FMO DATABASE

FMODB ID: 98L32

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1180336.080262
FMO2-HF: Nuclear repulsion	1126415.559463
FMO2-HF: Total energy	-53920.520799
FMO2-MP2: Total energy	-54078.400863

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.
-237.436	-232.232	40.701	-20.861	-25.041	-0.255

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 : 0.801 / q_NPA : 0.884

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	0.050	0.022	2.957	2.815	5.067	0.283	-0.981	-1.554	-0.002
4	A	6	SER	0	-0.002	-0.018	5.645	0.530	0.530	0.000	0.000	0.000	0.000
5	A	7	SER	0	-0.038	-0.015	8.883	1.885	1.885	0.000	0.000	0.000	0.000
6	A	8	PHE	0	0.018	0.011	6.558	1.163	1.163	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.005	0.005	2.337	2.928	3.249	1.105	-0.380	-1.046	0.004
8	A	10	ALA	0	0.025	0.016	2.895	1.622	2.414	0.079	-0.203	-0.668	0.000
9	A	11	ALA	0	0.001	-0.008	2.270	-19.351	-17.622	4.131	-2.348	-3.512	-0.036
10	A	12	GLN	0	-0.025	-0.016	2.266	-11.767	-10.754	4.420	-2.047	-3.386	-0.024
11	A	13	ILE	0	-0.021	-0.009	3.388	7.765	7.996	0.008	0.359	-0.597	-0.001
12	A	14	ARG	1	0.821	0.901	4.892	25.934	25.980	-0.001	-0.001	-0.044	0.000
13	A	15	ILE	0	-0.018	-0.002	8.189	1.344	1.344	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.014	0.004	11.200	0.457	0.457	0.000	0.000	0.000	0.000
15	A	17	ARG	1	0.903	0.974	14.217	16.513	16.513	0.000	0.000	0.000	0.000
16	A	18	PRO	0	0.015	0.021	17.850	-0.149	-0.149	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.004	-0.046	21.153	0.157	0.157	0.000	0.000	0.000	0.000
18	A	20	GLY	0	0.013	0.016	23.621	0.175	0.175	0.000	0.000	0.000	0.000
19	A	21	GLN	0	-0.068	-0.046	25.803	0.796	0.796	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.045	0.017	20.578	-0.291	-0.291	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.889	-0.936	23.314	-12.225	-12.225	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.760	-0.853	25.425	-11.626	-11.626	0.000	0.000	0.000	0.000
23	A	25	ILE	0	-0.035	-0.006	19.973	-0.361	-0.361	0.000	0.000	0.000	0.000
24	A	26	ILE	0	-0.016	-0.017	20.823	-0.700	-0.700	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.811	0.911	21.761	10.691	10.691	0.000	0.000	0.000	0.000
26	A	28	PHE	0	0.041	0.011	19.902	-0.146	-0.146	0.000	0.000	0.000	0.000
27	A	29	TYR	0	-0.049	-0.068	16.678	-0.864	-0.864	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.838	-0.888	18.414	-16.708	-16.708	0.000	0.000	0.000	0.000
29	A	31	GLU	-1	-0.861	-0.944	20.295	-11.585	-11.585	0.000	0.000	0.000	0.000
30	A	32	GLY	0	0.024	-0.001	22.871	0.323	0.323	0.000	0.000	0.000	0.000
31	A	33	LEU	0	-0.056	-0.031	17.199	0.069	0.069	0.000	0.000	0.000	0.000
32	A	34	CYS	0	-0.129	-0.042	18.733	-0.140	-0.140	0.000	0.000	0.000	0.000
33	A	35	LEU	0	0.009	0.018	13.249	-0.827	-0.827	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.889	0.934	13.455	21.719	21.719	0.000	0.000	0.000	0.000
35	A	37	ARG	1	0.869	0.905	13.651	13.531	13.531	0.000	0.000	0.000	0.000
36	A	38	ILE	0	-0.126	-0.066	9.399	0.006	0.006	0.000	0.000	0.000	0.000
37	A	39	GLY	0	-0.013	-0.003	13.348	-0.244	-0.244	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.846	-0.918	15.468	-15.158	-15.158	0.000	0.000	0.000	0.000
39	A	41	PHE	0	-0.087	-0.035	17.289	-0.062	-0.062	0.000	0.000	0.000	0.000
40	A	42	SER	0	-0.003	-0.026	20.855	0.311	0.311	0.000	0.000	0.000	0.000
41	A	43	GLN	0	-0.028	-0.035	24.459	0.372	0.372	0.000	0.000	0.000	0.000
42	A	44	HIS	0	-0.008	0.013	20.186	0.720	0.720	0.000	0.000	0.000	0.000
43	A	45	ASN	0	-0.073	-0.050	22.805	0.169	0.169	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.085	0.052	26.045	0.062	0.062	0.000	0.000	0.000	0.000
