FMO DATABASE

FMODB ID: N96NQ

Calculation Name: 1SJV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SJV

Chain ID: A

ChEMBL ID:

UniProt ID:

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	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	106
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-718071.576406
FMO2-HF: Nuclear repulsion	676282.560448
FMO2-HF: Total energy	-41789.015958
FMO2-MP2: Total energy	-41909.79262

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:8:GLY)

Summations of interaction energy for fragment #1(A:8:GLY)

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.
0.127	1.704	-0.028	-0.831	-0.718	-0.001

Interaction energy analysis for fragmet #1(A:8:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : -0.015

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	10	GLY	0	0.003	0.008	3.768	0.439	2.016	-0.028	-0.831	-0.718	-0.001
4	A	11	LEU	0	-0.015	0.005	7.038	-0.140	-0.140	0.000	0.000	0.000	0.000
5	A	12	VAL	0	0.006	0.001	10.668	0.114	0.114	0.000	0.000	0.000	0.000
6	A	13	GLN	0	-0.060	-0.037	13.382	-0.038	-0.038	0.000	0.000	0.000	0.000
7	A	14	ALA	0	-0.004	-0.008	17.095	0.009	0.009	0.000	0.000	0.000	0.000
8	A	15	GLY	0	0.001	-0.008	19.011	0.023	0.023	0.000	0.000	0.000	0.000
9	A	16	GLU	-1	-0.907	-0.937	16.440	-0.059	-0.059	0.000	0.000	0.000	0.000
10	A	17	SER	0	-0.019	-0.049	16.180	-0.034	-0.034	0.000	0.000	0.000	0.000
11	A	18	LEU	0	-0.036	-0.010	8.717	0.002	0.002	0.000	0.000	0.000	0.000
12	A	19	LYS	1	0.972	0.998	11.998	-0.329	-0.329	0.000	0.000	0.000	0.000
13	A	20	LEU	0	-0.022	0.003	7.573	0.186	0.186	0.000	0.000	0.000	0.000
14	A	21	SER	0	-0.026	-0.030	9.450	-0.131	-0.131	0.000	0.000	0.000	0.000
15	A	22	CYS	0	-0.025	0.002	9.221	0.297	0.297	0.000	0.000	0.000	0.000
16	A	23	ALA	0	0.055	0.027	11.332	-0.145	-0.145	0.000	0.000	0.000	0.000
17	A	24	ALA	0	0.005	0.003	13.331	0.010	0.010	0.000	0.000	0.000	0.000
18	A	24	SER	0	0.053	0.023	14.379	-0.026	-0.026	0.000	0.000	0.000	0.000
19	A	24	GLY	0	0.028	0.001	16.312	-0.048	-0.048	0.000	0.000	0.000	0.000
20	A	24	ASN	0	-0.017	-0.001	19.776	0.003	0.003	0.000	0.000	0.000	0.000
21	A	24	THR	0	0.011	-0.008	21.618	0.012	0.012	0.000	0.000	0.000	0.000
22	A	25	PHE	0	0.028	0.013	21.458	-0.017	-0.017	0.000	0.000	0.000	0.000
23	A	26	SER	0	-0.040	-0.021	24.005	0.001	0.001	0.000	0.000	0.000	0.000
24	A	27	GLY	0	0.035	0.014	22.853	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	28	GLY	0	0.005	0.002	23.539	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.033	-0.015	19.322	0.013	0.013	0.000	0.000	0.000	0.000
27	A	30	MET	0	0.032	0.032	16.377	0.004	0.004	0.000	0.000	0.000	0.000
28	A	31	GLY	0	0.017	-0.002	16.824	-0.016	-0.016	0.000	0.000	0.000	0.000
29	A	32	TRP	0	-0.010	0.022	8.973	0.017	0.017	0.000	0.000	0.000	0.000
30	A	33	TYR	0	0.006	0.002	12.910	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.848	0.927	11.677	0.284	0.284	0.000	0.000	0.000	0.000
