FMO DATABASE

FMODB ID: 8965Y

Calculation Name: 1MW5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1MW5

Chain ID: A

ChEMBL ID:

UniProt ID: P44209

Base Structure: X-ray

Registration Date: 2023-09-23

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	162
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1522310.935425
FMO2-HF: Nuclear repulsion	1458602.125184
FMO2-HF: Total energy	-63708.810241
FMO2-MP2: Total energy	-63898.0715

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:GLU)

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

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.
-60.732	-55.021	0.372	-2.438	-3.645	0.018

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.891 / q_NPA : -0.952

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	ASP	-1	-0.866	-0.927	2.827	32.090	35.542	0.222	-1.527	-2.147	0.011
4	A	6	LEU	0	-0.020	-0.008	3.085	-12.356	-10.490	0.150	-0.781	-1.235	0.007
5	A	7	LEU	0	0.043	0.014	4.305	-7.211	-6.818	0.000	-0.130	-0.263	0.000
6	A	8	MET	0	0.021	0.002	6.361	-4.619	-4.619	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.819	0.907	6.053	-43.274	-43.274	0.000	0.000	0.000	0.000
8	A	10	MET	0	-0.051	0.013	8.401	-2.551	-2.551	0.000	0.000	0.000	0.000
9	A	11	VAL	0	0.007	0.003	10.563	-1.732	-1.732	0.000	0.000	0.000	0.000
10	A	12	ARG	1	0.874	0.954	10.194	-24.844	-24.844	0.000	0.000	0.000	0.000
11	A	13	GLN	0	-0.058	-0.030	12.450	-1.753	-1.753	0.000	0.000	0.000	0.000
12	A	14	PRO	0	0.044	0.026	15.915	0.196	0.196	0.000	0.000	0.000	0.000
13	A	15	VAL	0	-0.028	-0.017	13.256	0.543	0.543	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.866	0.922	16.183	-14.066	-14.066	0.000	0.000	0.000	0.000
15	A	17	LEU	0	0.014	0.008	16.352	0.910	0.910	0.000	0.000	0.000	0.000
16	A	18	TYR	0	-0.065	-0.064	17.094	-0.669	-0.669	0.000	0.000	0.000	0.000
17	A	19	SER	0	0.043	0.028	18.146	0.384	0.384	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.078	0.015	18.157	0.171	0.171	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.046	0.024	20.182	-0.027	-0.027	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.014	0.000	21.292	-0.173	-0.173	0.000	0.000	0.000	0.000
21	A	23	LEU	0	0.030	0.024	15.976	-0.063	-0.063	0.000	0.000	0.000	0.000
22	A	24	PHE	0	0.037	0.012	20.176	-0.027	-0.027	0.000	0.000	0.000	0.000
23	A	25	HIS	0	-0.017	-0.003	22.352	-0.025	-0.025	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.742	-0.835	20.815	13.675	13.675	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.002	-0.014	16.859	-0.024	-0.024	0.000	0.000	0.000	0.000
26	A	28	SER	0	-0.036	-0.026	22.551	-0.367	-0.367	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.864	-0.919	25.941	9.888	9.888	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.013	-0.011	22.471	-0.294	-0.294	0.000	0.000	0.000	0.000
29	A	31	ILE	0	-0.006	0.002	23.204	-0.183	-0.183	0.000	0.000	0.000	0.000
30	A	32	THR	0	-0.002	-0.007	26.507	-0.337	-0.337	0.000	0.000	0.000	0.000
31	A	33	LYS	1	0.840	0.922	27.988	-10.882	-10.882	0.000	0.000	0.000	0.000
32	A	34	LEU	0	0.019	0.002	24.448	-0.190	-0.190	0.000	0.000	0.000	0.000
33	A	35	GLU	-1	-0.818	-0.916	29.069	10.182	10.182	0.000	0.000	0.000	0.000
34	A	36	HIS	0	-0.032	0.000	31.585	-0.455	-0.455	0.000	0.000	0.000	0.000
35	A	37	SER	0	-0.042	-0.054	31.512	-0.155	-0.155	0.000	0.000	0.000	0.000
36	A	38	VAL	0	-0.095	-0.032	31.969	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	39	GLN	0	0.001	0.009	34.226	-0.424	-0.424	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.931	0.961	37.192	-7.890	-7.890	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.785	-0.887	33.985	9.684	9.684	0.000	0.000	0.000	0.000
40	A	42	PRO	0	-0.071	-0.020	31.103	-0.130	-0.130	0.000	0.000	0.000	0.000
41	A	43	THR	0	0.020	0.002	33.772	-0.018	-0.018	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.021	0.014	32.465	0.046	0.046	0.000	0.000	0.000	0.000
43	A	45	LEU	0	-0.028	-0.032	27.424	0.074	0.074	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.048	-0.009	24.926	0.036	0.036	0.000	0.000	0.000	0.000
45	A	47	SER	0	0.110	0.071	23.489	0.206	0.206	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.766	-0.896	17.874	16.922	16.922	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.872	-0.899	19.078	14.235	14.235	0.000	0.000	0.000	0.000
48	A	50	ASN	0	0.014	-0.023	20.847	0.098	0.098	0.000	0.000	0.000	0.000
49	A	51	TRP	0	-0.004	-0.003	17.965	-0.052	-0.052	0.000	0.000	0.000	0.000
50	A	52	HIS	0	0.063	0.022	14.516	-0.986	-0.986	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.795	0.894	19.172	-13.378	-13.378	0.000	0.000	0.000	0.000
52	A	54	GLN	0	0.017	-0.005	21.627	-0.469	-0.469	0.000	0.000	0.000	0.000
53	A	55	PHE	0	0.039	0.013	16.974	-0.294	-0.294	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.002	0.016	17.557	0.044	0.044	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.919	0.962	20.166	-11.828	-11.828	0.000	0.000	0.000	0.000
56	A	58	PHE	0	0.003	0.003	21.781	-0.299	-0.299	0.000	0.000	0.000	0.000
57	A	59	ALA	0	0.038	0.002	19.266	-0.281	-0.281	0.000	0.000	0.000	0.000
58	A	60	GLN	0	-0.056	-0.036	21.111	0.290	0.290	0.000	0.000	0.000	0.000
59	A	61	ALA	0	-0.010	0.010	22.794	-0.384	-0.384	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.037	0.003	21.519	-0.419	-0.419	0.000	0.000	0.000	0.000
61	A	63	PRO	0	-0.004	-0.002	24.584	0.017	0.017	0.000	0.000	0.000	0.000
62	A	64	ALA	0	0.005	0.005	22.120	0.533	0.533	0.000	0.000	0.000	0.000
63	A	65	HIS	0	0.038	0.014	23.040	0.271	0.271	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.074	0.026	22.484	0.422	0.422	0.000	0.000	0.000	0.000
65	A	67	SER	0	-0.107	-0.042	23.030	0.158	0.158	0.000	0.000	0.000	0.000
66	A	68	ALA	0	0.030	0.015	25.179	-0.060	-0.060	0.000	0.000	0.000	0.000
67	A	69	SER	0	-0.023	-0.019	26.977	-0.107	-0.107	0.000	0.000	0.000	0.000
68	A	70	TRP	0	0.026	-0.005	29.807	0.103	0.103	0.000	0.000	0.000	0.000
69	A	71	LEU	0	0.065	0.029	31.486	0.143	0.143	0.000	0.000	0.000	0.000
70	A	72	ASN	0	0.026	0.039	28.605	0.131	0.131	0.000	0.000	0.000	0.000
71	A	73	LEU	0	0.012	0.006	24.975	0.292	0.292	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.810	-0.890	28.480	9.549	9.549	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.867	-0.945	31.298	9.279	9.279	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.033	-0.016	26.193	0.043	0.043	0.000	0.000	0.000	0.000
75	A	77	LEU	0	-0.037	-0.022	27.241	0.292	0.292	0.000	0.000	0.000	0.000
76	A	78	GLN	0	-0.040	-0.026	29.150	-0.079	-0.079	0.000	0.000	0.000	0.000
77	A	79	ALA	0	-0.017	0.012	27.535	-0.173	-0.173	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.054	-0.014	26.065	0.227	0.227	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.034	-0.020	28.581	-0.473	-0.473	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.063	0.013	31.093	0.096	0.096	0.000	0.000	0.000	0.000
81	A	83	ASN	0	-0.022	-0.011	33.701	-0.138	-0.138	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.001	-0.003	28.462	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.895	0.967	29.158	-9.353	-9.353	0.000	0.000	0.000	0.000
84	A	86	SER	0	0.073	0.043	29.780	0.331	0.331	0.000	0.000	0.000	0.000
85	A	87	ALA	0	0.038	0.015	28.963	0.121	0.121	0.000	0.000	0.000	0.000
86	A	88	PHE	0	0.002	0.002	22.090	0.299	0.299	0.000	0.000	0.000	0.000
87	A	89	LEU	0	0.047	0.022	25.493	0.478	0.478	0.000	0.000	0.000	0.000
88	A	90	HIS	1	0.819	0.891	27.046	-9.778	-9.778	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.018	-0.015	22.253	-0.275	-0.275	0.000	0.000	0.000	0.000
90	A	92	LEU	0	-0.034	-0.013	21.338	0.636	0.636	0.000	0.000	0.000	0.000
91	A	93	ILE	0	0.031	0.024	22.742	0.445	0.445	0.000	0.000	0.000	0.000
92	A	94	ALA	0	-0.016	0.002	24.604	0.159	0.159	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.796	0.885	18.073	-16.472	-16.472	0.000	0.000	0.000	0.000
94	A	96	LEU	0	0.004	0.003	19.217	0.626	0.626	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.886	0.920	21.167	-10.661	-10.661	0.000	0.000	0.000	0.000
96	A	98	SER	0	-0.034	-0.008	20.177	0.076	0.076	0.000	0.000	0.000	0.000
97	A	99	ARG	1	0.846	0.880	11.787	-23.015	-23.015	0.000	0.000	0.000	0.000
98	A	100	HIS	0	-0.025	0.006	18.512	0.181	0.181	0.000	0.000	0.000	0.000
99	A	101	LEU	0	-0.005	-0.011	21.136	-0.163	-0.163	0.000	0.000	0.000	0.000
100	A	102	GLN	0	-0.014	-0.009	15.681	0.954	0.954	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.012	0.021	17.071	0.340	0.340	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.010	-0.001	18.483	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.784	-0.872	17.582	13.987	13.987	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.019	-0.008	13.768	0.310	0.310	0.000	0.000	0.000	0.000
105	A	107	ASN	0	-0.061	-0.042	17.418	-0.218	-0.218	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.778	0.894	18.573	-14.210	-14.210	0.000	0.000	0.000	0.000
107	A	109	ILE	0	0.079	0.030	13.173	-0.280	-0.280	0.000	0.000	0.000	0.000
108	A	110	GLY	0	-0.028	-0.022	17.276	-0.180	-0.180	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.058	-0.045	18.944	-0.605	-0.605	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.977	-0.969	17.409	15.714	15.714	0.000	0.000	0.000	0.000
111	A	113	PRO	0	0.011	-0.001	20.542	0.341	0.341	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.001	-0.004	16.972	0.508	0.508	0.000	0.000	0.000	0.000
113	A	115	ASP	-1	-0.882	-0.926	21.159	11.007	11.007	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.060	-0.040	17.147	0.536	0.536	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.022	-0.040	21.547	-0.093	-0.093	0.000	0.000	0.000	0.000
116	A	118	ASN	0	-0.068	-0.036	24.247	-0.128	-0.128	0.000	0.000	0.000	0.000
117	A	119	LEU	0	0.011	0.023	25.055	-0.489	-0.489	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.065	0.038	24.210	0.431	0.431	0.000	0.000	0.000	0.000
119	A	121	ALA	0	-0.007	-0.008	19.542	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	122	PRO	0	-0.017	-0.007	20.287	0.499	0.499	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.015	0.023	14.103	0.528	0.528	0.000	0.000	0.000	0.000