45	A	47	TYR	0	-0.075	-0.034	22.572	0.114	0.114	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.766	-0.841	23.201	-12.509	-12.509	0.000	0.000	0.000	0.000
47	A	49	GLY	0	0.011	-0.015	19.339	-0.157	-0.157	0.000	0.000	0.000	0.000
48	A	50	VAL	0	-0.012	0.013	17.165	0.071	0.071	0.000	0.000	0.000	0.000
49	A	51	MET	0	-0.026	-0.009	11.862	-0.815	-0.815	0.000	0.000	0.000	0.000
50	A	52	PHE	0	0.026	0.014	12.658	0.351	0.351	0.000	0.000	0.000	0.000
51	A	53	GLY	0	-0.007	-0.007	9.219	-2.099	-2.099	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.016	0.014	8.271	2.805	2.805	0.000	0.000	0.000	0.000
53	A	55	PRO	0	-0.013	-0.013	8.028	-2.993	-2.993	0.000	0.000	0.000	0.000
54	A	56	HIS	0	0.022	-0.001	6.767	2.339	2.339	0.000	0.000	0.000	0.000
55	A	57	ALA	0	0.081	0.015	6.998	-1.435	-1.435	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.871	-0.909	1.671	-123.841	-127.533	19.542	-9.282	-6.567	-0.111
57	A	59	TYR	0	0.015	-0.007	1.857	-52.316	-49.881	11.135	-5.951	-7.618	-0.085
58	A	60	HIS	0	-0.024	0.015	4.461	9.298	9.375	-0.001	-0.027	-0.049	0.000
59	A	61	LEU	0	0.052	0.033	8.008	-0.137	-0.137	0.000	0.000	0.000	0.000
60	A	62	GLU	-1	-0.845	-0.940	11.502	-22.127	-22.127	0.000	0.000	0.000	0.000
61	A	63	PHE	0	0.035	0.019	13.866	0.377	0.377	0.000	0.000	0.000	0.000
62	A	64	THR	0	0.001	-0.006	17.666	0.287	0.287	0.000	0.000	0.000	0.000
63	A	65	GLN	0	0.042	0.009	20.317	0.015	0.015	0.000	0.000	0.000	0.000
64	A	66	TYR	0	-0.079	-0.044	24.140	0.076	0.076	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.824	-0.903	26.610	-10.338	-10.338	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.050	-0.018	29.882	0.349	0.349	0.000	0.000	0.000	0.000
67	A	69	GLY	0	-0.038	-0.011	31.215	0.217	0.217	0.000	0.000	0.000	0.000
68	A	70	SER	0	-0.039	-0.049	25.256	-0.337	-0.337	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.010	-0.007	26.665	0.396	0.396	0.000	0.000	0.000	0.000
70	A	72	ALA	0	0.021	0.026	23.546	-0.397	-0.397	0.000	0.000	0.000	0.000
71	A	73	PRO	0	-0.061	-0.036	20.369	0.406	0.406	0.000	0.000	0.000	0.000
72	A	74	VAL	0	-0.007	-0.004	23.658	0.146	0.146	0.000	0.000	0.000	0.000
73	A	75	PRO	0	0.013	0.011	25.468	-0.326	-0.326	0.000	0.000	0.000	0.000
74	A	76	HIS	0	-0.025	0.003	24.673	0.158	0.158	0.000	0.000	0.000	0.000
75	A	77	PRO	0	0.028	0.017	24.869	-0.566	-0.566	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.853	-0.943	24.454	-11.903	-11.903	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.081	-0.042	20.437	-0.857	-0.857	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.003	-0.006	19.624	-0.019	-0.019	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.040	-0.001	13.118	-1.214	-1.214	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.020	-0.007	15.945	0.733	0.733	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.015	0.015	14.215	-1.705	-1.705	0.000	0.000	0.000	0.000
82	A	84	TYR	0	-0.010	-0.016	15.261	1.054	1.054	0.000	0.000	0.000	0.000
83	A	85	VAL	0	0.008	0.005	17.227	-0.841	-0.841	0.000	0.000	0.000	0.000
84	A	86	PRO	0	-0.037	-0.018	19.068	0.834	0.834	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.036	-0.033	22.014	1.228	1.228	0.000	0.000	0.000	0.000
86	A	88	ALA	0	0.096	0.036	24.161	-0.168	-0.168	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.024	-0.009	26.891	0.174	0.174	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.875	-0.923	20.752	-14.774	-14.774	0.000	0.000	0.000	0.000
89	A	91	LEU	0	-0.009	0.007	23.259	-0.112	-0.112	0.000	0.000	0.000	0.000
90	A	92	ALA	0	0.025	0.022	24.388	0.080	0.080	0.000	0.000	0.000	0.000
91	A	93	ALA	0	-0.019	-0.003	25.831	0.221	0.221	0.000	0.000	0.000	0.000
92	A	94	ILE	0	-0.008	-0.005	20.928	0.169	0.169	0.000	0.000	0.000	0.000
