FMO DATABASE

FMODB ID: 1N45Z

Calculation Name: 1DCF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1DCF

Chain ID: A

ChEMBL ID:

UniProt ID: P49333

Base Structure: X-ray

Registration Date: 2023-09-21

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1210397.567837
FMO2-HF: Nuclear repulsion	1155939.642602
FMO2-HF: Total energy	-54457.925235
FMO2-MP2: Total energy	-54611.445684

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:HIS)

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

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.
-6.436	2.048	1.305	-3.745	-6.041	-0.003

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

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 : 0.006

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	SER	0	-0.053	-0.034	3.698	-1.680	1.545	0.129	-1.415	-1.939	0.005
4	A	4	ASN	0	-0.028	-0.008	5.217	-0.922	-0.780	-0.001	-0.011	-0.129	0.000
5	A	5	PHE	0	0.054	0.015	5.084	-0.147	-0.147	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.001	-0.013	10.592	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.004	0.015	13.965	0.015	0.015	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.023	-0.004	11.136	0.021	0.021	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.983	1.003	14.941	0.093	0.093	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.000	0.012	13.540	0.022	0.022	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.036	-0.025	16.978	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.011	-0.003	16.923	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	13	MET	0	-0.016	-0.015	19.486	0.007	0.007	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.796	-0.901	21.250	-0.186	-0.186	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.854	-0.922	23.280	-0.130	-0.130	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.038	0.017	24.348	0.000	0.000	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.008	-0.014	24.275	-0.011	-0.011	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.034	0.017	22.738	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.034	-0.016	20.470	-0.039	-0.039	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.925	0.960	19.589	0.126	0.126	0.000	0.000	0.000	0.000
21	A	21	MET	0	-0.058	-0.026	20.018	-0.017	-0.017	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.005	-0.010	16.584	-0.023	-0.023	0.000	0.000	0.000	0.000
23	A	23	THR	0	0.006	-0.003	14.755	-0.062	-0.062	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.946	0.973	15.195	0.180	0.180	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.014	0.007	16.523	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.008	-0.003	11.809	-0.040	-0.040	0.000	0.000	0.000	0.000
27	A	27	LEU	0	0.018	0.002	11.319	-0.064	-0.064	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.007	-0.005	13.056	0.024	0.024	0.000	0.000	0.000	0.000
29	A	29	HIS	0	-0.027	-0.003	10.626	0.087	0.087	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.044	-0.019	7.638	-0.070	-0.070	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.026	0.017	10.964	0.078	0.078	0.000	0.000	0.000	0.000
32	A	32	CYS	0	-0.040	0.002	12.028	0.058	0.058	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.935	-0.964	14.829	-0.164	-0.164	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.037	-0.016	16.244	0.016	0.016	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.058	-0.028	18.918	0.011	0.011	0.000	0.000	0.000	0.000
36	A	36	THR	0	-0.038	-0.024	20.713	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.005	0.003	22.979	0.010	0.010	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.005	-0.008	24.668	-0.010	-0.010	0.000	0.000	0.000	0.000
39	A	39	SER	0	0.052	0.020	27.196	0.007	0.007	0.000	0.000	0.000	0.000
40	A	40	ASN	0	0.069	0.014	27.715	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.886	-0.950	29.025	-0.049	-0.049	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.871	-0.946	28.526	-0.097	-0.097	0.000	0.000	0.000	0.000
43	A	43	CYS	0	0.011	0.003	24.487	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.001	0.005	26.753	0.003	0.003	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.900	0.970	29.007	0.064	0.064	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.017	-0.002	25.457	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.016	0.006	22.878	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.020	-0.012	24.366	0.009	0.009	0.000	0.000	0.000	0.000
49	A	49	HIS	0	0.033	0.011	23.427	0.004	0.004	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.947	-0.975	22.457	-0.076	-0.076	0.000	0.000	0.000	0.000
51	A	51	HIS	0	-0.070	-0.035	19.696	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.977	0.988	15.958	0.061	0.061	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.015	0.013	12.707	0.025	0.025	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.004	0.002	16.023	-0.029	-0.029	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.010	0.011	11.103	0.012	0.012	0.000	0.000	0.000	0.000
56	A	56	MET	0	-0.019	-0.010	16.619	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.738	-0.863	19.000	-0.163	-0.163	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.081	-0.051	19.821	0.019	0.019	0.000	0.000	0.000	0.000
59	A	59	CYS	0	-0.087	-0.029	21.440	0.000	0.000	0.000	0.000	0.000	0.000
60	A	60	MET	0	0.002	0.037	23.871	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	PRO	0	0.001	0.007	26.847	0.004	0.004	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.010	-0.011	29.107	0.004	0.004	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.055	-0.007	27.089	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.896	-0.944	28.250	-0.048	-0.048	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.005	-0.013	24.395	0.010	0.010	0.000	0.000	0.000	0.000
