FMO DATABASE

FMODB ID: 1N4JZ

Calculation Name: 5D1I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5D1I

Chain ID: A

ChEMBL ID:

UniProt ID: Q57AQ0

Base Structure: X-ray

Registration Date: 2023-09-20

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	117
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-907198.335574
FMO2-HF: Nuclear repulsion	862819.414043
FMO2-HF: Total energy	-44378.921532
FMO2-MP2: Total energy	-44510.132714

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:2:ALA)

Summations of interaction energy for fragment #1(A:2: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.
-4.084	2.349	1.489	-3.173	-4.747	-0.002

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.062 / q_NPA : 0.028

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	4	ASP	-1	-0.898	-0.964	2.817	-3.643	-0.716	0.144	-1.372	-1.698	0.003
4	A	5	ASP	-1	-0.846	-0.915	2.316	-4.008	-1.632	1.271	-1.352	-2.295	-0.004
5	A	6	ASP	-1	-0.830	-0.894	3.936	-3.061	-2.533	0.003	-0.157	-0.373	0.000
6	A	7	ILE	0	-0.036	-0.022	5.986	1.002	1.002	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.857	0.929	6.613	1.973	1.973	0.000	0.000	0.000	0.000
8	A	9	ILE	0	-0.020	-0.012	6.327	0.394	0.394	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.002	-0.004	9.708	0.303	0.303	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.027	0.008	11.692	0.166	0.166	0.000	0.000	0.000	0.000
11	A	12	THR	0	-0.101	-0.047	12.929	0.128	0.128	0.000	0.000	0.000	0.000
12	A	13	VAL	0	-0.053	-0.012	14.128	0.081	0.081	0.000	0.000	0.000	0.000
13	A	14	GLY	0	0.069	0.031	16.745	0.011	0.011	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.046	-0.021	19.925	0.018	0.018	0.000	0.000	0.000	0.000
15	A	16	PHE	0	-0.067	-0.052	14.971	0.020	0.020	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.931	-0.942	17.974	-0.338	-0.338	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.031	-0.018	19.368	-0.013	-0.013	0.000	0.000	0.000	0.000
18	A	19	PHE	0	-0.023	-0.007	16.712	0.017	0.017	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.048	0.022	17.834	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	21	PRO	0	0.045	-0.006	13.394	-0.051	-0.051	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.979	-0.982	13.407	-0.417	-0.417	0.000	0.000	0.000	0.000
22	A	23	GLN	0	0.066	0.028	15.319	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.026	0.017	12.240	-0.035	-0.035	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.952	0.986	7.891	0.712	0.712	0.000	0.000	0.000	0.000
25	A	26	LEU	0	0.001	0.001	11.619	-0.050	-0.050	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.019	-0.008	13.356	0.022	0.022	0.000	0.000	0.000	0.000
27	A	28	ALA	0	-0.012	-0.015	8.065	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	29	PHE	0	-0.064	-0.034	9.417	-0.058	-0.058	0.000	0.000	0.000	0.000
29	A	30	GLY	0	-0.049	-0.016	11.219	0.111	0.111	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.048	-0.018	10.121	0.101	0.101	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.829	-0.889	11.531	-0.220	-0.220	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.784	0.866	2.793	1.971	2.573	0.071	-0.292	-0.381	-0.001
33	A	34	LEU	0	-0.039	-0.020	9.842	0.161	0.161	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.052	0.025	10.295	-0.038	-0.038	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.079	-0.045	12.667	0.013	0.013	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.970	0.981	15.803	-0.158	-0.158	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.023	0.011	18.236	-0.026	-0.026	0.000	0.000	0.000	0.000
38	A	39	GLY	0	0.006	-0.002	20.398	0.008	0.008	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.902	0.963	17.514	0.059	0.059	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.833	-0.909	21.166	-0.075	-0.075	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.085	-0.029	16.988	0.003	0.003	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.054	-0.040	20.144	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.907	0.941	24.036	0.065	0.065	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.720	-0.842	27.660	-0.102	-0.102	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.003	-0.006	29.280	0.008	0.008	0.000	0.000	0.000	0.000
46	A	47	GLN	0	-0.025	0.006	25.319	0.006	0.006	0.000	0.000	0.000	0.000
47	A	48	SER	0	0.007	-0.007	28.386	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	49	ALA	0	-0.010	-0.003	24.391	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.863	-0.931	23.115	-0.198	-0.198	0.000	0.000	0.000	0.000
50	A	51	CYS	0	-0.087	-0.029	18.658	-0.013	-0.013	0.000	0.000	0.000	0.000
51	A	52	ALA	0	0.032	0.033	17.609	0.031	0.031	0.000	0.000	0.000	0.000
52	A	53	TYR	0	0.026	-0.003	14.910	-0.026	-0.026	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.032	0.019	11.611	0.051	0.051	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.011	0.011	11.430	-0.072	-0.072	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.008	0.018	5.413	-0.091	-0.091	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.012	-0.008	7.394	0.050	0.050	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.066	0.035	10.153	0.021	0.021	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.074	-0.044	13.854	-0.036	-0.036	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.009	0.022	16.395	0.020	0.020	0.000	0.000	0.000	0.000
