FMO DATABASE

FMODB ID: LNQ19

Calculation Name: 1TWU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TWU

Chain ID: A

ChEMBL ID:

UniProt ID: P37479

Base Structure: X-ray

Registration Date: 2023-09-22

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	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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1178688.407881
FMO2-HF: Nuclear repulsion	1124768.177012
FMO2-HF: Total energy	-53920.230869
FMO2-MP2: Total energy	-54078.116771

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-207.244	-200.105	31.315	-17.338	-21.112	-0.199

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.823 / q_NPA : 0.903

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	5	PHE	0	0.004	0.005	2.996	2.472	4.497	0.069	-0.729	-1.365	0.001
4	A	6	SER	0	-0.011	-0.021	5.861	0.776	0.776	0.000	0.000	0.000	0.000
5	A	7	SER	0	0.000	0.003	9.505	1.008	1.008	0.000	0.000	0.000	0.000
6	A	8	PHE	0	0.014	0.012	6.732	1.347	1.347	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.023	-0.010	2.374	3.329	3.978	0.653	-0.414	-0.887	0.003
8	A	10	ALA	0	0.022	0.017	3.061	2.342	3.005	0.040	-0.152	-0.550	0.000
9	A	11	ALA	0	0.014	-0.001	2.443	-16.212	-13.925	2.453	-1.908	-2.832	-0.029
10	A	12	GLN	0	-0.042	-0.031	2.119	-14.785	-17.281	8.760	-2.157	-4.106	-0.025
11	A	13	ILE	0	-0.024	-0.013	3.683	7.160	7.501	0.003	0.034	-0.378	0.000
12	A	14	ARG	1	0.820	0.903	5.204	25.221	25.256	-0.001	0.000	-0.034	0.000
13	A	15	ILE	0	-0.018	0.008	8.496	1.449	1.449	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.008	-0.005	11.530	0.241	0.241	0.000	0.000	0.000	0.000
15	A	17	ARG	1	0.922	0.979	14.529	16.621	16.621	0.000	0.000	0.000	0.000
16	A	18	PRO	0	0.010	0.016	17.983	-0.162	-0.162	0.000	0.000	0.000	0.000
17	A	19	THR	0	0.010	-0.045	21.398	0.259	0.259	0.000	0.000	0.000	0.000
18	A	20	GLY	0	0.029	0.027	23.906	0.108	0.108	0.000	0.000	0.000	0.000
19	A	21	GLN	0	-0.084	-0.057	26.086	0.779	0.779	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.045	0.007	20.683	-0.342	-0.342	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.899	-0.944	23.743	-11.963	-11.963	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.831	-0.911	25.864	-11.360	-11.360	0.000	0.000	0.000	0.000
23	A	25	ILE	0	-0.045	-0.014	20.173	-0.351	-0.351	0.000	0.000	0.000	0.000
24	A	26	ILE	0	0.000	-0.008	21.161	-0.697	-0.697	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.890	0.963	22.310	10.525	10.525	0.000	0.000	0.000	0.000
26	A	28	PHE	0	0.026	0.014	20.376	-0.085	-0.085	0.000	0.000	0.000	0.000
27	A	29	TYR	0	-0.060	-0.067	17.083	-0.774	-0.774	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.839	-0.899	19.024	-16.266	-16.266	0.000	0.000	0.000	0.000
29	A	31	GLU	-1	-0.907	-0.961	20.486	-11.709	-11.709	0.000	0.000	0.000	0.000
30	A	32	GLY	0	0.023	-0.008	23.238	0.344	0.344	0.000	0.000	0.000	0.000
31	A	33	LEU	0	-0.070	-0.036	17.537	0.089	0.089	0.000	0.000	0.000	0.000
32	A	34	CYS	0	-0.108	-0.027	19.283	0.012	0.012	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.012	0.010	13.878	-0.893	-0.893	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.916	0.948	13.749	21.426	21.426	0.000	0.000	0.000	0.000
35	A	37	ARG	1	0.886	0.914	14.350	13.406	13.406	0.000	0.000	0.000	0.000
36	A	38	ILE	0	-0.138	-0.076	9.781	0.206	0.206	0.000	0.000	0.000	0.000
37	A	39	GLY	0	0.005	0.003	13.739	-0.840	-0.840	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.845	-0.915	15.517	-14.678	-14.678	0.000	0.000	0.000	0.000
39	A	41	PHE	0	-0.081	-0.028	17.569	-0.083	-0.083	0.000	0.000	0.000	0.000
40	A	42	SER	0	-0.006	-0.016	20.966	0.321	0.321	0.000	0.000	0.000	0.000
41	A	43	GLN	0	-0.040	-0.032	24.608	0.392	0.392	0.000	0.000	0.000	0.000
42	A	44	HIS	0	-0.023	-0.001	20.561	0.548	0.548	0.000	0.000	0.000	0.000
43	A	45	ASN	0	-0.068	-0.050	23.088	0.132	0.132	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.084	0.043	26.260	0.013	0.013	0.000	0.000	0.000	0.000
45	A	47	TYR	0	-0.067	-0.021	22.505	0.095	0.095	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.754	-0.839	23.203	-12.397	-12.397	0.000	0.000	0.000	0.000
47	A	49	GLY	0	0.026	-0.010	19.312	-0.157	-0.157	0.000	0.000	0.000	0.000
48	A	50	VAL	0	-0.013	0.007	17.601	0.084	0.084	0.000	0.000	0.000	0.000
49	A	51	MET	0	-0.037	-0.016	12.223	-0.503	-0.503	0.000	0.000	0.000	0.000
50	A	52	PHE	0	0.009	0.003	13.156	0.404	0.404	0.000	0.000	0.000	0.000
51	A	53	GLY	0	-0.005	-0.010	9.958	-2.141	-2.141	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.029	0.014	8.751	2.511	2.511	0.000	0.000	0.000	0.000
53	A	55	PRO	0	-0.011	-0.020	8.154	-2.851	-2.851	0.000	0.000	0.000	0.000
54	A	56	HIS	0	0.021	-0.010	6.722	2.416	2.416	0.000	0.000	0.000	0.000
55	A	57	ALA	0	0.099	0.032	6.965	0.268	0.268	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.903	-0.920	1.784	-121.082	-123.175	18.442	-9.159	-7.190	-0.112
57	A	59	TYR	0	0.034	-0.010	2.751	-26.420	-20.726	0.897	-2.850	-3.740	-0.037
58	A	60	HIS	0	-0.013	0.015	5.010	8.030	8.064	-0.001	-0.003	-0.030	0.000
59	A	61	LEU	0	0.023	0.016	8.434	-0.253	-0.253	0.000	0.000	0.000	0.000
60	A	62	GLU	-1	-0.812	-0.918	11.810	-21.285	-21.285	0.000	0.000	0.000	0.000
61	A	63	PHE	0	0.016	0.011	14.205	0.304	0.304	0.000	0.000	0.000	0.000
62	A	64	THR	0	0.008	-0.003	17.941	0.295	0.295	0.000	0.000	0.000	0.000
63	A	65	GLN	0	0.063	0.036	20.468	0.026	0.026	0.000	0.000	0.000	0.000
64	A	66	TYR	0	-0.086	-0.056	24.272	0.025	0.025	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.830	-0.916	26.696	-10.232	-10.232	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.051	-0.021	29.794	0.371	0.371	0.000	0.000	0.000	0.000
67	A	69	GLY	0	-0.047	-0.015	31.092	0.150	0.150	0.000	0.000	0.000	0.000
68	A	70	SER	0	-0.049	-0.035	25.301	-0.274	-0.274	0.000	0.000	0.000	0.000
69	A	71	THR	0	0.008	0.004	27.210	0.337	0.337	0.000	0.000	0.000	0.000
70	A	72	ALA	0	0.015	0.020	24.003	-0.413	-0.413	0.000	0.000	0.000	0.000
71	A	73	PRO	0	-0.077	-0.045	20.950	0.346	0.346	0.000	0.000	0.000	0.000
72	A	74	VAL	0	0.003	0.003	24.220	0.226	0.226	0.000	0.000	0.000	0.000
73	A	75	PRO	0	-0.013	0.002	25.472	-0.313	-0.313	0.000	0.000	0.000	0.000
74	A	76	HIS	0	-0.008	0.004	24.787	0.182	0.182	0.000	0.000	0.000	0.000
75	A	77	PRO	0	-0.005	0.002	25.148	-0.519	-0.519	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.843	-0.943	24.987	-11.716	-11.716	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.100	-0.043	20.451	-0.776	-0.776	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.009	-0.018	19.904	0.175	0.175	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.019	0.015	13.484	-1.165	-1.165	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.033	-0.020	16.311	0.748	0.748	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.004	0.008	14.143	-1.734	-1.734	0.000	0.000	0.000	0.000
82	A	84	TYR	0	-0.021	-0.023	15.412	1.002	1.002	0.000	0.000	0.000	0.000
83	A	85	VAL	0	0.013	0.006	17.509	-0.759	-0.759	0.000	0.000	0.000	0.000
84	A	86	PRO	0	-0.032	-0.023	18.860	0.833	0.833	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.046	-0.028	21.745	1.184	1.184	0.000	0.000	0.000	0.000
86	A	88	ALA	0	0.097	0.030	23.993	-0.123	-0.123	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.018	-0.005	26.700	0.207	0.207	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.874	-0.923	21.012	-14.516	-14.516	0.000	0.000	0.000	0.000
89	A	91	LEU	0	-0.028	0.000	23.302	-0.102	-0.102	0.000	0.000	0.000	0.000
90	A	92	ALA	0	0.015	0.006	24.436	0.070	0.070	0.000	0.000	0.000	0.000
