FMO DATABASE

FMODB ID: 3JZVL

Calculation Name: 1S7O-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1S7O

Chain ID: A

ChEMBL ID:

UniProt ID: P67253

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptAll
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	106
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-823059.440849
FMO2-HF: Nuclear repulsion	777872.168954
FMO2-HF: Total energy	-45187.271894
FMO2-MP2: Total energy	-45317.479746

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:7:GLU)

Summations of interaction energy for fragment #1(A:7: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.
-23.609	-35.611	46.341	-19.837	-14.499	0.233

Interaction energy analysis for fragmet #1(A:7:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.790 / q_NPA : -0.879

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	9	THR	0	-0.009	-0.009	3.894	-2.339	-1.050	-0.014	-0.576	-0.699	0.002
4	A	10	ASN	0	0.078	0.026	6.497	0.059	0.059	0.000	0.000	0.000	0.000
5	A	11	ARG	1	0.824	0.900	9.490	-26.985	-26.985	0.000	0.000	0.000	0.000
6	A	12	MET	0	-0.014	0.007	5.653	-2.499	-2.499	0.000	0.000	0.000	0.000
7	A	13	ASN	0	-0.045	-0.019	8.244	-0.334	-0.334	0.000	0.000	0.000	0.000
8	A	14	ALA	0	0.085	0.047	10.177	-1.057	-1.057	0.000	0.000	0.000	0.000
9	A	15	LEU	0	-0.051	-0.029	10.446	-1.021	-1.021	0.000	0.000	0.000	0.000
10	A	16	PHE	0	-0.005	-0.012	10.602	-0.806	-0.806	0.000	0.000	0.000	0.000
11	A	17	GLU	-1	-0.860	-0.945	12.464	17.124	17.124	0.000	0.000	0.000	0.000
12	A	18	PHE	0	-0.019	-0.001	15.530	-0.925	-0.925	0.000	0.000	0.000	0.000
13	A	19	TYR	0	-0.039	-0.064	14.486	-1.232	-1.232	0.000	0.000	0.000	0.000
14	A	20	ALA	0	0.031	0.012	14.828	-0.073	-0.073	0.000	0.000	0.000	0.000
15	A	21	ALA	0	-0.022	-0.011	16.243	-0.418	-0.418	0.000	0.000	0.000	0.000
16	A	22	LEU	0	-0.058	-0.016	18.572	-0.830	-0.830	0.000	0.000	0.000	0.000
17	A	23	LEU	0	-0.038	0.007	13.836	0.582	0.582	0.000	0.000	0.000	0.000
18	A	24	THR	0	-0.025	-0.038	18.299	-0.774	-0.774	0.000	0.000	0.000	0.000
19	A	25	ASP	-1	-0.724	-0.877	18.239	14.821	14.821	0.000	0.000	0.000	0.000
20	A	26	LYS	1	0.798	0.885	18.115	-13.222	-13.222	0.000	0.000	0.000	0.000
21	A	27	GLN	0	-0.003	0.029	14.771	0.256	0.256	0.000	0.000	0.000	0.000
22	A	28	MET	0	0.038	0.046	13.487	2.153	2.153	0.000	0.000	0.000	0.000
23	A	29	ASN	0	0.000	0.006	14.233	0.307	0.307	0.000	0.000	0.000	0.000
24	A	30	TYR	0	0.005	0.000	11.062	0.344	0.344	0.000	0.000	0.000	0.000
25	A	31	ILE	0	-0.005	0.002	8.241	1.108	1.108	0.000	0.000	0.000	0.000
26	A	32	GLU	-1	-0.882	-0.952	10.577	16.745	16.745	0.000	0.000	0.000	0.000
27	A	33	LEU	0	0.010	0.005	12.974	0.100	0.100	0.000	0.000	0.000	0.000
28	A	34	TYR	0	-0.074	-0.046	2.672	-0.827	0.815	0.152	-0.694	-1.100	-0.004
29	A	35	TYR	0	-0.092	-0.086	4.495	0.166	0.234	-0.001	-0.007	-0.059	0.000
