FMO DATABASE

FMODB ID: 5314Z

Calculation Name: 3V69-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3V69

Chain ID: A

ChEMBL ID:

UniProt ID: Q9CWU5

Base Structure: X-ray

Registration Date: 2023-06-20

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1045355.335222
FMO2-HF: Nuclear repulsion	996493.580104
FMO2-HF: Total energy	-48861.755117
FMO2-MP2: Total energy	-49002.402033

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.
-25.974	-24.5	19.739	-9.635	-11.574	-0.007

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 : 0.019 / q_NPA : 0.020

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	LEU	0	0.014	-0.006	2.683	-1.718	1.445	0.760	-1.922	-2.001	-0.008
4	A	5	LYS	1	0.841	0.931	4.997	0.419	0.463	-0.001	-0.005	-0.037	0.000
5	A	6	ARG	1	0.829	0.904	6.028	0.054	0.054	0.000	0.000	0.000	0.000
6	A	7	PHE	0	0.014	0.005	7.228	0.062	0.062	0.000	0.000	0.000	0.000
7	A	8	GLN	0	-0.043	-0.022	9.252	0.025	0.025	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.009	-0.042	10.503	0.072	0.072	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.070	-0.033	13.374	-0.062	-0.062	0.000	0.000	0.000	0.000
10	A	11	VAL	0	-0.026	-0.016	13.465	-0.051	-0.051	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.000	-0.003	10.570	0.096	0.096	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.039	0.045	7.753	-0.034	-0.034	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.835	-0.912	5.968	-0.754	-0.754	0.000	0.000	0.000	0.000
14	A	15	HIS	1	0.802	0.873	1.961	-22.755	-27.562	13.087	-4.032	-4.247	0.027
15	A	16	LYS	1	0.842	0.927	3.319	-2.250	-1.578	0.028	-0.393	-0.306	-0.003
16	A	17	GLN	0	0.014	-0.010	4.665	-0.632	-0.614	-0.001	-0.005	-0.012	0.000
17	A	18	GLY	0	-0.012	-0.003	6.327	-0.113	-0.113	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.022	0.002	7.323	1.002	1.002	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.025	0.041	8.836	-0.046	-0.046	0.000	0.000	0.000	0.000
20	A	21	PHE	0	-0.023	-0.029	4.868	0.997	0.997	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.856	-0.916	8.648	-0.056	-0.056	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.020	-0.001	9.894	0.068	0.068	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.036	-0.017	8.076	-0.082	-0.082	0.000	0.000	0.000	0.000
24	A	25	GLY	0	-0.012	0.004	12.384	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.903	-0.953	16.110	0.101	0.101	0.000	0.000	0.000	0.000
26	A	27	PRO	0	-0.044	-0.012	15.313	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.934	0.945	18.497	-0.038	-0.038	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.060	0.037	18.242	0.010	0.010	0.000	0.000	0.000	0.000
29	A	30	PRO	0	-0.003	0.006	18.593	-0.023	-0.023	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.938	0.952	21.578	-0.112	-0.112	0.000	0.000	0.000	0.000
31	A	32	TRP	0	-0.006	0.006	17.403	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.009	-0.003	14.736	0.019	0.019	0.000	0.000	0.000	0.000
33	A	34	HIS	0	0.032	0.017	19.733	-0.035	-0.035	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.055	0.034	17.175	0.049	0.049	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.786	-0.906	17.000	0.353	0.353	0.000	0.000	0.000	0.000
36	A	37	CYS	0	-0.170	-0.074	16.667	0.059	0.059	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.041	-0.034	11.712	0.103	0.103	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.951	-0.964	13.132	0.556	0.556	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.847	-0.898	15.105	0.740	0.740	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.011	0.016	10.793	-0.053	-0.053	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.771	0.870	13.157	-0.612	-0.612	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.882	0.941	8.529	-1.746	-1.746	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.016	-0.005	11.543	-0.204	-0.204	0.000	0.000	0.000	0.000
44	A	45	TYR	0	-0.048	-0.055	8.772	0.064	0.064	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.031	0.020	11.251	-0.116	-0.116	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.803	-0.905	11.556	0.294	0.294	0.000	0.000	0.000	0.000
47	A	48	PRO	0	0.031	0.000	9.834	0.025	0.025	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.933	0.974	11.939	-0.086	-0.086	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.057	0.028	14.908	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.048	-0.003	9.137	0.019	0.019	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.767	-0.878	12.965	-0.050	-0.050	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.039	-0.001	15.200	-0.017	-0.017	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.058	-0.026	15.485	0.009	0.009	0.000	0.000	0.000	0.000