91	A	93	ALA	0	-0.016	-0.005	26.012	0.236	0.236	0.000	0.000	0.000	0.000
92	A	94	ILE	0	0.000	0.002	21.381	0.170	0.170	0.000	0.000	0.000	0.000
93	A	95	THR	0	0.007	-0.015	24.695	0.299	0.299	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.003	0.002	26.437	0.416	0.416	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.803	0.900	23.848	13.455	13.455	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.020	0.009	22.718	0.198	0.198	0.000	0.000	0.000	0.000
97	A	99	LYS	1	0.848	0.920	27.267	10.308	10.308	0.000	0.000	0.000	0.000
98	A	100	HIS	0	-0.083	-0.035	30.578	0.237	0.237	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.054	-0.004	26.097	0.141	0.141	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.013	0.010	30.752	0.084	0.084	0.000	0.000	0.000	0.000
101	A	103	TYR	0	-0.061	-0.040	26.953	0.030	0.030	0.000	0.000	0.000	0.000
102	A	104	GLN	0	0.005	-0.004	29.405	0.322	0.322	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.812	-0.898	28.839	-10.687	-10.687	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.060	-0.037	28.019	0.362	0.362	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.880	-0.933	29.852	-9.960	-9.960	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.057	-0.019	27.384	-0.165	-0.165	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.782	-0.893	28.395	-10.004	-10.004	0.000	0.000	0.000	0.000
108	A	110	ASN	0	-0.024	-0.017	26.415	0.575	0.575	0.000	0.000	0.000	0.000
109	A	111	PRO	0	0.072	0.022	28.854	-0.218	-0.218	0.000	0.000	0.000	0.000
110	A	112	TYR	0	-0.048	-0.013	21.953	0.128	0.128	0.000	0.000	0.000	0.000
111	A	113	TRP	0	0.000	-0.019	19.699	-0.280	-0.280	0.000	0.000	0.000	0.000
112	A	114	SER	0	0.030	0.016	26.322	-0.122	-0.122	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.113	-0.055	29.048	0.498	0.498	0.000	0.000	0.000	0.000
114	A	116	GLY	0	-0.011	-0.009	27.859	-0.304	-0.304	0.000	0.000	0.000	0.000
115	A	117	GLY	0	-0.007	-0.017	25.469	-0.598	-0.598	0.000	0.000	0.000	0.000
116	A	118	VAL	0	0.006	0.018	25.202	0.414	0.414	0.000	0.000	0.000	0.000
117	A	119	THR	0	0.019	0.005	24.390	-0.829	-0.829	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.026	-0.008	24.340	0.577	0.577	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.822	-0.897	24.069	-11.668	-11.668	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.798	-0.877	20.872	-14.472	-14.472	0.000	0.000	0.000	0.000
121	A	123	PRO	0	0.015	-0.015	23.315	0.357	0.357	0.000	0.000	0.000	0.000
122	A	124	ASP	-1	-0.842	-0.884	23.590	-12.348	-12.348	0.000	0.000	0.000	0.000
123	A	125	GLY	0	0.008	0.006	25.600	0.070	0.070	0.000	0.000	0.000	0.000
124	A	126	TRP	0	-0.088	-0.040	14.672	-0.553	-0.553	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.801	0.889	22.372	11.553	11.553	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.008	0.003	18.670	-0.907	-0.907	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.004	-0.002	20.078	0.711	0.711	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.020	0.015	19.865	-1.094	-1.094	0.000	0.000	0.000	0.000
129	A	131	MET	0	-0.007	0.008	20.590	0.766	0.766	0.000	0.000	0.000	0.000
130	A	132	ASN	0	0.026	0.018	21.387	-0.657	-0.657	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.022	-0.034	20.890	0.238	0.238	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.972	0.970	17.386	13.667	13.667	0.000	0.000	0.000	0.000
133	A	135	GLY	0	0.026	0.042	16.146	-1.060	-1.060	0.000	0.000	0.000	0.000
134	A	136	ILE	0	-0.013	-0.006	14.027	1.033	1.033	0.000	0.000	0.000	0.000
135	A	137	SER	0	-0.014	-0.019	14.889	-0.872	-0.872	0.000	0.000	0.000	0.000
136	A	138	GLY	0	0.033	0.026	13.416	-0.800	-0.800	0.000	0.000	0.000	0.000
137	A	139	LYS	1	0.943	0.976	14.469	13.625	13.625	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)