FMO DATABASE

FMODB ID: 4315N

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:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1043565.648305
FMO2-HF: Nuclear repulsion	994704.31574
FMO2-HF: Total energy	-48861.332565
FMO2-MP2: Total energy	-49001.972252

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.
-10.455	-4.201	11.548	-7.223	-10.58	-0.019

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 : 0.002 / q_NPA : 0.001

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	-0.008	-0.031	2.872	-2.260	1.643	0.640	-2.333	-2.210	-0.001
4	A	5	LYS	1	0.870	0.975	5.272	0.262	0.333	-0.001	-0.008	-0.061	0.000
5	A	6	ARG	1	0.874	0.920	5.905	0.238	0.238	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.005	-0.007	7.632	0.047	0.047	0.000	0.000	0.000	0.000
7	A	8	GLN	0	-0.015	-0.008	9.863	0.012	0.012	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.005	-0.037	10.703	0.065	0.065	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.079	-0.039	13.688	-0.060	-0.060	0.000	0.000	0.000	0.000
10	A	11	VAL	0	-0.035	-0.024	13.647	-0.047	-0.047	0.000	0.000	0.000	0.000
11	A	12	PRO	0	0.008	0.010	10.336	0.095	0.095	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.042	0.036	7.810	-0.029	-0.029	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.792	-0.891	5.818	-0.850	-0.850	0.000	0.000	0.000	0.000
14	A	15	HIS	1	0.745	0.872	2.140	-9.724	-8.198	2.199	-1.359	-2.365	0.010
15	A	16	LYS	1	0.850	0.932	3.265	0.857	1.715	0.342	-0.498	-0.703	-0.003
16	A	17	GLN	0	0.045	0.001	4.777	-0.630	-0.599	-0.001	-0.004	-0.026	0.000
17	A	18	GLY	0	-0.030	-0.008	6.342	-0.212	-0.212	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.034	0.018	7.859	0.595	0.595	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.020	0.033	9.152	-0.089	-0.089	0.000	0.000	0.000	0.000
20	A	21	PHE	0	-0.016	-0.031	5.069	0.863	0.863	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.879	-0.936	8.868	0.003	0.003	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.018	0.011	10.016	0.020	0.020	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.035	-0.007	8.265	-0.076	-0.076	0.000	0.000	0.000	0.000
24	A	25	GLY	0	-0.028	-0.013	12.430	0.005	0.005	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.905	-0.956	15.943	0.073	0.073	0.000	0.000	0.000	0.000
26	A	27	PRO	0	-0.038	-0.001	15.785	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.940	0.954	18.824	-0.014	-0.014	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.053	0.035	18.676	0.010	0.010	0.000	0.000	0.000	0.000
29	A	30	PRO	0	0.006	0.001	19.004	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.954	0.963	21.981	-0.086	-0.086	0.000	0.000	0.000	0.000
31	A	32	TRP	0	-0.005	0.002	17.673	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.015	-0.003	15.272	0.014	0.014	0.000	0.000	0.000	0.000
33	A	34	HIS	0	0.046	0.024	20.069	-0.028	-0.028	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.062	0.026	17.564	0.042	0.042	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.807	-0.912	17.483	0.302	0.302	0.000	0.000	0.000	0.000
36	A	37	CYS	0	-0.147	-0.052	16.894	0.051	0.051	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.057	-0.035	12.270	0.076	0.076	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.957	-0.964	13.389	0.487	0.487	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.861	-0.909	15.010	0.646	0.646	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.009	0.009	10.697	-0.039	-0.039	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.806	0.892	13.172	-0.515	-0.515	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.888	0.951	8.752	-1.295	-1.295	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.022	-0.007	11.500	-0.137	-0.137	0.000	0.000	0.000	0.000
44	A	45	TYR	0	-0.051	-0.042	9.384	0.036	0.036	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.038	0.023	11.307	-0.099	-0.099	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.826	-0.911	11.479	0.341	0.341	0.000	0.000	0.000	0.000
47	A	48	PRO	0	0.054	0.007	9.894	0.014	0.014	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.962	0.988	11.469	-0.133	-0.133	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.041	0.018	14.499	-0.020	-0.020	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.043	0.007	8.652	0.010	0.010	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.771	-0.885	12.857	-0.020	-0.020	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.031	0.005	15.114	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.058	-0.028	15.233	0.005	0.005	0.000	0.000	0.000	0.000
