FMO DATABASE

FMODB ID: LNRQ9

Calculation Name: 4IT7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4IT7

Chain ID: A

ChEMBL ID:

UniProt ID: E9N3T6

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-742141.046532
FMO2-HF: Nuclear repulsion	701479.664597
FMO2-HF: Total energy	-40661.381935
FMO2-MP2: Total energy	-40778.74364

3D Structure Molmil

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:6:GLY)

Summations of interaction energy for fragment #1(A:6: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.
-0.018999999999999	2.112	1.632	-1.674	-2.09	0

Interaction energy analysis for fragmet #1(A:6:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : 0.000

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	8	PHE	0	-0.071	-0.040	3.810	1.655	3.099	-0.019	-0.861	-0.564	0.002
4	A	9	SER	0	0.033	0.019	7.212	-0.017	-0.017	0.000	0.000	0.000	0.000
5	A	10	THR	0	-0.035	-0.024	9.540	-0.045	-0.045	0.000	0.000	0.000	0.000
6	A	11	LYS	1	0.894	0.960	13.311	-0.386	-0.386	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.780	-0.906	15.138	0.140	0.140	0.000	0.000	0.000	0.000
8	A	13	VAL	0	-0.018	-0.006	18.908	0.007	0.007	0.000	0.000	0.000	0.000
9	A	14	ASN	0	-0.048	-0.026	20.941	-0.029	-0.029	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.821	-0.896	18.128	0.291	0.291	0.000	0.000	0.000	0.000
11	A	16	PRO	0	0.037	0.009	21.353	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	17	LYS	1	0.826	0.903	16.393	-0.258	-0.258	0.000	0.000	0.000	0.000
13	A	18	ILE	0	-0.022	-0.010	15.568	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	19	GLN	0	0.006	-0.009	19.493	-0.030	-0.030	0.000	0.000	0.000	0.000
15	A	20	ALA	0	-0.008	0.004	22.313	-0.015	-0.015	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.026	-0.019	16.520	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	22	ALA	0	0.030	0.014	20.743	-0.019	-0.019	0.000	0.000	0.000	0.000
18	A	23	GLY	0	0.031	0.027	22.409	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.788	0.872	20.802	-0.113	-0.113	0.000	0.000	0.000	0.000
20	A	25	ALA	0	0.039	0.010	20.956	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	26	LEU	0	0.008	0.007	22.992	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	27	GLN	0	-0.006	-0.006	26.514	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	28	ARG	1	0.892	0.948	23.368	-0.036	-0.036	0.000	0.000	0.000	0.000
24	A	29	ILE	0	-0.012	-0.004	24.071	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	30	ASN	0	-0.016	-0.024	27.188	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	31	ALA	0	-0.038	-0.018	29.152	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	32	ALA	0	0.014	0.011	27.888	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	33	SER	0	-0.040	-0.001	29.874	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	34	ASN	0	0.026	-0.012	31.478	0.003	0.003	0.000	0.000	0.000	0.000
30	A	35	ASP	-1	-0.861	-0.909	34.293	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	36	LEU	0	0.053	0.020	36.147	0.001	0.001	0.000	0.000	0.000	0.000
32	A	37	PHE	0	-0.036	-0.005	37.993	0.002	0.002	0.000	0.000	0.000	0.000
33	A	38	GLN	0	0.006	0.002	34.458	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	39	GLN	0	-0.046	-0.021	30.909	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	40	THR	0	0.031	0.016	31.422	0.005	0.005	0.000	0.000	0.000	0.000
36	A	41	ILE	0	0.010	0.005	25.479	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	42	VAL	0	-0.028	-0.013	29.038	0.001	0.001	0.000	0.000	0.000	0.000
38	A	43	LYS	1	0.961	0.961	26.435	-0.047	-0.047	0.000	0.000	0.000	0.000
39	A	44	VAL	0	0.023	0.016	20.763	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	45	ILE	0	-0.044	-0.011	21.721	0.008	0.008	0.000	0.000	0.000	0.000
41	A	46	SER	0	-0.060	-0.061	17.783	0.016	0.016	0.000	0.000	0.000	0.000
42	A	47	ALA	0	0.063	0.015	16.029	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	48	LYS	1	0.926	0.983	11.291	0.093	0.093	0.000	0.000	0.000	0.000
44	A	49	THR	0	0.026	0.012	9.583	-0.169	-0.169	0.000	0.000	0.000	0.000
45	A	50	GLN	0	0.004	0.014	4.294	0.080	0.201	-0.001	-0.026	-0.094	0.000
46	A	51	VAL	0	0.019	-0.005	4.403	-0.879	-0.770	-0.001	-0.020	-0.088	0.000
47	A	52	VAL	0	-0.001	0.011	2.006	-0.547	-0.263	1.646	-0.698	-1.233	-0.002
48	A	53	ALA	0	0.026	0.014	3.798	-0.223	-0.050	0.007	-0.069	-0.111	0.000