93	A	95	THR	0	0.008	-0.015	24.383	0.258	0.258	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.012	-0.006	26.139	0.399	0.399	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.804	0.902	23.428	13.661	13.661	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.018	0.008	22.189	0.221	0.221	0.000	0.000	0.000	0.000
97	A	99	LYS	1	0.830	0.909	26.751	10.515	10.515	0.000	0.000	0.000	0.000
98	A	100	HIS	0	-0.068	-0.037	30.173	0.166	0.166	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.067	-0.012	25.663	0.126	0.126	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.026	0.026	30.245	0.061	0.061	0.000	0.000	0.000	0.000
101	A	103	TYR	0	-0.067	-0.058	26.137	0.007	0.007	0.000	0.000	0.000	0.000
102	A	104	GLN	0	-0.016	-0.019	28.830	0.353	0.353	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.805	-0.898	28.549	-10.801	-10.801	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.062	-0.027	27.923	0.384	0.384	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.841	-0.906	29.584	-10.198	-10.198	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.057	-0.021	27.256	-0.283	-0.283	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.806	-0.899	28.582	-10.154	-10.154	0.000	0.000	0.000	0.000
108	A	110	ASN	0	-0.008	-0.001	25.972	0.567	0.567	0.000	0.000	0.000	0.000
109	A	111	PRO	0	0.067	0.020	28.227	-0.319	-0.319	0.000	0.000	0.000	0.000
110	A	112	TYR	0	-0.069	-0.022	21.470	0.104	0.104	0.000	0.000	0.000	0.000
111	A	113	TRP	0	0.024	-0.013	19.648	-0.387	-0.387	0.000	0.000	0.000	0.000
112	A	114	SER	0	0.028	0.009	25.971	-0.148	-0.148	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.112	-0.057	29.060	0.452	0.452	0.000	0.000	0.000	0.000
114	A	116	GLY	0	-0.016	-0.013	27.550	-0.211	-0.211	0.000	0.000	0.000	0.000
115	A	117	GLY	0	-0.022	-0.027	25.183	-0.558	-0.558	0.000	0.000	0.000	0.000
116	A	118	VAL	0	0.001	0.020	25.065	0.471	0.471	0.000	0.000	0.000	0.000
117	A	119	THR	0	0.018	0.005	24.341	-0.879	-0.879	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.035	-0.021	24.022	0.562	0.562	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.824	-0.896	23.804	-11.787	-11.787	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.796	-0.879	20.726	-14.600	-14.600	0.000	0.000	0.000	0.000
121	A	123	PRO	0	0.006	-0.008	23.166	0.395	0.395	0.000	0.000	0.000	0.000
122	A	124	ASP	-1	-0.833	-0.877	22.938	-12.722	-12.722	0.000	0.000	0.000	0.000
123	A	125	GLY	0	0.001	-0.002	24.765	-0.061	-0.061	0.000	0.000	0.000	0.000
124	A	126	TRP	0	-0.083	-0.041	14.482	-0.542	-0.542	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.774	0.852	21.980	11.683	11.683	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.015	0.013	18.269	-0.794	-0.794	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.005	-0.006	19.743	0.770	0.770	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.005	0.003	19.647	-1.092	-1.092	0.000	0.000	0.000	0.000
129	A	131	MET	0	0.008	0.016	20.556	0.766	0.766	0.000	0.000	0.000	0.000
130	A	132	ASN	0	0.010	0.012	21.242	-0.596	-0.596	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.034	-0.035	20.420	0.234	0.234	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.952	0.958	16.989	14.072	14.072	0.000	0.000	0.000	0.000
133	A	135	GLY	0	0.040	0.048	15.501	-1.050	-1.050	0.000	0.000	0.000	0.000
134	A	136	ILE	0	-0.008	-0.013	14.394	1.152	1.152	0.000	0.000	0.000	0.000
135	A	137	SER	0	-0.018	-0.015	14.602	-0.967	-0.967	0.000	0.000	0.000	0.000
136	A	138	GLY	0	0.040	0.027	12.952	-0.456	-0.456	0.000	0.000	0.000	0.000
137	A	139	LYS	1	0.933	0.973	13.962	14.025	14.025	0.000	0.000	0.000	0.000

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