30	A	36	ALA	0	-0.020	-0.010	10.275	-0.437	-0.437	0.000	0.000	0.000	0.000
31	A	37	ASP	-1	-0.883	-0.932	13.512	14.465	14.465	0.000	0.000	0.000	0.000
32	A	38	ASP	-1	-0.945	-0.955	9.911	21.171	21.171	0.000	0.000	0.000	0.000
33	A	39	TYR	0	-0.021	0.006	10.769	0.075	0.075	0.000	0.000	0.000	0.000
34	A	40	SER	0	-0.042	-0.067	7.484	2.420	2.420	0.000	0.000	0.000	0.000
35	A	41	LEU	0	-0.026	-0.045	4.108	-0.459	-0.315	-0.001	-0.017	-0.127	0.000
36	A	42	ALA	0	-0.071	-0.036	7.958	-0.424	-0.424	0.000	0.000	0.000	0.000
37	A	43	GLU	-1	-0.748	-0.836	11.045	18.491	18.491	0.000	0.000	0.000	0.000
38	A	44	ILE	0	0.043	0.032	9.520	-0.601	-0.601	0.000	0.000	0.000	0.000
39	A	45	ALA	0	-0.070	-0.047	12.397	-0.342	-0.342	0.000	0.000	0.000	0.000
40	A	46	ASP	-1	-0.925	-0.967	14.090	15.808	15.808	0.000	0.000	0.000	0.000
41	A	47	GLU	-1	-0.944	-0.975	16.153	15.392	15.392	0.000	0.000	0.000	0.000
42	A	48	PHE	0	-0.025	-0.020	16.433	-0.693	-0.693	0.000	0.000	0.000	0.000
43	A	49	GLY	0	-0.025	0.011	18.774	-0.363	-0.363	0.000	0.000	0.000	0.000
44	A	50	VAL	0	-0.066	-0.022	14.810	-0.172	-0.172	0.000	0.000	0.000	0.000
45	A	51	SER	0	0.008	-0.008	14.997	0.672	0.672	0.000	0.000	0.000	0.000
46	A	52	ARG	1	1.031	0.994	6.517	-29.803	-29.803	0.000	0.000	0.000	0.000
47	A	53	GLN	0	-0.111	-0.055	9.766	1.447	1.447	0.000	0.000	0.000	0.000
48	A	54	ALA	0	0.013	0.009	10.218	2.131	2.131	0.000	0.000	0.000	0.000
49	A	55	VAL	0	0.040	0.029	8.997	0.549	0.549	0.000	0.000	0.000	0.000
50	A	56	TYR	0	-0.043	-0.033	1.592	-26.102	-35.520	21.234	-7.098	-4.718	0.085
51	A	57	ASP	-1	-0.843	-0.932	7.179	34.746	34.746	0.000	0.000	0.000	0.000
52	A	58	ASN	0	-0.132	-0.068	9.134	-0.037	-0.037	0.000	0.000	0.000	0.000
53	A	59	ILE	0	0.087	0.054	5.711	-0.610	-0.610	0.000	0.000	0.000	0.000
54	A	60	LYS	1	0.827	0.909	1.803	-149.184	-155.116	24.971	-11.383	-7.655	0.150
55	A	61	ARG	1	0.830	0.919	6.843	-26.777	-26.777	0.000	0.000	0.000	0.000
56	A	62	THR	0	0.030	-0.004	10.428	-1.171	-1.171	0.000	0.000	0.000	0.000
57	A	63	GLU	-1	-0.781	-0.896	4.269	52.869	53.074	0.000	-0.062	-0.141	0.000
58	A	64	LYS	1	0.914	0.963	8.311	-35.097	-35.097	0.000	0.000	0.000	0.000
59	A	65	ILE	0	-0.054	-0.007	9.990	-2.626	-2.626	0.000	0.000	0.000	0.000
60	A	66	LEU	0	0.027	0.021	9.457	-1.527	-1.527	0.000	0.000	0.000	0.000
61	A	67	GLU	-1	-0.758	-0.846	8.986	27.821	27.821	0.000	0.000	0.000	0.000
62	A	68	THR	0	-0.110	-0.071	12.083	-2.308	-2.308	0.000	0.000	0.000	0.000
63	A	69	TYR	0	-0.054	-0.039	15.141	-1.681	-1.681	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.691	-0.807	14.317	16.814	16.814	0.000	0.000	0.000	0.000
65	A	71	MET	0	-0.063	-0.042	14.947	-0.646	-0.646	0.000	0.000	0.000	0.000
66	A	72	LYS	1	0.837	0.923	17.523	-16.734	-16.734	0.000	0.000	0.000	0.000
67	A	73	LEU	0	-0.048	-0.023	19.694	-0.867	-0.867	0.000	0.000	0.000	0.000
68	A	74	HIS	0	-0.051	-0.015	19.019	-0.357	-0.357	0.000	0.000	0.000	0.000
