU	-1	-0.857	-0.939	8.602	-1.882	-1.882	0.000	0.000	0.000	0.000
70	A	108	GLU	-1	-0.907	-0.957	12.465	-0.553	-0.553	0.000	0.000	0.000	0.000
71	A	109	ARG	1	0.949	0.971	14.279	0.586	0.586	0.000	0.000	0.000	0.000
72	A	110	GLY	0	0.014	0.012	17.518	0.042	0.042	0.000	0.000	0.000	0.000
73	A	111	ASN	0	0.010	-0.004	20.035	-0.026	-0.026	0.000	0.000	0.000	0.000
74	A	112	LYS	1	0.930	0.978	19.673	0.384	0.384	0.000	0.000	0.000	0.000
75	A	113	GLY	0	0.095	0.043	17.101	-0.033	-0.033	0.000	0.000	0.000	0.000
76	A	114	ALA	0	0.009	0.017	12.754	0.031	0.031	0.000	0.000	0.000	0.000
77	A	115	ALA	0	-0.041	-0.016	14.734	0.083	0.083	0.000	0.000	0.000	0.000
78	A	116	LEU	0	0.021	0.004	11.803	-0.119	-0.119	0.000	0.000	0.000	0.000
79	A	117	THR	0	-0.007	-0.036	12.959	0.118	0.118	0.000	0.000	0.000	0.000
80	A	118	THR	0	-0.022	-0.028	12.898	-0.073	-0.073	0.000	0.000	0.000	0.000
81	A	119	PHE	0	-0.026	0.002	14.314	0.054	0.054	0.000	0.000	0.000	0.000
82	A	120	ILE	0	-0.037	-0.009	8.791	-0.081	-0.081	0.000	0.000	0.000	0.000
83	A	121	SER	0	-0.019	-0.028	9.049	0.136	0.136	0.000	0.000	0.000	0.000
84	A	122	LEU	0	-0.010	-0.001	9.122	0.059	0.059	0.000	0.000	0.000	0.000
85	A	123	ALA	0	0.016	0.014	10.957	-0.026	-0.026	0.000	0.000	0.000	0.000
86	A	124	GLY	0	-0.008	-0.009	12.922	0.026	0.026	0.000	0.000	0.000	0.000
87	A	125	SER	0	-0.034	-0.010	14.559	-0.026	-0.026	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:39:ALA)