32	A	35	GLN	0	-0.016	-0.011	11.589	0.043	0.043	0.000	0.000	0.000	0.000
33	A	36	ALA	0	0.057	0.046	11.766	-0.158	-0.158	0.000	0.000	0.000	0.000
34	A	37	PRO	0	0.023	-0.011	12.825	0.060	0.060	0.000	0.000	0.000	0.000
35	A	38	GLY	0	0.002	0.005	15.257	0.043	0.043	0.000	0.000	0.000	0.000
36	A	39	LYS	1	0.957	0.996	17.424	0.395	0.395	0.000	0.000	0.000	0.000
37	A	40	GLN	0	0.034	0.004	17.582	-0.046	-0.046	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.896	0.961	15.512	0.216	0.216	0.000	0.000	0.000	0.000
39	A	42	GLU	-1	-0.849	-0.928	16.168	-0.227	-0.227	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.034	-0.021	16.322	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	44	VAL	0	-0.008	0.001	14.377	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.030	0.006	17.336	0.015	0.015	0.000	0.000	0.000	0.000
43	A	46	THR	0	-0.027	-0.013	18.009	0.004	0.004	0.000	0.000	0.000	0.000
44	A	47	ILE	0	-0.030	-0.007	19.722	0.003	0.003	0.000	0.000	0.000	0.000
45	A	48	ASN	0	0.029	0.020	22.110	0.013	0.013	0.000	0.000	0.000	0.000
46	A	49	SER	0	0.017	-0.008	24.791	0.006	0.006	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.913	0.954	26.452	-0.041	-0.041	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.026	0.026	25.527	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	52	ILE	0	-0.033	-0.014	26.357	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.006	-0.012	23.311	0.000	0.000	0.000	0.000	0.000	0.000
51	A	54	ASN	0	0.013	0.000	23.074	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	55	TYR	0	0.040	0.018	19.919	0.015	0.015	0.000	0.000	0.000	0.000
53	A	56	ALA	0	0.031	0.035	20.622	0.000	0.000	0.000	0.000	0.000	0.000
54	A	57	ASP	-1	-0.848	-0.930	22.404	-0.076	-0.076	0.000	0.000	0.000	0.000
55	A	58	PHE	0	-0.008	-0.018	17.767	0.009	0.009	0.000	0.000	0.000	0.000
56	A	59	VAL	0	-0.022	0.012	19.329	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	60	LYS	1	0.922	0.955	21.672	0.100	0.100	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.011	0.010	24.474	0.003	0.003	0.000	0.000	0.000	0.000
59	A	62	ARG	1	0.794	0.888	19.189	0.174	0.174	0.000	0.000	0.000	0.000
60	A	63	PHE	0	0.005	-0.002	16.448	0.013	0.013	0.000	0.000	0.000	0.000
61	A	64	THR	0	-0.041	-0.020	18.685	0.005	0.005	0.000	0.000	0.000	0.000
62	A	65	ILE	0	-0.041	-0.006	17.184	0.028	0.028	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.015	-0.011	18.252	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	67	ARG	1	0.937	0.975	18.482	-0.124	-0.124	0.000	0.000	0.000	0.000
65	A	68	ASP	-1	-0.825	-0.921	19.554	0.269	0.269	0.000	0.000	0.000	0.000
66	A	69	ASN	0	-0.060	-0.061	21.003	0.020	0.020	0.000	0.000	0.000	0.000
67	A	70	ALA	0	0.002	0.012	23.208	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	71	LYS	1	0.978	0.984	18.187	-0.391	-0.391	0.000	0.000	0.000	0.000