69	A	75	MET	0	0.019	0.027	18.948	-0.276	-0.276	0.000	0.000	0.000	0.000
70	A	76	TYR	0	0.038	0.011	13.993	0.438	0.438	0.000	0.000	0.000	0.000
71	A	77	SER	0	-0.041	-0.051	17.318	-0.512	-0.512	0.000	0.000	0.000	0.000
72	A	78	ASP	-1	-0.836	-0.911	18.760	11.819	11.819	0.000	0.000	0.000	0.000
73	A	79	TYR	0	-0.019	-0.013	18.656	-0.237	-0.237	0.000	0.000	0.000	0.000
74	A	80	VAL	0	-0.047	-0.008	17.082	-0.292	-0.292	0.000	0.000	0.000	0.000
75	A	81	VAL	0	0.027	0.020	20.433	-0.530	-0.530	0.000	0.000	0.000	0.000
76	A	82	ARG	1	0.735	0.841	23.599	-12.590	-12.590	0.000	0.000	0.000	0.000
77	A	83	SER	0	-0.001	-0.012	22.368	-0.487	-0.487	0.000	0.000	0.000	0.000
78	A	84	GLU	-1	-0.937	-0.969	21.683	13.413	13.413	0.000	0.000	0.000	0.000
79	A	85	ILE	0	-0.010	-0.004	25.125	-0.534	-0.534	0.000	0.000	0.000	0.000
80	A	86	PHE	0	-0.022	-0.029	27.100	-0.521	-0.521	0.000	0.000	0.000	0.000
81	A	87	ASP	-1	-0.861	-0.931	25.282	11.129	11.129	0.000	0.000	0.000	0.000
82	A	88	ASP	-1	-0.928	-0.961	28.645	9.884	9.884	0.000	0.000	0.000	0.000
83	A	89	MET	0	-0.118	-0.062	30.932	-0.403	-0.403	0.000	0.000	0.000	0.000
84	A	90	ILE	0	0.001	-0.006	29.603	-0.390	-0.390	0.000	0.000	0.000	0.000
85	A	91	ALA	0	-0.035	-0.016	31.753	-0.293	-0.293	0.000	0.000	0.000	0.000
86	A	92	HIS	0	-0.075	-0.032	33.711	-0.316	-0.316	0.000	0.000	0.000	0.000
87	A	93	TYR	0	-0.067	-0.028	36.402	-0.423	-0.423	0.000	0.000	0.000	0.000
88	A	94	PRO	0	0.032	0.005	36.364	-0.049	-0.049	0.000	0.000	0.000	0.000
89	A	95	HIS	0	-0.042	-0.025	37.741	-0.067	-0.067	0.000	0.000	0.000	0.000
90	A	96	ASP	-1	-0.864	-0.917	39.937	7.296	7.296	0.000	0.000	0.000	0.000
91	A	97	GLU	-1	-0.885	-0.951	39.459	7.257	7.257	0.000	0.000	0.000	0.000
92	A	98	TYR	0	0.000	0.004	39.829	0.139	0.139	0.000	0.000	0.000	0.000
93	A	99	LEU	0	-0.010	-0.012	36.665	0.115	0.115	0.000	0.000	0.000	0.000
94	A	100	GLN	0	0.002	0.006	35.432	0.283	0.283	0.000	0.000	0.000	0.000
95	A	101	GLU	-1	-0.839	-0.923	34.894	8.634	8.634	0.000	0.000	0.000	0.000
96	A	102	LYS	1	0.760	0.882	35.592	-7.698	-7.698	0.000	0.000	0.000	0.000
97	A	103	ILE	0	0.047	0.030	30.604	0.200	0.200	0.000	0.000	0.000	0.000
98	A	104	SER	0	-0.047	0.006	30.771	0.489	0.489	0.000	0.000	0.000	0.000
99	A	105	ILE	0	-0.003	-0.002	30.861	0.294	0.294	0.000	0.000	0.000	0.000
100	A	106	LEU	0	-0.002	0.007	30.107	0.201	0.201	0.000	0.000	0.000	0.000
101	A	107	THR	0	0.041	0.011	25.765	0.469	0.469	0.000	0.000	0.000	0.000
102	A	108	SER	0	-0.107	-0.062	26.245	0.391	0.391	0.000	0.000	0.000	0.000
103	A	109	ILE	0	-0.035	-0.018	27.618	0.078	0.078	0.000	0.000	0.000	0.000
104	A	110	ASP	-1	-0.796	-0.886	23.985	12.375	12.375	0.000	0.000	0.000	0.000
105	A	111	ASN	0	-0.063	-0.013	21.784	1.093	1.093	0.000	0.000	0.000	0.000
106	A	112	ARG	1	0.865	0.934	23.287	-10.264	-10.264	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLU)