FMO DATABASE

FMODB ID: 49GLN

Calculation Name: 1TVD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TVD

Chain ID: A

ChEMBL ID:

UniProt ID: A0JD37

Base Structure: X-ray

Registration Date: 2023-06-26

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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-962030.793383
FMO2-HF: Nuclear repulsion	916390.91302
FMO2-HF: Total energy	-45639.880363
FMO2-MP2: Total energy	-45774.891374

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:ASP)

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

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.
-28.392	-39.672	49.442	-20.751	-17.411	0.152

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.806 / q_NPA : -0.870

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	3	VAL	0	0.052	0.050	3.893	-1.841	0.251	-0.019	-1.076	-0.996	0.003
4	A	4	THR	0	-0.066	-0.036	7.051	-1.342	-1.342	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.019	0.005	10.181	0.945	0.945	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.002	-0.008	13.732	-0.060	-0.060	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.015	-0.011	16.420	-0.574	-0.574	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.005	0.009	19.482	0.359	0.359	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.783	-0.890	20.953	14.114	14.114	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.048	-0.017	23.208	-0.801	-0.801	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.029	0.003	26.369	0.208	0.208	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.011	0.010	29.181	-0.123	-0.123	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.055	0.041	31.637	-0.071	-0.071	0.000	0.000	0.000	0.000
14	A	14	SER	0	0.034	-0.001	33.585	0.305	0.305	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.055	-0.023	34.133	-0.261	-0.261	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.045	-0.029	31.622	-0.093	-0.093	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.872	-0.903	27.942	10.638	10.638	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.034	-0.019	24.116	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.032	0.015	20.781	0.229	0.229	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.037	0.011	18.307	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.011	-0.006	16.671	0.744	0.744	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.054	-0.024	11.554	0.890	0.890	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.013	0.001	9.549	-1.341	-1.341	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.007	-0.036	6.556	0.626	0.626	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.872	-0.942	4.362	45.166	45.445	-0.001	-0.063	-0.215	0.000
26	A	26	THR	0	-0.026	-0.046	1.544	-13.681	-24.214	29.097	-12.406	-6.158	0.065
27	A	27	VAL	0	-0.008	0.001	3.150	-19.416	-20.230	0.069	1.606	-0.860	0.009
28	A	28	TYR	0	-0.055	-0.037	1.681	-38.616	-43.824	17.217	-6.625	-5.384	0.070
29	A	29	SER	0	-0.007	-0.011	6.303	-2.009	-2.009	0.000	0.000	0.000	0.000
30	A	30	ASN	0	-0.003	0.010	9.599	2.018	2.018	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.011	0.030	6.609	-0.770	-0.770	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.839	-0.895	9.068	21.280	21.280	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.016	-0.013	9.469	3.013	3.013	0.000	0.000	0.000	0.000
34	A	34	PHE	0	-0.011	-0.020	11.813	-2.497	-2.497	0.000	0.000	0.000	0.000
35	A	35	TRP	0	-0.027	-0.035	13.315	0.707	0.707	0.000	0.000	0.000	0.000
36	A	36	TYR	0	0.024	0.018	13.650	-1.384	-1.384	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.817	0.893	17.612	-11.812	-11.812	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.009	0.011	20.043	-0.216	-0.216	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.885	0.928	21.919	-10.823	-10.823	0.000	0.000	0.000	0.000
40	A	40	PRO	0	0.018	-0.011	25.566	0.154	0.154	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.803	-0.845	27.898	10.502	10.502	0.000	0.000	0.000	0.000
42	A	42	TYR	0	-0.006	-0.010	24.646	-0.149	-0.149	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.057	-0.042	23.751	0.482	0.482	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.028	-0.003	16.909	0.065	0.065	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.005	0.000	21.434	-0.430	-0.430	0.000	0.000	0.000	0.000
46	A	46	PHE	0	0.044	0.019	17.809	0.525	0.525	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.056	-0.023	19.418	-0.760	-0.760	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.019	-0.007	18.734	-0.630	-0.630	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.033	-0.017	15.655	0.316	0.316	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.001	-0.020	15.536	-1.290	-1.290	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.709	-0.815	13.863	19.442	19.442	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.968	-1.020	13.867	19.862	19.862	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.091	-0.046	15.541	-1.252	-1.252	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.791	0.888	18.550	-17.052	-17.052	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.022	-0.025	18.412	1.010	1.010	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.900	-0.934	20.219	13.254	13.254	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.043	0.017	20.840	0.735	0.735	0.000	0.000	0.000	0.000