69	A	72	LYN	0	-0.109	-0.020	18.258	0.033	0.033	0.000	0.000	0.000	0.000
70	A	73	THR	0	-0.058	-0.034	14.503	-0.016	-0.016	0.000	0.000	0.000	0.000
71	A	74	VAL	0	0.024	0.060	14.382	-0.070	-0.070	0.000	0.000	0.000	0.000
72	A	75	TYR	0	0.016	-0.039	13.955	0.144	0.144	0.000	0.000	0.000	0.000
73	A	76	LEU	0	-0.008	-0.008	12.785	-0.060	-0.060	0.000	0.000	0.000	0.000
74	A	77	GLU	-1	-0.895	-0.957	13.773	0.128	0.128	0.000	0.000	0.000	0.000
75	A	78	MET	0	-0.031	0.000	11.204	-0.042	-0.042	0.000	0.000	0.000	0.000
76	A	79	ASN	0	0.121	0.075	16.174	0.001	0.001	0.000	0.000	0.000	0.000
77	A	80	SER	0	-0.023	-0.015	18.916	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	81	LEU	0	0.010	0.017	13.680	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	82	GLU	-1	-0.874	-0.938	17.877	-0.160	-0.160	0.000	0.000	0.000	0.000
80	A	83	PRO	0	0.007	-0.011	17.322	-0.048	-0.048	0.000	0.000	0.000	0.000
81	A	84	GLU	-1	-0.944	-0.966	17.071	-0.287	-0.287	0.000	0.000	0.000	0.000
82	A	85	ASP	-1	-0.774	-0.858	15.098	-0.260	-0.260	0.000	0.000	0.000	0.000
83	A	86	THR	0	-0.036	0.003	12.363	-0.101	-0.101	0.000	0.000	0.000	0.000
84	A	87	ALA	0	-0.044	-0.034	11.151	0.072	0.072	0.000	0.000	0.000	0.000
85	A	88	VAL	0	0.003	0.012	5.946	-0.228	-0.228	0.000	0.000	0.000	0.000
86	A	89	TYR	0	-0.017	-0.037	7.335	0.395	0.395	0.000	0.000	0.000	0.000
87	A	90	TYR	0	-0.014	-0.016	7.131	0.031	0.031	0.000	0.000	0.000	0.000
88	A	92	TYR	0	0.005	-0.013	11.761	-0.031	-0.031	0.000	0.000	0.000	0.000
89	A	93	THR	0	-0.049	-0.049	14.814	0.019	0.019	0.000	0.000	0.000	0.000
90	A	94	HIS	0	0.020	0.023	18.109	-0.020	-0.020	0.000	0.000	0.000	0.000
91	A	95	TYR	0	-0.042	-0.036	19.859	0.006	0.006	0.000	0.000	0.000	0.000
92	A	96	PHE	0	0.021	0.006	24.422	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	97	ARG	1	0.891	0.944	27.897	-0.060	-0.060	0.000	0.000	0.000	0.000
94	A	98	SER	0	-0.002	0.006	31.340	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	99	TYR	0	0.042	0.013	33.640	0.006	0.006	0.000	0.000	0.000	0.000
96	A	100	TRP	0	0.006	0.006	37.770	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	101	GLY	0	0.020	0.021	41.362	0.002	0.002	0.000	0.000	0.000	0.000
98	A	102	GLN	0	0.012	-0.001	44.548	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	103	GLY	0	0.014	0.013	47.798	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	104	THR	0	-0.044	-0.028	49.647	0.001	0.001	0.000	0.000	0.000	0.000
101	A	105	GLN	0	0.026	0.017	52.846	0.000	0.000	0.000	0.000	0.000	0.000
102	A	106	VAL	0	0.021	0.009	54.447	0.000	0.000	0.000	0.000	0.000	0.000
103	A	107	THR	0	-0.020	-0.019	57.041	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	108	VAL	0	0.016	0.013	59.414	0.000	0.000	0.000	0.000	0.000	0.000
105	A	109	SER	0	-0.011	-0.023	62.181	0.000	0.000	0.000	0.000	0.000	0.000
106	A	110	SER	0	0.003	0.029	65.891	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:GLY)