FMO DATABASE

FMODB ID: G53V1

Calculation Name: 1DIV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1DIV

Chain ID: A

ChEMBL ID:

UniProt ID: P02417

Base Structure: X-ray

Registration Date: 2023-09-24

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	OptH
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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1124678.22947
FMO2-HF: Nuclear repulsion	1068799.295498
FMO2-HF: Total energy	-55878.933972
FMO2-MP2: Total energy	-56046.463704

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:1:MET)

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

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.
-11.345	-21.059	46.441	-17.75	-18.977	-0.07

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.060 / q_NPA : 0.032

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	3	VAL	0	0.011	0.000	2.565	-3.838	0.438	1.127	-2.546	-2.857	-0.003
4	A	4	ILE	0	0.009	0.005	4.527	-0.230	-0.145	-0.001	-0.021	-0.064	0.000
5	A	5	PHE	0	0.016	-0.007	8.187	0.273	0.273	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.008	-0.007	10.324	-0.026	-0.026	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.849	0.894	13.066	-0.080	-0.080	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.892	-0.945	14.394	-0.167	-0.167	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.051	0.054	13.551	-0.053	-0.053	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.934	0.988	16.108	0.338	0.338	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.057	0.029	19.593	0.009	0.009	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.926	0.961	17.905	0.053	0.053	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.023	-0.008	15.166	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	14	LYS	1	1.000	0.988	14.597	0.089	0.089	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.947	0.978	15.622	0.255	0.255	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.006	-0.020	13.226	0.016	0.016	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-1.001	-0.999	12.183	-0.751	-0.751	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.044	0.033	7.604	-0.046	-0.046	0.000	0.000	0.000	0.000
19	A	19	LYS	1	1.013	1.009	7.122	1.428	1.428	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.042	-0.025	1.699	-0.732	-13.125	21.992	-6.478	-3.121	-0.022
21	A	21	VAL	0	-0.078	-0.020	3.142	0.052	2.047	0.047	-0.842	-1.200	0.001
22	A	22	ALA	0	0.064	0.038	1.770	-7.827	-14.537	15.661	-5.530	-3.420	-0.045
23	A	23	ASP	-1	-0.826	-0.928	2.017	4.917	6.983	4.422	-2.417	-4.071	-0.006
24	A	24	GLY	0	0.036	0.003	3.179	-0.496	-1.594	0.129	1.322	-0.353	0.000
25	A	25	TYR	0	0.012	-0.010	6.435	-0.099	-0.034	-0.001	-0.003	-0.060	0.000
26	A	26	ALA	0	0.037	0.030	3.360	-0.627	-0.140	0.554	-0.288	-0.753	0.002
27	A	27	ASN	0	0.016	-0.002	3.712	-0.603	0.287	0.034	-0.264	-0.660	-0.001
28	A	28	ASN	0	0.003	-0.012	5.605	-0.668	-0.668	0.000	0.000	0.000	0.000
29	A	29	PHE	0	0.006	0.016	8.799	-0.203	-0.203	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.014	0.014	7.096	-0.094	-0.094	0.000	0.000	0.000	0.000
31	A	31	PHE	0	-0.027	0.000	2.902	-1.290	-1.291	2.462	-0.591	-1.870	0.004
32	A	32	LYS	1	0.877	0.954	8.263	-0.749	-0.749	0.000	0.000	0.000	0.000
33	A	33	GLN	0	0.027	0.014	11.377	-0.048	-0.048	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.016	-0.021	12.215	-0.075	-0.075	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.025	-0.012	11.429	-0.060	-0.060	0.000	0.000	0.000	0.000
36	A	36	ALA	0	-0.035	-0.005	7.283	-0.206	-0.206	0.000	0.000	0.000	0.000
37	A	37	ILE	0	0.040	0.025	7.524	0.178	0.178	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.807	-0.925	3.464	0.069	0.566	0.016	-0.082	-0.432	0.000
39	A	39	ALA	0	-0.050	0.000	4.296	-0.461	-0.334	-0.001	-0.010	-0.116	0.000
40	A	40	THR	0	0.030	0.005	6.160	-0.088	-0.088	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.033	-0.003	7.890	0.034	0.034	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.016	0.018	11.022	0.039	0.039	0.000	0.000	0.000	0.000
