FMO DATABASE

FMODB ID: VQR51

Calculation Name: 5MR1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5MR1

Chain ID: A

ChEMBL ID:

UniProt ID: Q8WWN9

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	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	101
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-816120.722985
FMO2-HF: Nuclear repulsion	774800.684651
FMO2-HF: Total energy	-41320.038334
FMO2-MP2: Total energy	-41440.859235

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:42:ALA)

Summations of interaction energy for fragment #1(A:42: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.
-29.198	-27.605	14.196	-7.155	-8.637	0.02

Interaction energy analysis for fragmet #1(A:42:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.015 / q_NPA : 0.005

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	44	CYS	0	-0.042	-0.022	3.413	-0.272	1.231	-0.004	-0.727	-0.773	0.002
4	A	45	GLN	0	0.025	0.012	2.713	-2.413	-0.509	0.527	-0.858	-1.573	-0.007
5	A	46	GLY	0	0.021	0.014	4.388	0.194	0.204	-0.001	-0.012	0.002	0.000
6	A	47	TRP	0	0.009	0.010	8.017	0.046	0.046	0.000	0.000	0.000	0.000
7	A	48	LEU	0	-0.007	0.005	10.641	0.027	0.027	0.000	0.000	0.000	0.000
8	A	49	TYR	0	-0.062	-0.068	13.208	0.035	0.035	0.000	0.000	0.000	0.000
9	A	50	LYS	1	0.958	0.977	15.862	0.145	0.145	0.000	0.000	0.000	0.000
10	A	51	LYS	1	0.816	0.929	17.698	0.117	0.117	0.000	0.000	0.000	0.000
11	A	52	LYS	1	0.956	0.971	21.066	0.122	0.122	0.000	0.000	0.000	0.000
12	A	53	GLU	-1	-0.781	-0.874	23.093	-0.055	-0.055	0.000	0.000	0.000	0.000
13	A	54	LYS	1	1.008	1.004	24.769	0.041	0.041	0.000	0.000	0.000	0.000
14	A	55	GLY	0	-0.022	-0.005	27.295	0.002	0.002	0.000	0.000	0.000	0.000
15	A	56	SER	0	0.045	0.019	27.614	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	57	PHE	0	0.070	0.019	25.553	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	58	LEU	0	0.052	0.033	27.814	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	59	SER	0	-0.027	-0.007	27.551	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	60	ASN	0	0.055	0.011	25.503	0.002	0.002	0.000	0.000	0.000	0.000
20	A	61	LYS	1	0.950	0.978	24.594	0.094	0.094	0.000	0.000	0.000	0.000
21	A	62	TRP	0	-0.028	-0.031	19.437	0.008	0.008	0.000	0.000	0.000	0.000
22	A	63	LYS	1	0.851	0.931	17.155	0.218	0.218	0.000	0.000	0.000	0.000
23	A	64	LYS	1	0.856	0.922	15.251	0.323	0.323	0.000	0.000	0.000	0.000
24	A	65	PHE	0	0.001	-0.007	12.633	0.042	0.042	0.000	0.000	0.000	0.000
25	A	66	TRP	0	0.051	0.044	5.845	0.092	0.092	0.000	0.000	0.000	0.000
26	A	67	VAL	0	-0.003	-0.019	8.084	0.108	0.108	0.000	0.000	0.000	0.000
27	A	68	ILE	0	0.036	0.009	2.456	-0.780	-0.525	0.967	-0.308	-0.914	-0.001
28	A	69	LEU	0	-0.004	0.000	3.759	0.383	0.577	0.000	-0.046	-0.147	0.000
