FMO DATABASE

FMODB ID: 85M2Y

Calculation Name: 4M6A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4M6A

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-09-19

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	89
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-525413.55717
FMO2-HF: Nuclear repulsion	492158.525092
FMO2-HF: Total energy	-33255.032078
FMO2-MP2: Total energy	-33354.244153

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:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-1.276	-0.096	-0.007	-0.487	-0.686	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.014 / q_NPA : -0.010

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	ALA	0	0.042	0.019	3.890	-1.295	-0.115	-0.007	-0.487	-0.686	0.002
4	A	5	PRO	0	0.016	0.000	5.807	0.463	0.463	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.936	0.962	8.525	0.101	0.101	0.000	0.000	0.000	0.000
6	A	7	ASN	0	-0.031	-0.026	11.883	0.001	0.001	0.000	0.000	0.000	0.000
7	A	8	LEU	0	0.036	0.036	14.279	0.014	0.014	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.010	-0.005	15.953	0.023	0.023	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.001	-0.003	19.672	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.043	-0.023	22.247	0.010	0.010	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.897	-0.941	25.894	-0.110	-0.110	0.000	0.000	0.000	0.000
12	A	13	VAL	0	-0.028	-0.014	26.373	0.003	0.003	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.038	-0.028	29.268	0.002	0.002	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.838	-0.915	26.939	-0.115	-0.115	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.916	-0.961	31.758	-0.074	-0.074	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.045	-0.011	30.403	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.011	0.008	30.297	0.007	0.007	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.795	0.857	30.478	0.093	0.093	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.016	0.024	27.652	0.005	0.005	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.035	-0.058	31.726	0.000	0.000	0.000	0.000	0.000	0.000
21	A	22	TRP	0	-0.049	0.004	28.392	0.003	0.003	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.005	-0.009	34.480	0.000	0.000	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.016	0.001	33.589	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	25	PRO	0	-0.004	-0.001	35.645	0.002	0.002	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.806	-0.885	35.292	-0.095	-0.095	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.037	-0.025	33.219	0.002	0.002	0.000	0.000	0.000	0.000
27	A	28	ALA	0	-0.030	-0.012	33.069	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	29	PHE	0	-0.026	-0.010	28.710	0.000	0.000	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.790	-0.889	25.869	-0.141	-0.141	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.042	-0.026	23.553	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	32	PHE	0	0.014	0.008	25.230	0.012	0.012	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.028	-0.007	19.683	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.001	0.004	22.635	0.016	0.016	0.000	0.000	0.000	0.000
34	A	35	GLN	0	0.043	0.018	21.365	-0.025	-0.025	0.000	0.000	0.000	0.000
35	A	36	TYR	0	0.016	0.003	22.129	0.010	0.010	0.000	0.000	0.000	0.000
36	A	37	GLN	0	0.005	0.005	21.908	-0.017	-0.017	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.754	-0.841	23.968	-0.075	-0.075	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.027	-0.073	26.228	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.965	-0.984	27.818	-0.062	-0.062	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.829	0.903	22.507	0.090	0.090	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.041	-0.012	22.107	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	GLY	0	-0.021	-0.017	19.185	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.891	-0.928	17.490	-0.118	-0.118	0.000	0.000	0.000	0.000
44	A	45	ALA	0	-0.031	-0.008	18.968	0.001	0.001	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.001	0.008	17.556	-0.027	-0.027	0.000	0.000	0.000	0.000
46	A	47	ASN	0	-0.043	-0.032	16.786	0.025	0.025	0.000	0.000	0.000	0.000
47	A	48	LEU	0	0.027	0.025	17.045	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.058	-0.053	19.230	0.010	0.010	0.000	0.000	0.000	0.000
49	A	50	VAL	0	0.018	0.033	21.000	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	51	PRO	0	0.053	0.018	23.995	0.001	0.001	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.013	0.009	26.021	0.007	0.007	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.040	-0.043	29.012	0.008	0.008	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.875	-0.910	27.773	-0.128	-0.128	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.808	0.870	30.583	0.110	0.110	0.000	0.000	0.000	0.000
55	A	56	SER	0	0.012	0.003	31.481	0.008	0.008	0.000	0.000	0.000	0.000
56	A	57	TYR	0	-0.022	-0.014	22.853	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.742	-0.826	27.703	-0.105	-0.105	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.043	-0.028	25.109	-0.012	-0.012	0.000	0.000	0.000	0.000
59	A	60	THR	0	0.017	0.012	25.365	0.007	0.007	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.022	-0.019	23.857	-0.010	-0.010	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.067	-0.023	24.930	0.000	0.000	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.827	0.885	25.656	0.085	0.085	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.051	0.043	28.972	0.003	0.003	0.000	0.000	0.000	0.000
64	A	65	GLY	0	-0.029	-0.007	32.828	0.003	0.003	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.074	-0.045	30.132	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.865	-0.907	31.258	-0.064	-0.064	0.000	0.000	0.000	0.000
67	A	68	TYR	0	0.024	0.020	24.820	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.019	0.018	27.498	0.004	0.004	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.012	-0.023	26.897	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.019	-0.014	26.324	0.010	0.010	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.007	0.020	25.887	-0.012	-0.012	0.000	0.000	0.000	0.000
72	A	73	TYR	0	0.008	0.010	25.021	0.008	0.008	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.056	0.037	26.408	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.007	-0.011	22.913	0.002	0.002	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.851	0.924	26.282	0.123	0.123	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.003	-0.009	24.440	0.004	0.004	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.007	-0.007	22.232	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	79	HIS	0	-0.095	-0.042	22.931	0.002	0.002	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.866	0.942	20.912	0.165	0.165	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.018	-0.018	26.085	0.005	0.005	0.000	0.000	0.000	0.000
81	A	82	ASN	0	-0.004	-0.017	28.719	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	83	PRO	0	-0.002	0.023	28.409	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.018	0.005	30.112	0.007	0.007	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.029	-0.039	29.857	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.020	-0.004	31.249	0.005	0.005	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.818	-0.898	31.334	-0.090	-0.090	0.000	0.000	0.000	0.000
87	A	88	PHE	0	-0.071	-0.027	29.236	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	THR	0	0.039	0.016	32.887	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.035	-0.029	30.562	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:2:LEU)