43	A	43	ASN	0	0.023	0.000	9.549	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.007	0.003	8.635	-0.019	-0.019	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.987	0.990	11.967	0.235	0.235	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.013	0.004	14.848	0.015	0.015	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.022	0.029	12.438	0.019	0.019	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.893	-0.966	15.279	-0.296	-0.296	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.032	0.021	17.445	0.018	0.018	0.000	0.000	0.000	0.000
50	A	50	GLN	0	-0.045	-0.026	17.183	0.034	0.034	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.911	0.962	15.527	0.327	0.327	0.000	0.000	0.000	0.000
52	A	52	GLN	0	-0.002	-0.010	20.312	0.000	0.000	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.901	0.977	22.760	0.102	0.102	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.992	-1.000	20.864	-0.129	-0.129	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.013	-0.010	24.417	0.009	0.009	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.941	0.986	26.142	0.082	0.082	0.000	0.000	0.000	0.000
57	A	57	GLN	0	0.031	-0.005	26.947	0.000	0.000	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.036	0.031	28.362	0.005	0.005	0.000	0.000	0.000	0.000
59	A	59	ALA	0	-0.012	-0.009	30.233	0.003	0.003	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.943	-0.962	32.477	-0.060	-0.060	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.904	-0.961	32.034	-0.066	-0.066	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.019	0.000	34.546	0.005	0.005	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.052	0.015	36.329	0.004	0.004	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.042	-0.043	37.571	0.003	0.003	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.007	0.000	39.098	0.003	0.003	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.928	0.951	38.960	0.062	0.062	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.999	1.043	41.744	0.046	0.046	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.087	-0.045	43.298	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.911	0.939	44.906	0.044	0.044	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.906	-0.953	46.584	-0.039	-0.039	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.051	-0.032	47.176	0.001	0.001	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.025	-0.017	47.365	0.002	0.002	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.832	-0.906	49.707	-0.036	-0.036	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.929	0.988	52.322	0.031	0.031	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.125	-0.044	52.756	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.011	-0.006	56.345	0.000	0.000	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.052	-0.007	54.919	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	THR	0	0.021	0.009	58.177	0.000	0.000	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.025	-0.016	57.497	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.017	0.016	61.827	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.040	-0.055	64.348	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.916	0.949	66.455	0.013	0.013	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.010	-0.001	68.493	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.074	0.035	70.491	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.894	-0.960	70.941	-0.014	-0.014	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.003	0.011	72.527	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.007	0.005	70.702	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.900	0.944	64.945	0.016	0.016	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.025	0.018	63.352	0.000	0.000	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.044	0.021	67.281	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.003	0.007	63.903	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.048	-0.031	59.180	0.000	0.000	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.006	0.009	57.546	0.000	0.000	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.020	-0.027	53.928	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	95	SER	0	0.070	0.006	49.544	0.000	0.000	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.955	0.984	50.761	0.021	0.021	0.000	0.000	0.000	0.000