54	A	55	PHE	0	-0.013	-0.019	11.747	0.027	0.027	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.057	0.032	16.137	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.885	0.923	15.493	0.107	0.107	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.854	-0.930	12.432	-0.126	-0.126	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.030	-0.001	12.581	0.021	0.021	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.872	-0.927	13.583	0.085	0.085	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.011	0.010	17.036	0.010	0.010	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.047	-0.008	11.720	0.016	0.016	0.000	0.000	0.000	0.000
62	A	63	PRO	0	0.044	0.019	15.484	0.020	0.020	0.000	0.000	0.000	0.000
63	A	64	HIS	0	0.008	0.021	17.887	0.005	0.005	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.015	0.006	17.211	0.004	0.004	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.694	-0.822	13.837	0.459	0.459	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.051	-0.042	18.174	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.049	-0.015	21.613	-0.018	-0.018	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.016	-0.012	18.685	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	70	HIS	1	0.801	0.897	21.043	-0.237	-0.237	0.000	0.000	0.000	0.000
70	A	71	THR	0	0.027	0.013	16.632	0.004	0.004	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.034	-0.002	11.883	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	73	ILE	0	-0.024	-0.020	11.452	0.087	0.087	0.000	0.000	0.000	0.000
73	A	74	HIS	0	0.014	0.015	3.022	-0.913	-0.594	0.018	-0.110	-0.227	0.001
74	A	75	VAL	0	0.005	-0.001	6.780	0.263	0.263	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.031	-0.015	2.289	-0.081	1.222	2.682	-1.447	-2.537	-0.016
76	A	77	VAL	0	0.029	0.007	3.471	-0.248	-0.091	0.002	0.022	-0.181	0.000
77	A	78	TRP	0	0.025	-0.005	2.393	-0.970	-0.365	3.164	-1.743	-2.026	-0.008
78	A	79	GLY	0	0.054	0.035	6.805	0.151	0.151	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.023	-0.003	10.576	0.109	0.109	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.896	-0.942	13.164	-0.210	-0.210	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.827	0.939	5.340	-0.630	-0.630	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.892	0.947	9.966	-0.569	-0.569	0.000	0.000	0.000	0.000
83	A	84	ALA	0	0.021	0.020	7.037	0.094	0.094	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.836	-0.907	5.591	3.591	3.591	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.032	0.024	6.958	0.409	0.409	0.000	0.000	0.000	0.000
86	A	87	TRP	0	-0.034	-0.035	6.576	-0.049	-0.049	0.000	0.000	0.000	0.000
87	A	88	ILE	0	0.019	0.018	9.817	-0.123	-0.123	0.000	0.000	0.000	0.000
88	A	89	PHE	0	0.029	0.001	8.335	-0.018	-0.018	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.086	0.021	14.360	-0.087	-0.087	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.035	0.012	18.172	0.028	0.028	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.018	0.004	20.605	0.013	0.013	0.000	0.000	0.000	0.000
92	A	93	PRO	0	-0.031	-0.021	21.623	0.010	0.010	0.000	0.000	0.000	0.000
93	A	94	PHE	0	0.085	0.040	20.976	0.002	0.002	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.759	0.857	16.122	-0.673	-0.673	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.912	0.972	18.770	-0.331	-0.331	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.842	-0.919	21.403	0.301	0.301	0.000	0.000	0.000	0.000
97	A	98	VAL	0	0.006	0.002	17.140	-0.012	-0.012	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.798	-0.891	17.099	0.613	0.613	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.816	0.899	18.499	-0.314	-0.314	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.030	0.006	21.372	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.003	-0.002	14.843	-0.018	-0.018	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.046	-0.030	18.515	0.000	0.000	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.821	-0.883	19.567	0.238	0.238	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.020	-0.001	18.315	-0.026	-0.026	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.035	0.007	17.297	-0.026	-0.026	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.022	-0.015	19.141	-0.022	-0.022	0.000	0.000	0.000	0.000
107	A	108	TYR	0	0.030	0.008	22.428	-0.027	-0.027	0.000	0.000	0.000	0.000
108	A	109	CYS	0	-0.033	-0.015	19.695	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.860	0.922	18.122	-0.270	-0.270	0.000	0.000	0.000	0.000
110	A	111	MET	0	-0.013	0.000	22.200	-0.017	-0.017	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.831	0.890	24.134	-0.107	-0.107	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.021	-0.008	20.177	-0.012	-0.012	0.000	0.000	0.000	0.000
113	A	114	MET	0	-0.016	-0.013	23.899	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.846	-0.888	26.630	0.079	0.079	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.059	-0.030	25.248	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-1.031	-1.004	25.179	0.022	0.022	0.000	0.000	0.000	0.000

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