122	A	124	TYR	0	-0.030	-0.022	16.262	-0.861	-0.861	0.000	0.000	0.000	0.000
123	A	125	VAL	0	0.026	0.014	12.938	1.041	1.041	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.019	-0.008	11.147	-1.029	-1.029	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.008	-0.027	11.654	1.642	1.642	0.000	0.000	0.000	0.000
126	A	128	PRO	0	0.024	0.016	12.393	-0.849	-0.849	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.784	-0.874	15.196	12.724	12.724	0.000	0.000	0.000	0.000
128	A	130	SER	0	0.014	0.015	18.329	-0.603	-0.603	0.000	0.000	0.000	0.000
129	A	131	PHE	0	0.078	0.023	18.317	0.848	0.848	0.000	0.000	0.000	0.000
130	A	132	ALA	0	0.024	0.023	19.236	0.611	0.611	0.000	0.000	0.000	0.000
131	A	133	ALA	0	-0.001	0.003	15.056	0.741	0.741	0.000	0.000	0.000	0.000
132	A	134	ARG	1	0.752	0.843	14.547	-13.434	-13.434	0.000	0.000	0.000	0.000
133	A	135	ILE	0	0.019	0.002	15.164	0.882	0.882	0.000	0.000	0.000	0.000
134	A	136	THR	0	-0.023	-0.025	13.427	0.231	0.231	0.000	0.000	0.000	0.000
135	A	137	LEU	0	-0.055	-0.011	8.311	0.828	0.828	0.000	0.000	0.000	0.000
136	A	138	LEU	0	0.018	0.006	11.798	1.253	1.253	0.000	0.000	0.000	0.000
137	A	139	VAL	0	-0.055	-0.009	14.012	-0.065	-0.065	0.000	0.000	0.000	0.000
138	A	140	GLN	0	-0.011	-0.018	12.651	0.054	0.054	0.000	0.000	0.000	0.000
139	A	141	ASP	-1	-0.853	-0.909	6.631	43.124	43.124	0.000	0.000	0.000	0.000
140	A	142	LYS	1	0.911	0.955	6.423	-36.425	-36.425	0.000	0.000	0.000	0.000
141	A	143	ALA	0	-0.012	0.001	5.028	-0.624	-0.624	0.000	0.000	0.000	0.000
142	A	144	LEU	0	0.002	0.003	7.082	-1.529	-1.529	0.000	0.000	0.000	0.000
143	A	145	PRO	0	0.007	0.004	7.075	0.327	0.327	0.000	0.000	0.000	0.000
144	A	146	TYR	0	-0.010	-0.012	8.546	-2.385	-2.385	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.003	0.001	10.969	0.986	0.986	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.867	0.944	13.632	-15.914	-15.914	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.018	-0.022	16.425	0.199	0.199	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.033	0.006	19.226	-0.539	-0.539	0.000	0.000	0.000	0.000
149	A	151	MET	0	-0.076	-0.029	21.872	-0.016	-0.016	0.000	0.000	0.000	0.000
150	A	152	GLU	-1	-0.794	-0.868	23.644	11.296	11.296	0.000	0.000	0.000	0.000
151	A	153	TYR	0	-0.033	-0.015	26.070	-0.270	-0.270	0.000	0.000	0.000	0.000
152	A	154	TRP	0	0.061	0.005	27.911	0.058	0.058	0.000	0.000	0.000	0.000
153	A	155	HIS	0	0.033	0.022	31.018	0.007	0.007	0.000	0.000	0.000	0.000
154	A	156	ALA	0	0.006	-0.003	29.531	-0.172	-0.172	0.000	0.000	0.000	0.000
155	A	157	LEU	0	-0.056	-0.023	26.271	0.175	0.175	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.931	-0.948	30.205	8.142	8.142	0.000	0.000	0.000	0.000
157	A	159	TYR	0	-0.009	-0.014	33.339	0.051	0.051	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.891	0.939	33.610	-8.652	-8.652	0.000	0.000	0.000	0.000
159	A	161	GLY	0	-0.015	0.007	36.048	-0.139	-0.139	0.000	0.000	0.000	0.000
160	A	162	GLU	-1	-0.954	-0.988	36.086	7.585	7.585	0.000	0.000	0.000	0.000
161	A	163	LEU	0	-0.049	-0.016	36.903	0.084	0.084	0.000	0.000	0.000	0.000
162	A	164	ASN	0	-0.013	0.005	32.091	0.246	0.246	0.000	0.000	0.000	0.000

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