FMO DATABASE

FMODB ID: 43VMN

Calculation Name: 1TUL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TUL

Chain ID: A

ChEMBL ID:

UniProt ID: Q06691

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	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	102
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-772958.061444
FMO2-HF: Nuclear repulsion	732022.397812
FMO2-HF: Total energy	-40935.663633
FMO2-MP2: Total energy	-41053.433119

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:7:GLY)

Summations of interaction energy for fragment #1(A:7:GLY)

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.
-3.016	-1.794	-0.016	-0.571	-0.635	0.002

Interaction energy analysis for fragmet #1(A:7:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.003 / q_NPA : -0.015

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	9	PRO	0	0.060	0.041	3.800	-1.266	-0.044	-0.016	-0.571	-0.635	0.002
4	A	10	ASP	-1	-0.882	-0.911	6.502	-0.548	-0.548	0.000	0.000	0.000	0.000
5	A	11	ILE	0	-0.020	-0.006	9.149	0.050	0.050	0.000	0.000	0.000	0.000
6	A	12	ILE	0	0.031	0.019	12.326	0.011	0.011	0.000	0.000	0.000	0.000
7	A	13	VAL	0	-0.011	0.000	15.331	0.040	0.040	0.000	0.000	0.000	0.000
8	A	14	ASN	0	-0.037	-0.025	18.687	-0.012	-0.012	0.000	0.000	0.000	0.000
9	A	15	ALA	0	0.013	0.015	22.140	0.013	0.013	0.000	0.000	0.000	0.000
10	A	16	GLN	0	-0.030	-0.017	24.754	0.006	0.006	0.000	0.000	0.000	0.000
11	A	17	ILE	0	0.004	-0.008	28.208	0.003	0.003	0.000	0.000	0.000	0.000
12	A	18	ASN	0	-0.072	-0.042	30.534	0.002	0.002	0.000	0.000	0.000	0.000
13	A	19	SER	0	-0.010	-0.024	32.181	0.000	0.000	0.000	0.000	0.000	0.000
14	A	20	GLU	-1	-0.949	-0.961	35.177	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	21	ASP	-1	-0.887	-0.948	34.797	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	22	GLU	-1	-0.885	-0.944	34.488	-0.031	-0.031	0.000	0.000	0.000	0.000
17	A	23	ASN	0	-0.099	-0.041	34.385	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	24	VAL	0	0.019	-0.004	29.801	0.003	0.003	0.000	0.000	0.000	0.000
19	A	25	LEU	0	-0.037	0.005	26.979	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	26	ASP	-1	-0.713	-0.847	26.424	-0.039	-0.039	0.000	0.000	0.000	0.000
21	A	27	PHE	0	-0.004	-0.012	21.024	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	28	ILE	0	-0.005	-0.008	22.062	0.007	0.007	0.000	0.000	0.000	0.000
23	A	29	ILE	0	-0.041	-0.015	17.199	-0.022	-0.022	0.000	0.000	0.000	0.000
24	A	30	GLU	-1	-0.903	-0.942	17.827	-0.263	-0.263	0.000	0.000	0.000	0.000
25	A	31	ASP	-1	-0.880	-0.951	15.815	-0.289	-0.289	0.000	0.000	0.000	0.000
26	A	32	GLU	-1	-1.000	-0.997	16.584	-0.093	-0.093	0.000	0.000	0.000	0.000
27	A	33	TYR	0	-0.063	-0.076	7.971	0.111	0.111	0.000	0.000	0.000	0.000
28	A	34	TYR	0	-0.006	-0.006	13.742	0.078	0.078	0.000	0.000	0.000	0.000
29	A	35	LEU	0	-0.049	-0.033	8.217	0.061	0.061	0.000	0.000	0.000	0.000
30	A	36	LYS	1	1.016	1.021	12.522	-0.227	-0.227	0.000	0.000	0.000	0.000
31	A	37	LYS	1	0.848	0.944	7.846	-0.880	-0.880	0.000	0.000	0.000	0.000
32	A	38	ARG	1	0.938	0.966	10.856	-0.994	-0.994	0.000	0.000	0.000	0.000
33	A	39	GLY	0	0.024	0.012	13.635	0.082	0.082	0.000	0.000	0.000	0.000
34	A	40	VAL	0	0.022	0.008	14.282	0.014	0.014	0.000	0.000	0.000	0.000
35	A	41	GLY	0	-0.074	-0.027	10.726	0.098	0.098	0.000	0.000	0.000	0.000
36	A	42	ALA	0	0.034	0.014	9.583	-0.107	-0.107	0.000	0.000	0.000	0.000
37	A	43	HIS	0	0.010	-0.006	7.882	0.268	0.268	0.000	0.000	0.000	0.000
38	A	44	ILE	0	0.061	0.038	7.733	0.070	0.070	0.000	0.000	0.000	0.000
39	A	45	ILE	0	-0.020	-0.010	9.958	-0.092	-0.092	0.000	0.000	0.000	0.000
40	A	46	LYS	1	0.956	0.973	12.603	0.551	0.551	0.000	0.000	0.000	0.000
41	A	47	VAL	0	-0.019	-0.015	14.369	0.013	0.013	0.000	0.000	0.000	0.000
42	A	48	ALA	0	0.000	0.019	18.139	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	49	SER	0	-0.019	-0.029	20.108	0.017	0.017	0.000	0.000	0.000	0.000
44	A	50	SER	0	-0.040	-0.027	22.871	0.005	0.005	0.000	0.000	0.000	0.000
45	A	51	PRO	0	0.059	0.023	26.218	0.005	0.005	0.000	0.000	0.000	0.000
46	A	52	GLN	0	-0.007	-0.009	27.876	0.008	0.008	0.000	0.000	0.000	0.000
47	A	53	LEU	0	-0.008	0.004	23.039	0.008	0.008	0.000	0.000	0.000	0.000
48	A	54	ARG	1	0.921	0.967	27.461	0.063	0.063	0.000	0.000	0.000	0.000
49	A	55	LEU	0	-0.046	-0.029	30.280	0.006	0.006	0.000	0.000	0.000	0.000
50	A	56	LEU	0	-0.023	-0.010	25.291	0.006	0.006	0.000	0.000	0.000	0.000
51	A	57	TYR	0	-0.037	-0.037	24.325	0.007	0.007	0.000	0.000	0.000	0.000
52	A	58	LYS	1	0.821	0.923	30.433	0.047	0.047	0.000	0.000	0.000	0.000
53	A	59	ASN	0	-0.044	-0.017	32.643	0.001	0.001	0.000	0.000	0.000	0.000
54	A	60	ALA	0	0.033	0.031	31.682	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	61	TYR	0	0.018	-0.015	24.324	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	62	SER	0	-0.001	0.018	28.236	0.004	0.004	0.000	0.000	0.000	0.000
57	A	63	THR	0	0.013	0.005	21.935	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	64	VAL	0	-0.001	0.008	25.335	0.010	0.010	0.000	0.000	0.000	0.000
59	A	65	SER	0	-0.011	-0.025	21.601	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	66	CYS	0	-0.036	0.003	22.500	0.000	0.000	0.000	0.000	0.000	0.000
61	A	67	GLY	0	0.041	0.005	22.182	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	68	ASN	0	-0.043	-0.002	20.929	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	69	TYR	0	-0.033	-0.059	17.147	0.030	0.030	0.000	0.000	0.000	0.000
64	A	70	GLY	0	0.018	0.032	17.923	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	71	VAL	0	-0.005	-0.011	17.353	0.008	0.008	0.000	0.000	0.000	0.000
66	A	72	LEU	0	-0.008	0.004	16.637	0.005	0.005	0.000	0.000	0.000	0.000
67	A	73	CYS	0	-0.022	-0.005	17.758	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	74	ASN	0	-0.004	0.002	19.575	0.022	0.022	0.000	0.000	0.000	0.000
69	A	75	LEU	0	-0.015	0.003	21.323	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	76	VAL	0	0.009	-0.008	20.567	0.003	0.003	0.000	0.000	0.000	0.000
71	A	77	GLN	0	-0.033	-0.022	23.123	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	78	ASN	0	0.001	-0.006	24.665	0.014	0.014	0.000	0.000	0.000	0.000
73	A	79	GLY	0	0.001	0.007	25.384	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	80	GLU	-1	-0.803	-0.918	26.576	-0.055	-0.055	0.000	0.000	0.000	0.000
75	A	81	TYR	0	-0.031	-0.018	26.093	0.007	0.007	0.000	0.000	0.000	0.000
76	A	82	ASP	-1	-0.762	-0.865	21.167	-0.173	-0.173	0.000	0.000	0.000	0.000
77	A	83	LEU	0	-0.023	0.003	20.572	0.021	0.021	0.000	0.000	0.000	0.000
78	A	84	ASN	0	0.036	0.035	16.836	-0.043	-0.043	0.000	0.000	0.000	0.000
79	A	85	ALA	0	0.031	-0.005	15.641	0.026	0.026	0.000	0.000	0.000	0.000
80	A	86	ILE	0	-0.020	0.004	11.467	-0.034	-0.034	0.000	0.000	0.000	0.000
81	A	87	MET	0	0.027	0.021	12.248	0.015	0.015	0.000	0.000	0.000	0.000
82	A	88	PHE	0	-0.024	-0.023	12.507	0.052	0.052	0.000	0.000	0.000	0.000
83	A	89	ASN	0	-0.002	-0.005	12.365	0.001	0.001	0.000	0.000	0.000	0.000
84	A	90	CYS	0	0.012	0.002	15.185	0.047	0.047	0.000	0.000	0.000	0.000
85	A	91	ALA	0	0.001	0.003	17.974	0.019	0.019	0.000	0.000	0.000	0.000
86	A	92	GLU	-1	-0.957	-0.976	15.524	0.230	0.230	0.000	0.000	0.000	0.000
87	A	93	ILE	0	-0.022	-0.025	11.159	-0.038	-0.038	0.000	0.000	0.000	0.000
88	A	94	LYS	1	0.979	1.002	15.219	-0.056	-0.056	0.000	0.000	0.000	0.000
89	A	95	LEU	0	-0.033	-0.007	14.690	0.000	0.000	0.000	0.000	0.000	0.000
90	A	96	ASN	0	0.063	0.018	17.947	-0.029	-0.029	0.000	0.000	0.000	0.000
91	A	97	LYS	1	0.974	0.983	20.251	0.171	0.171	0.000	0.000	0.000	0.000
92	A	98	GLY	0	-0.042	-0.031	21.065	0.016	0.016	0.000	0.000	0.000	0.000
93	A	99	GLN	0	0.008	0.029	21.120	0.009	0.009	0.000	0.000	0.000	0.000
94	A	100	MET	0	0.023	0.016	22.161	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	101	LEU	0	-0.015	-0.001	16.280	0.013	0.013	0.000	0.000	0.000	0.000
96	A	102	PHE	0	0.006	-0.021	18.396	0.023	0.023	0.000	0.000	0.000	0.000
97	A	103	GLN	0	0.042	0.017	22.550	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	104	THR	0	-0.016	0.000	24.459	0.005	0.005	0.000	0.000	0.000	0.000
99	A	105	LYS	1	0.887	0.966	26.989	0.013	0.013	0.000	0.000	0.000	0.000
100	A	106	ILE	0	0.003	0.007	30.155	0.004	0.004	0.000	0.000	0.000	0.000
101	A	107	TRP	0	-0.068	-0.050	31.955	0.000	0.000	0.000	0.000	0.000	0.000
102	A	108	ARG	1	0.944	0.968	35.507	0.032	0.032	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)