29	A	70	LYS	1	0.829	0.882	2.014	-27.248	-29.588	12.706	-5.168	-5.199	0.026
30	A	71	GLY	0	0.060	0.039	4.177	-0.451	-0.384	0.001	-0.036	-0.033	0.000
31	A	72	SER	0	0.021	0.018	7.555	-0.288	-0.288	0.000	0.000	0.000	0.000
32	A	73	SER	0	-0.020	-0.010	8.231	-0.127	-0.127	0.000	0.000	0.000	0.000
33	A	74	LEU	0	-0.028	0.003	7.089	0.008	0.008	0.000	0.000	0.000	0.000
34	A	75	TYR	0	0.042	0.018	6.609	0.039	0.039	0.000	0.000	0.000	0.000
35	A	76	TRP	0	-0.015	-0.003	8.540	-0.182	-0.182	0.000	0.000	0.000	0.000
36	A	77	TYR	0	0.051	0.028	7.428	0.049	0.049	0.000	0.000	0.000	0.000
37	A	78	SER	0	-0.018	-0.049	12.124	-0.029	-0.029	0.000	0.000	0.000	0.000
38	A	79	ASN	0	-0.029	-0.018	13.441	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	80	GLN	0	0.011	-0.012	9.763	0.079	0.079	0.000	0.000	0.000	0.000
40	A	81	MET	0	0.000	0.019	10.362	-0.052	-0.052	0.000	0.000	0.000	0.000
41	A	82	ALA	0	-0.039	0.002	12.470	0.056	0.056	0.000	0.000	0.000	0.000
42	A	83	GLU	-1	-0.785	-0.881	11.395	-0.135	-0.135	0.000	0.000	0.000	0.000
43	A	84	LYS	1	0.816	0.895	12.465	0.099	0.099	0.000	0.000	0.000	0.000
44	A	85	ALA	0	-0.020	-0.008	10.911	-0.043	-0.043	0.000	0.000	0.000	0.000
45	A	86	ASP	-1	-0.796	-0.880	12.660	-0.191	-0.191	0.000	0.000	0.000	0.000
46	A	87	GLY	0	-0.030	-0.021	13.983	0.032	0.032	0.000	0.000	0.000	0.000
47	A	88	PHE	0	-0.015	-0.010	11.442	-0.053	-0.053	0.000	0.000	0.000	0.000
48	A	89	VAL	0	-0.030	-0.007	12.051	0.000	0.000	0.000	0.000	0.000	0.000
49	A	90	ASN	0	-0.005	-0.013	11.863	-0.028	-0.028	0.000	0.000	0.000	0.000
50	A	91	LEU	0	0.017	-0.010	10.165	-0.046	-0.046	0.000	0.000	0.000	0.000
51	A	92	PRO	0	0.000	0.005	13.849	-0.026	-0.026	0.000	0.000	0.000	0.000
52	A	93	ASP	-1	-0.853	-0.898	16.551	0.124	0.124	0.000	0.000	0.000	0.000
53	A	94	PHE	0	-0.043	-0.017	16.517	-0.030	-0.030	0.000	0.000	0.000	0.000
54	A	95	THR	0	-0.029	-0.031	18.621	0.002	0.002	0.000	0.000	0.000	0.000
55	A	96	VAL	0	0.011	-0.019	15.539	-0.017	-0.017	0.000	0.000	0.000	0.000
56	A	97	GLU	-1	-0.784	-0.843	18.463	-0.048	-0.048	0.000	0.000	0.000	0.000
57	A	98	ARG	1	0.900	0.940	19.926	0.121	0.121	0.000	0.000	0.000	0.000
58	A	99	ALA	0	0.018	0.004	21.363	0.014	0.014	0.000	0.000	0.000	0.000
59	A	100	SER	0	-0.022	-0.042	23.121	-0.013	-0.013	0.000	0.000	0.000	0.000
60	A	101	GLU	-1	-0.754	-0.851	25.775	-0.089	-0.089	0.000	0.000	0.000	0.000
61	A	102	CYS	0	-0.134	-0.044	23.904	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	103	LYS	1	0.968	0.993	25.918	0.097	0.097	0.000	0.000	0.000	0.000
63	A	104	LYS	1	0.796	0.927	19.741	0.233	0.233	0.000	0.000	0.000	0.000
64	A	105	LYS	1	0.969	0.962	22.844	0.200	0.200	0.000	0.000	0.000	0.000
65	A	106	HIS	0	0.024	0.015	18.765	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	107	ALA	0	0.027	0.022	18.333	-0.029	-0.029	0.000	0.000	0.000	0.000