66	A	66	TYR	0	0.045	0.013	21.403	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.060	0.026	25.296	0.009	0.009	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.050	-0.022	24.123	0.005	0.005	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.120	0.041	22.623	0.000	0.000	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.010	0.027	24.354	0.006	0.006	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.911	0.950	27.447	0.035	0.035	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.009	-0.007	22.979	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	HIS	0	0.014	0.034	22.622	0.009	0.009	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.957	-0.950	26.580	0.008	0.008	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.785	0.874	27.912	0.045	0.045	0.000	0.000	0.000	0.000
76	A	76	PHE	0	-0.038	-0.019	25.120	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	77	THR	0	-0.061	-0.032	28.089	0.005	0.005	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.901	0.945	30.190	0.000	0.000	0.000	0.000	0.000	0.000
79	A	79	GLN	0	-0.035	-0.010	30.725	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.941	0.964	29.503	0.013	0.013	0.000	0.000	0.000	0.000
81	A	81	HIS	0	0.018	0.022	25.413	0.005	0.005	0.000	0.000	0.000	0.000
82	A	82	GLN	0	0.066	0.020	21.351	0.003	0.003	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.857	0.951	19.444	-0.073	-0.073	0.000	0.000	0.000	0.000
84	A	84	PRO	0	-0.057	-0.014	19.174	0.009	0.009	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.054	0.026	13.321	0.004	0.004	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.046	-0.023	17.027	-0.034	-0.034	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.032	0.011	12.182	0.028	0.028	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.002	0.004	15.260	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.001	0.014	14.554	-0.026	-0.026	0.000	0.000	0.000	0.000
90	A	90	SER	0	0.033	-0.023	16.758	0.015	0.015	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.049	0.024	17.570	-0.034	-0.034	0.000	0.000	0.000	0.000
92	A	92	ASN	0	0.013	0.012	19.125	0.020	0.020	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.092	0.051	14.662	0.004	0.004	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.800	-0.902	18.061	0.018	0.018	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.977	0.965	21.172	-0.055	-0.055	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.035	0.007	23.173	0.006	0.006	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.002	-0.015	18.865	0.000	0.000	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.898	0.941	17.639	-0.089	-0.089	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.930	-0.971	20.451	0.080	0.080	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.850	0.939	23.356	0.023	0.023	0.000	0.000	0.000	0.000
101	A	101	CYS	0	0.006	-0.002	19.058	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	102	MET	0	0.015	0.024	19.986	0.003	0.003	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.017	-0.003	22.408	0.000	0.000	0.000	0.000	0.000	0.000
104	A	104	PHE	0	-0.084	-0.057	24.121	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.014	-0.001	22.532	-0.011	-0.011	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.054	-0.032	17.970	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-0.811	-0.900	15.508	0.106	0.106	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.017	0.011	12.904	0.067	0.067	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.059	-0.037	12.884	-0.042	-0.042	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.010	0.000	9.115	0.003	0.003	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.033	-0.002	12.577	0.041	0.041	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.817	0.902	13.743	0.128	0.128	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.001	-0.026	16.165	0.040	0.040	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.011	0.015	11.919	-0.029	-0.029	0.000	0.000	0.000	0.000
115	A	115	SER	0	0.006	-0.015	10.041	-0.066	-0.066	0.000	0.000	0.000	0.000
116	A	116	LEU	0	0.015	-0.007	7.436	-0.092	-0.092	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.908	-0.937	5.138	-3.847	-3.847	0.000	0.000	0.000	0.000
118	A	118	ASN	0	0.027	0.011	4.748	-0.626	-0.561	-0.001	-0.002	-0.062	0.000
119	A	119	ILE	0	0.009	0.004	6.896	0.343	0.343	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.849	0.913	2.476	1.786	2.988	0.854	-0.656	-1.399	0.004
121	A	121	ASP	-1	-0.880	-0.927	2.901	1.176	2.509	0.166	-0.550	-0.950	-0.005
122	A	122	VAL	0	0.049	0.036	3.501	1.197	1.358	0.012	0.051	-0.224	-0.001
123	A	123	LEU	0	-0.041	-0.023	6.624	0.187	0.187	0.000	0.000	0.000	0.000
124	A	124	SER	0	0.023	-0.007	3.508	0.696	1.673	0.113	-0.368	-0.721	0.000
125	A	125	ASP	-1	-0.897	-0.938	5.624	1.548	1.548	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.151	-0.086	7.249	-0.376	-0.376	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.078	-0.049	8.592	-0.160	-0.160	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.919	-0.950	3.689	-5.215	-3.836	0.033	-0.794	-0.617	-0.006
129	A	129	PRO	0	-0.059	-0.030	7.846	0.161	0.161	0.000	0.000	0.000	0.000
130	A	130	ARG	1	1.003	1.002	8.891	-0.591	-0.591	0.000	0.000	0.000	0.000
131	A	131	VAL	0	-0.027	-0.016	11.291	-0.051	-0.051	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.050	-0.020	14.259	0.055	0.055	0.000	0.000	0.000	0.000
133	A	133	TYR	0	-0.009	-0.002	13.207	-0.036	-0.036	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.936	-0.965	18.182	0.313	0.313	0.000	0.000	0.000	0.000

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