97	A	97	GLN	0	0.105	0.071	52.435	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.014	0.007	52.834	0.000	0.000	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.006	-0.006	49.774	0.000	0.000	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.936	-0.975	51.606	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.022	-0.015	54.059	0.001	0.001	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.023	0.001	50.178	0.000	0.000	0.000	0.000	0.000	0.000
103	A	103	GLN	0	0.018	-0.004	50.054	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.065	-0.042	52.900	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	GLN	0	0.005	-0.006	56.489	0.000	0.000	0.000	0.000	0.000	0.000
106	A	106	HIS	0	0.007	-0.001	53.930	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	107	GLY	0	-0.002	0.021	52.881	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.067	-0.028	48.338	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.969	0.993	44.917	0.028	0.028	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.012	-0.013	45.247	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.832	-0.916	41.945	-0.030	-0.030	0.000	0.000	0.000	0.000
112	A	112	LYN	0	0.082	0.035	44.624	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.832	0.895	41.157	0.029	0.029	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.927	0.980	39.684	0.042	0.042	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.023	0.002	44.188	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.929	-0.965	43.984	-0.040	-0.040	0.000	0.000	0.000	0.000
117	A	117	LEU	0	-0.047	-0.027	47.904	0.000	0.000	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.003	0.009	50.550	0.000	0.000	0.000	0.000	0.000	0.000
119	A	119	ASP	-1	-0.888	-0.935	52.147	-0.022	-0.022	0.000	0.000	0.000	0.000
120	A	120	ALA	0	-0.078	-0.053	55.523	0.000	0.000	0.000	0.000	0.000	0.000
121	A	121	ILE	0	0.063	0.036	56.921	0.001	0.001	0.000	0.000	0.000	0.000
122	A	122	ARG	1	0.911	0.942	59.609	0.017	0.017	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.005	-0.034	63.066	0.001	0.001	0.000	0.000	0.000	0.000
124	A	124	LEU	0	0.050	0.043	64.335	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.005	0.015	65.555	0.000	0.000	0.000	0.000	0.000	0.000
126	A	126	TYR	0	-0.017	-0.015	61.855	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	127	THR	0	-0.018	-0.016	56.778	0.000	0.000	0.000	0.000	0.000	0.000
128	A	128	ASN	0	0.026	0.028	55.134	0.000	0.000	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.033	0.008	50.994	0.000	0.000	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.022	0.028	48.204	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	131	VAL	0	0.006	0.001	45.392	0.001	0.001	0.000	0.000	0.000	0.000
132	A	132	LYS	1	0.907	0.973	39.619	0.050	0.050	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.061	-0.037	41.716	0.000	0.000	0.000	0.000	0.000	0.000
134	A	134	HIS	0	0.031	0.014	33.917	0.001	0.001	0.000	0.000	0.000	0.000
135	A	135	PRO	0	0.000	-0.004	33.737	0.002	0.002	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.907	-0.960	34.767	-0.077	-0.077	0.000	0.000	0.000	0.000
137	A	137	VAL	0	-0.073	-0.040	38.512	0.001	0.001	0.000	0.000	0.000	0.000
138	A	138	THR	0	0.008	0.001	41.302	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	139	ALA	0	-0.018	0.001	44.532	0.000	0.000	0.000	0.000	0.000	0.000
140	A	140	THR	0	-0.008	-0.005	47.800	0.001	0.001	0.000	0.000	0.000	0.000
141	A	141	LEU	0	0.005	0.003	51.334	0.000	0.000	0.000	0.000	0.000	0.000
142	A	142	LYS	1	0.920	0.960	52.992	0.026	0.026	0.000	0.000	0.000	0.000
143	A	143	VAL	0	-0.009	-0.008	55.471	0.000	0.000	0.000	0.000	0.000	0.000
144	A	144	HIS	0	-0.021	-0.015	58.207	0.000	0.000	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.016	0.007	61.445	0.000	0.000	0.000	0.000	0.000	0.000
146	A	146	THR	0	0.010	0.012	63.720	0.000	0.000	0.000	0.000	0.000	0.000
147	A	147	GLU	-1	-0.868	-0.924	67.216	-0.014	-0.014	0.000	0.000	0.000	0.000
148	A	148	GLN	0	-0.015	-0.018	67.636	0.000	0.000	0.000	0.000	0.000	0.000
149	A	149	LYN	0	0.017	0.041	70.544	0.000	0.000	0.000	0.000	0.000	0.000

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