67	A	108	PHE	0	0.009	0.000	12.854	0.015	0.015	0.000	0.000	0.000	0.000
68	A	109	LYS	1	0.825	0.903	18.547	0.050	0.050	0.000	0.000	0.000	0.000
69	A	110	ILE	0	0.025	0.020	14.356	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	111	SER	0	-0.047	-0.037	18.480	0.000	0.000	0.000	0.000	0.000	0.000
71	A	112	HIS	0	0.133	0.068	19.768	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	113	PRO	0	0.012	0.009	21.985	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	114	GLN	0	-0.023	-0.008	24.246	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	115	ILE	0	-0.024	0.006	19.094	0.003	0.003	0.000	0.000	0.000	0.000
75	A	116	LYS	1	0.833	0.897	20.368	0.027	0.027	0.000	0.000	0.000	0.000
76	A	117	THR	0	0.029	0.035	21.358	0.008	0.008	0.000	0.000	0.000	0.000
77	A	118	PHE	0	-0.049	-0.021	17.414	-0.015	-0.015	0.000	0.000	0.000	0.000
78	A	119	TYR	0	-0.022	-0.051	19.187	0.001	0.001	0.000	0.000	0.000	0.000
79	A	120	PHE	0	0.017	0.005	13.646	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	121	ALA	0	-0.016	-0.011	16.183	0.027	0.027	0.000	0.000	0.000	0.000
81	A	122	ALA	0	0.027	0.043	14.803	-0.032	-0.032	0.000	0.000	0.000	0.000
82	A	123	GLU	-1	-0.807	-0.874	15.888	-0.256	-0.256	0.000	0.000	0.000	0.000
83	A	124	ASN	0	-0.064	-0.048	16.238	0.035	0.035	0.000	0.000	0.000	0.000
84	A	125	VAL	0	0.035	-0.001	17.561	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	126	GLN	0	0.071	0.039	16.595	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	127	GLU	-1	-0.776	-0.894	12.550	-0.493	-0.493	0.000	0.000	0.000	0.000
87	A	128	MET	0	-0.048	-0.009	13.084	-0.027	-0.027	0.000	0.000	0.000	0.000
88	A	129	ASN	0	0.016	0.001	15.045	0.013	0.013	0.000	0.000	0.000	0.000
89	A	130	VAL	0	0.017	0.019	9.788	0.023	0.023	0.000	0.000	0.000	0.000
90	A	131	TRP	0	0.035	-0.002	6.318	-0.055	-0.055	0.000	0.000	0.000	0.000
91	A	132	LEU	0	-0.003	-0.003	11.501	0.047	0.047	0.000	0.000	0.000	0.000
92	A	133	ASN	0	-0.020	-0.004	12.712	0.009	0.009	0.000	0.000	0.000	0.000
93	A	134	LYS	1	0.902	0.950	7.255	0.839	0.839	0.000	0.000	0.000	0.000
94	A	135	LEU	0	0.006	-0.008	10.607	0.110	0.110	0.000	0.000	0.000	0.000
95	A	136	GLY	0	0.009	0.002	12.129	0.070	0.070	0.000	0.000	0.000	0.000
96	A	137	SER	0	-0.029	-0.017	11.631	0.048	0.048	0.000	0.000	0.000	0.000
97	A	138	ALA	0	-0.030	-0.014	9.494	0.071	0.071	0.000	0.000	0.000	0.000
98	A	139	VAL	0	-0.011	-0.001	11.452	0.060	0.060	0.000	0.000	0.000	0.000
99	A	140	ILE	0	-0.011	0.002	14.875	0.009	0.009	0.000	0.000	0.000	0.000
100	A	141	HIS	1	0.802	0.868	15.180	-0.143	-0.143	0.000	0.000	0.000	0.000
101	A	142	GLN	0	0.045	0.039	17.524	-0.054	-0.054	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:42:ALA)