49	A	54	GLY	0	0.074	0.048	7.550	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	55	THR	0	-0.038	-0.017	7.971	0.190	0.190	0.000	0.000	0.000	0.000
51	A	56	ASN	0	-0.030	-0.019	8.088	-0.125	-0.125	0.000	0.000	0.000	0.000
52	A	57	THR	0	0.037	0.007	9.477	0.174	0.174	0.000	0.000	0.000	0.000
53	A	58	VAL	0	-0.055	-0.023	11.433	-0.081	-0.081	0.000	0.000	0.000	0.000
54	A	59	LEU	0	0.005	-0.006	13.861	0.040	0.040	0.000	0.000	0.000	0.000
55	A	60	GLU	-1	-0.899	-0.906	17.368	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	61	LEU	0	-0.009	-0.010	20.158	0.016	0.016	0.000	0.000	0.000	0.000
57	A	62	LEU	0	0.004	0.010	23.459	-0.012	-0.012	0.000	0.000	0.000	0.000
58	A	63	ILE	0	0.006	-0.010	26.651	0.007	0.007	0.000	0.000	0.000	0.000
59	A	64	ALA	0	0.002	-0.010	29.316	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	65	PRO	0	0.041	0.047	33.125	0.002	0.002	0.000	0.000	0.000	0.000
61	A	66	THR	0	0.018	-0.008	35.412	0.003	0.003	0.000	0.000	0.000	0.000
62	A	67	SER	0	0.030	0.005	38.055	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	68	CYS	0	-0.097	-0.043	36.296	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	69	ARG	1	0.860	0.920	39.123	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	70	LYS	1	0.862	0.915	33.488	0.006	0.006	0.000	0.000	0.000	0.000
66	A	71	ASN	0	-0.087	-0.031	38.848	0.000	0.000	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.825	-0.907	41.330	0.008	0.008	0.000	0.000	0.000	0.000
68	A	73	THR	0	-0.037	-0.025	41.379	0.001	0.001	0.000	0.000	0.000	0.000
69	A	74	SER	0	0.020	0.021	39.875	0.000	0.000	0.000	0.000	0.000	0.000
70	A	75	ALA	0	0.014	-0.006	42.034	0.001	0.001	0.000	0.000	0.000	0.000
71	A	76	GLY	0	-0.015	-0.008	41.074	0.001	0.001	0.000	0.000	0.000	0.000
72	A	77	ASN	0	-0.029	0.007	36.623	0.001	0.001	0.000	0.000	0.000	0.000
73	A	79	GLU	-1	-0.846	-0.929	36.381	0.034	0.034	0.000	0.000	0.000	0.000
74	A	80	ALA	0	-0.004	-0.003	35.034	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	81	VAL	0	0.000	0.008	37.021	0.000	0.000	0.000	0.000	0.000	0.000
76	A	82	SER	0	-0.009	-0.020	38.936	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	83	ASN	0	-0.080	0.024	39.634	0.000	0.000	0.000	0.000	0.000	0.000
78	A	84	GLY	0	0.091	0.018	37.326	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	85	THR	0	-0.001	-0.032	34.471	0.002	0.002	0.000	0.000	0.000	0.000
80	A	86	LYS	1	0.897	0.946	31.366	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	87	GLN	0	0.004	0.004	28.567	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	88	ILE	0	0.010	0.008	23.289	0.008	0.008	0.000	0.000	0.000	0.000
83	A	89	CYS	0	-0.058	-0.005	22.768	0.000	0.000	0.000	0.000	0.000	0.000
84	A	90	THR	0	0.038	0.023	17.202	0.009	0.009	0.000	0.000	0.000	0.000
85	A	91	VAL	0	-0.020	-0.015	18.450	-0.014	-0.014	0.000	0.000	0.000	0.000
86	A	92	ALA	0	-0.017	-0.001	13.665	0.016	0.016	0.000	0.000	0.000	0.000
87	A	93	ILE	0	-0.007	-0.002	14.446	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	94	TRP	0	-0.043	-0.021	10.160	0.027	0.027	0.000	0.000	0.000	0.000
89	A	95	GLU	-1	-0.803	-0.895	12.695	0.235	0.235	0.000	0.000	0.000	0.000
90	A	96	LYS	1	0.840	0.907	12.484	0.092	0.092	0.000	0.000	0.000	0.000
91	A	97	PRO	0	0.011	-0.001	14.411	-0.025	-0.025	0.000	0.000	0.000	0.000
92	A	98	TRP	0	-0.006	-0.009	11.189	0.016	0.016	0.000	0.000	0.000	0.000
93	A	99	GLU	-1	-0.842	-0.899	16.209	-0.050	-0.050	0.000	0.000	0.000	0.000
94	A	100	ASN	0	-0.081	-0.041	19.368	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	101	PHE	0	0.011	0.028	15.313	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	102	GLU	-1	-0.793	-0.892	17.243	0.128	0.128	0.000	0.000	0.000	0.000
97	A	103	GLU	-1	-0.904	-0.943	16.578	-0.084	-0.084	0.000	0.000	0.000	0.000
98	A	104	ILE	0	-0.027	-0.026	16.908	0.007	0.007	0.000	0.000	0.000	0.000
99	A	105	THR	0	0.033	0.010	17.096	-0.016	-0.016	0.000	0.000	0.000	0.000
100	A	106	ILE	0	-0.028	-0.020	18.750	0.006	0.006	0.000	0.000	0.000	0.000
101	A	107	LYS	1	0.919	0.957	16.087	0.148	0.148	0.000	0.000	0.000	0.000
102	A	108	GLU	-1	-0.829	-0.909	19.869	-0.100	-0.100	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.906	0.954	22.314	0.057	0.057	0.000	0.000	0.000	0.000
104	A	111	SER	0	0.012	-0.007	27.851	0.006	0.006	0.000	0.000	0.000	0.000
105	A	112	ALA	0	-0.004	0.009	28.587	-0.003	-0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:GLY)