58	A	57	ALA	0	-0.006	0.000	23.172	-0.327	-0.327	0.000	0.000	0.000	0.000
59	A	57	ASP	-1	-0.863	-0.917	24.637	10.933	10.933	0.000	0.000	0.000	0.000
60	A	57	PHE	0	-0.074	-0.044	24.161	-0.277	-0.277	0.000	0.000	0.000	0.000
61	A	57	THR	0	-0.069	-0.058	23.964	-0.086	-0.086	0.000	0.000	0.000	0.000
62	A	57	GLN	0	0.020	0.008	27.359	0.281	0.281	0.000	0.000	0.000	0.000
63	A	58	GLY	0	-0.002	-0.009	29.661	-0.416	-0.416	0.000	0.000	0.000	0.000
64	A	59	ARG	1	0.718	0.835	29.327	-10.463	-10.463	0.000	0.000	0.000	0.000
65	A	60	PHE	0	0.010	0.008	23.622	0.193	0.193	0.000	0.000	0.000	0.000
66	A	61	SER	0	-0.019	0.003	23.923	-0.165	-0.165	0.000	0.000	0.000	0.000
67	A	62	VAL	0	0.038	0.016	18.241	0.254	0.254	0.000	0.000	0.000	0.000
68	A	63	LYS	1	0.928	0.967	19.145	-14.117	-14.117	0.000	0.000	0.000	0.000
69	A	64	HIS	0	0.041	0.040	13.413	2.070	2.070	0.000	0.000	0.000	0.000
70	A	65	ILE	0	-0.069	-0.032	15.342	-1.161	-1.161	0.000	0.000	0.000	0.000
71	A	66	LEU	0	0.074	0.039	13.806	1.067	1.067	0.000	0.000	0.000	0.000
72	A	67	THR	0	-0.017	-0.018	13.340	1.531	1.531	0.000	0.000	0.000	0.000
73	A	68	GLN	0	-0.049	-0.029	14.117	-0.322	-0.322	0.000	0.000	0.000	0.000
74	A	69	LYS	1	0.838	0.947	6.354	-42.052	-42.052	0.000	0.000	0.000	0.000
75	A	70	ALA	0	0.018	0.016	10.396	1.129	1.129	0.000	0.000	0.000	0.000
76	A	71	PHE	0	0.075	0.006	12.673	-0.227	-0.227	0.000	0.000	0.000	0.000
77	A	72	HIS	0	0.036	0.038	14.363	0.014	0.014	0.000	0.000	0.000	0.000
78	A	73	LEU	0	0.039	0.036	17.210	-0.451	-0.451	0.000	0.000	0.000	0.000
79	A	74	VAL	0	-0.043	-0.020	19.601	-0.230	-0.230	0.000	0.000	0.000	0.000
80	A	75	ILE	0	-0.019	-0.007	23.307	-0.016	-0.016	0.000	0.000	0.000	0.000
81	A	76	SER	0	-0.042	-0.037	26.248	-0.308	-0.308	0.000	0.000	0.000	0.000
82	A	77	PRO	0	0.020	0.023	29.805	-0.052	-0.052	0.000	0.000	0.000	0.000
83	A	78	VAL	0	0.013	-0.008	27.941	0.172	0.172	0.000	0.000	0.000	0.000
84	A	79	ARG	1	0.858	0.893	30.620	-9.339	-9.339	0.000	0.000	0.000	0.000
85	A	80	THR	0	0.049	0.015	31.125	0.298	0.298	0.000	0.000	0.000	0.000
86	A	81	GLU	-1	-0.818	-0.866	30.298	9.644	9.644	0.000	0.000	0.000	0.000
87	A	82	ASP	-1	-0.750	-0.839	26.910	11.099	11.099	0.000	0.000	0.000	0.000
88	A	83	SER	0	-0.018	-0.006	26.262	0.442	0.442	0.000	0.000	0.000	0.000
89	A	84	ALA	0	-0.005	0.008	23.379	-0.142	-0.142	0.000	0.000	0.000	0.000
90	A	85	THR	0	-0.030	-0.008	18.944	-0.109	-0.109	0.000	0.000	0.000	0.000
91	A	86	TYR	0	0.000	-0.012	18.588	0.332	0.332	0.000	0.000	0.000	0.000
92	A	87	TYR	0	-0.006	-0.006	13.597	-0.131	-0.131	0.000	0.000	0.000	0.000
93	A	89	ALA	0	-0.006	-0.024	9.026	0.593	0.593	0.000	0.000	0.000	0.000
94	A	90	PHE	0	0.019	0.012	2.353	-5.223	-3.168	1.040	-1.218	-1.877	0.006
95	A	91	THR	0	-0.003	0.000	6.987	1.353	1.353	0.000	0.000	0.000	0.000
96	A	92	LEU	0	0.000	0.006	3.117	3.394	4.452	0.140	-0.414	-0.785	0.002
97	A	98	PRO	0	0.045	0.019	5.993	-5.708	-5.708	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.050	0.037	9.194	0.440	0.440	0.000	0.000	0.000	0.000
99	A	100	PRO	0	-0.080	-0.034	11.599	0.740	0.740	0.000	0.000	0.000	0.000
100	A	101	THR	0	-0.045	-0.025	7.423	-1.111	-1.111	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.848	-0.936	10.471	22.890	22.890	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.851	0.920	9.468	-26.080	-26.080	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.005	0.010	7.972	3.479	3.479	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.009	0.011	2.302	-1.029	-1.238	1.899	-0.555	-1.136	-0.003
105	A	106	PHE	0	0.027	-0.004	6.208	-0.722	-0.722	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.006	0.007	8.480	1.349	1.349	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.787	0.870	10.659	-16.674	-16.674	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.044	0.030	13.570	-0.990	-0.990	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.064	-0.037	16.063	0.244	0.244	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.838	0.908	19.153	-11.270	-11.270	0.000	0.000	0.000	0.000
111	A	112	VAL	0	0.024	0.015	22.669	-0.051	-0.051	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.035	-0.012	25.232	0.010	0.010	0.000	0.000	0.000	0.000
113	A	114	VAL	0	0.001	0.008	28.794	-0.091	-0.091	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.836	-0.927	31.399	8.804	8.804	0.000	0.000	0.000	0.000
115	A	116	PRO	0	-0.038	-0.017	34.982	-0.077	-0.077	0.000	0.000	0.000	0.000

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