54	A	55	PHE	0	-0.018	-0.023	11.602	0.011	0.011	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.058	0.033	16.008	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.909	0.941	15.487	0.102	0.102	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.882	-0.945	12.911	-0.115	-0.115	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.029	-0.008	12.945	0.015	0.015	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.919	-0.964	13.873	0.065	0.065	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.006	0.009	17.179	0.005	0.005	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.028	-0.009	12.006	0.019	0.019	0.000	0.000	0.000	0.000
62	A	63	PRO	0	0.036	0.024	15.982	0.019	0.019	0.000	0.000	0.000	0.000
63	A	64	HIS	0	0.019	0.015	18.077	0.008	0.008	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.014	0.010	17.168	0.004	0.004	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.686	-0.819	13.904	0.387	0.387	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.057	-0.040	18.287	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.072	-0.024	21.809	-0.015	-0.015	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.031	-0.024	18.498	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	70	HIS	1	0.813	0.913	20.839	-0.208	-0.208	0.000	0.000	0.000	0.000
70	A	71	THR	0	0.028	0.014	16.331	0.009	0.009	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.040	-0.005	12.467	-0.029	-0.029	0.000	0.000	0.000	0.000
72	A	73	ILE	0	-0.009	-0.019	11.124	0.075	0.075	0.000	0.000	0.000	0.000
73	A	74	HIS	0	0.004	0.008	3.216	-0.667	-0.388	0.009	-0.081	-0.208	0.000
74	A	75	VAL	0	0.010	0.008	6.698	0.218	0.218	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.016	-0.003	2.134	0.712	-0.419	5.785	-1.842	-2.813	-0.019
76	A	77	VAL	0	0.054	0.015	3.340	-0.231	-0.357	0.000	0.352	-0.226	-0.001
77	A	78	TRP	0	-0.008	-0.019	2.220	-0.665	0.178	2.575	-1.450	-1.968	-0.005
78	A	79	GLY	0	0.047	0.037	6.387	-0.053	-0.053	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.021	-0.014	10.192	0.128	0.128	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.936	-0.956	12.889	-0.070	-0.070	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.864	0.957	5.358	-0.860	-0.860	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.923	0.961	10.466	-0.520	-0.520	0.000	0.000	0.000	0.000
83	A	84	ALA	0	0.004	0.009	7.168	0.128	0.128	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.847	-0.929	5.951	2.817	2.817	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.025	0.021	6.862	0.252	0.252	0.000	0.000	0.000	0.000
86	A	87	TRP	0	-0.036	-0.051	6.343	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	88	ILE	0	0.026	0.018	9.449	-0.103	-0.103	0.000	0.000	0.000	0.000
88	A	89	PHE	0	0.019	0.001	8.504	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.090	0.014	14.445	-0.069	-0.069	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.048	0.018	18.187	0.024	0.024	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.041	0.022	20.374	0.008	0.008	0.000	0.000	0.000	0.000
92	A	93	PRO	0	-0.046	-0.035	21.383	0.005	0.005	0.000	0.000	0.000	0.000
93	A	94	PHE	0	0.040	0.031	20.840	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.773	0.857	15.836	-0.584	-0.584	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.915	0.965	18.668	-0.284	-0.284	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.833	-0.912	21.212	0.264	0.264	0.000	0.000	0.000	0.000
97	A	98	VAL	0	0.005	-0.005	17.223	-0.012	-0.012	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.841	-0.910	17.223	0.511	0.511	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.855	0.940	18.604	-0.265	-0.265	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.035	0.016	21.023	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.014	0.006	14.630	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.037	-0.024	18.097	0.004	0.004	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.841	-0.923	19.454	0.212	0.212	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.043	-0.013	17.989	-0.021	-0.021	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.037	0.002	17.121	-0.022	-0.022	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.036	-0.017	18.932	-0.014	-0.014	0.000	0.000	0.000	0.000
107	A	108	TYR	0	0.042	0.016	22.313	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	109	CYS	0	-0.032	-0.016	19.417	-0.018	-0.018	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.872	0.932	17.988	-0.262	-0.262	0.000	0.000	0.000	0.000
110	A	111	MET	0	-0.006	0.003	21.672	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.875	0.923	23.951	-0.101	-0.101	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.034	-0.015	19.476	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	114	MET	0	-0.020	-0.019	23.303	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.857	-0.896	25.908	0.081	0.081	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.077	-0.044	25.018	-0.008	-0.008	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-1.041	-0.999	25.094	0.043	0.043	0.000	0.000	0.000	0.000

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