60	A	61	THR	0	0.039	0.008	19.345	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.058	-0.026	21.401	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	63	PHE	0	-0.026	-0.020	24.747	0.010	0.010	0.000	0.000	0.000	0.000
63	A	64	HIS	1	0.856	0.897	28.330	0.089	0.089	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.841	-0.917	31.497	-0.052	-0.052	0.000	0.000	0.000	0.000
65	A	66	GLY	0	-0.001	0.002	33.505	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.934	-0.972	36.833	-0.043	-0.043	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.976	-0.986	39.456	-0.024	-0.024	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.013	0.002	35.812	0.004	0.004	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.842	0.912	27.063	0.041	0.041	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.031	0.024	32.432	0.004	0.004	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.017	-0.018	27.550	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	73	ILE	0	-0.067	-0.022	27.454	0.000	0.000	0.000	0.000	0.000	0.000
73	A	74	ARG	1	0.960	0.969	22.684	0.180	0.180	0.000	0.000	0.000	0.000
74	A	75	PRO	0	0.042	0.036	21.343	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	76	VAL	0	-0.055	-0.038	18.464	-0.015	-0.015	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.073	0.024	15.645	0.029	0.029	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.028	-0.025	10.637	-0.030	-0.030	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.010	0.013	11.844	0.033	0.033	0.000	0.000	0.000	0.000
79	A	80	ALA	0	-0.043	0.000	13.109	0.023	0.023	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.045	0.017	15.115	-0.045	-0.045	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.052	-0.021	17.162	0.061	0.061	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.033	-0.008	19.256	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.823	-0.918	20.082	-0.366	-0.366	0.000	0.000	0.000	0.000
84	A	85	MET	0	0.037	0.007	21.247	0.010	0.010	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.024	0.000	22.865	0.014	0.014	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.058	-0.020	18.543	0.015	0.015	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.008	-0.004	23.105	0.004	0.004	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.002	0.010	26.351	0.017	0.017	0.000	0.000	0.000	0.000
89	A	90	GLN	0	-0.018	-0.003	28.076	-0.013	-0.013	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.007	-0.011	27.048	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	THR	0	0.003	-0.002	28.745	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.793	0.901	21.290	0.204	0.204	0.000	0.000	0.000	0.000
93	A	94	LEU	0	0.057	0.025	26.879	0.012	0.012	0.000	0.000	0.000	0.000
94	A	95	THR	0	-0.048	-0.021	25.271	0.003	0.003	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.031	0.019	26.425	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.017	-0.017	21.185	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	98	VAL	0	0.010	0.003	22.117	0.005	0.005	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.006	0.007	17.881	-0.012	-0.012	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.829	-0.895	19.562	-0.041	-0.041	0.000	0.000	0.000	0.000
100	A	101	VAL	0	-0.019	-0.019	16.373	0.026	0.026	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.919	-0.954	13.696	0.216	0.216	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.031	-0.038	13.085	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.878	-0.910	6.645	0.109	0.109	0.000	0.000	0.000	0.000
104	A	105	VAL	0	-0.024	-0.021	10.205	-0.122	-0.122	0.000	0.000	0.000	0.000
105	A	106	ILE	0	0.040	0.018	7.381	0.043	0.043	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.814	0.868	10.520	0.356	0.356	0.000	0.000	0.000	0.000
107	A	108	ILE	0	0.038	0.023	12.470	-0.017	-0.017	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.027	0.005	15.700	0.064	0.064	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.974	0.972	19.016	0.175	0.175	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.073	-0.035	21.339	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	112	ILE	0	0.003	0.001	15.839	0.019	0.019	0.000	0.000	0.000	0.000
112	A	113	PHE	0	0.082	0.027	19.154	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.786	0.848	20.011	0.201	0.201	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.938	0.962	20.701	0.248	0.248	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.027	0.007	16.597	0.009	0.009	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.044	-0.006	21.037	0.008	0.008	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.832	-0.864	24.099	-0.171	-0.171	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)