FMO DATABASE

FMODB ID: G5461

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1522878.995889
FMO2-HF: Nuclear repulsion	1459171.075506
FMO2-HF: Total energy	-63707.920383
FMO2-MP2: Total energy	-63897.234674

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.
-56.436	-50.534	0.338	-2.56	-3.68	0.019

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 : -0.887 / q_NPA : -0.946

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	-0.901	-0.939	2.937	30.859	34.426	0.212	-1.588	-2.191	0.011
4	A	6	LEU	0	-0.003	-0.006	3.157	-13.170	-11.285	0.126	-0.805	-1.205	0.008
5	A	7	LEU	0	0.024	-0.001	4.194	-7.767	-7.317	0.000	-0.167	-0.284	0.000
6	A	8	MET	0	0.022	0.009	6.399	-4.720	-4.720	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.890	0.942	7.209	-35.757	-35.757	0.000	0.000	0.000	0.000
8	A	10	MET	0	-0.056	0.010	8.500	-2.682	-2.682	0.000	0.000	0.000	0.000
9	A	11	VAL	0	0.024	0.016	10.403	-1.730	-1.730	0.000	0.000	0.000	0.000
10	A	12	ARG	1	0.887	0.954	10.546	-24.653	-24.653	0.000	0.000	0.000	0.000
11	A	13	GLN	0	-0.069	-0.041	12.539	-1.713	-1.713	0.000	0.000	0.000	0.000
12	A	14	PRO	0	0.040	0.024	15.968	0.241	0.241	0.000	0.000	0.000	0.000
13	A	15	VAL	0	-0.022	-0.009	13.293	0.553	0.553	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.942	0.968	16.240	-14.102	-14.102	0.000	0.000	0.000	0.000
15	A	17	LEU	0	0.005	0.003	16.481	0.909	0.909	0.000	0.000	0.000	0.000
16	A	18	TYR	0	-0.035	-0.043	17.132	-0.683	-0.683	0.000	0.000	0.000	0.000
17	A	19	SER	0	0.050	0.041	18.153	0.540	0.540	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.083	0.025	18.212	0.154	0.154	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.032	0.014	20.184	-0.043	-0.043	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.047	-0.030	21.550	-0.069	-0.069	0.000	0.000	0.000	0.000
21	A	23	LEU	0	0.058	0.036	15.987	-0.079	-0.079	0.000	0.000	0.000	0.000
22	A	24	PHE	0	0.034	0.011	20.200	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	25	HIS	0	0.011	0.000	22.371	0.043	0.043	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.734	-0.817	20.390	13.769	13.769	0.000	0.000	0.000	0.000
25	A	27	PHE	0	-0.015	-0.024	16.943	0.016	0.016	0.000	0.000	0.000	0.000
26	A	28	SER	0	-0.032	-0.017	22.589	-0.346	-0.346	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.945	-0.972	26.155	9.786	9.786	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.036	-0.018	22.433	-0.269	-0.269	0.000	0.000	0.000	0.000
29	A	31	ILE	0	-0.014	-0.006	23.119	-0.161	-0.161	0.000	0.000	0.000	0.000
30	A	32	THR	0	0.019	0.014	26.554	-0.328	-0.328	0.000	0.000	0.000	0.000
31	A	33	LYS	1	0.872	0.941	28.012	-10.869	-10.869	0.000	0.000	0.000	0.000
32	A	34	LEU	0	0.008	-0.008	24.520	-0.185	-0.185	0.000	0.000	0.000	0.000
33	A	35	GLU	-1	-0.872	-0.955	29.128	9.987	9.987	0.000	0.000	0.000	0.000
34	A	36	HIS	0	-0.026	-0.003	31.638	-0.456	-0.456	0.000	0.000	0.000	0.000
35	A	37	SER	0	-0.041	-0.037	31.525	-0.161	-0.161	0.000	0.000	0.000	0.000
36	A	38	VAL	0	-0.094	-0.033	31.939	0.009	0.009	0.000	0.000	0.000	0.000
37	A	39	GLN	0	0.006	0.012	34.219	-0.444	-0.444	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.933	0.958	37.190	-7.884	-7.884	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.856	-0.938	34.742	9.413	9.413	0.000	0.000	0.000	0.000
40	A	42	PRO	0	-0.111	-0.031	31.166	-0.113	-0.113	0.000	0.000	0.000	0.000
41	A	43	THR	0	0.025	0.006	33.766	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.021	0.012	32.793	0.044	0.044	0.000	0.000	0.000	0.000
43	A	45	LEU	0	-0.003	-0.027	27.223	0.071	0.071	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.074	-0.017	24.888	0.024	0.024	0.000	0.000	0.000	0.000
45	A	47	SER	0	0.094	0.062	23.914	0.234	0.234	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.768	-0.912	18.209	16.665	16.665	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.911	-0.940	19.189	14.411	14.411	0.000	0.000	0.000	0.000
48	A	50	ASN	0	0.011	-0.038	21.013	0.243	0.243	0.000	0.000	0.000	0.000
49	A	51	TRP	0	-0.052	-0.026	17.880	-0.140	-0.140	0.000	0.000	0.000	0.000
50	A	52	HIS	0	0.068	0.023	14.993	-0.880	-0.880	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.862	0.957	19.162	-13.476	-13.476	0.000	0.000	0.000	0.000
52	A	54	GLN	0	0.016	0.002	21.616	-0.488	-0.488	0.000	0.000	0.000	0.000
53	A	55	PHE	0	0.050	0.017	16.865	-0.268	-0.268	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.006	0.017	17.504	0.059	0.059	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.915	0.957	20.154	-11.935	-11.935	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.001	0.009	21.740	-0.289	-0.289	0.000	0.000	0.000	0.000
57	A	59	ALA	0	0.040	-0.003	19.281	-0.274	-0.274	0.000	0.000	0.000	0.000
58	A	60	GLN	0	-0.060	-0.038	21.173	0.287	0.287	0.000	0.000	0.000	0.000
59	A	61	ALA	0	-0.008	0.013	22.794	-0.365	-0.365	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.047	0.003	21.427	-0.410	-0.410	0.000	0.000	0.000	0.000
61	A	63	PRO	0	0.006	0.003	24.584	0.015	0.015	0.000	0.000	0.000	0.000
62	A	64	ALA	0	0.004	0.007	22.204	0.531	0.531	0.000	0.000	0.000	0.000
63	A	65	HIS	0	0.038	0.014	23.112	0.227	0.227	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.077	0.025	22.548	0.423	0.423	0.000	0.000	0.000	0.000
65	A	67	SER	0	-0.096	-0.036	23.089	0.142	0.142	0.000	0.000	0.000	0.000
66	A	68	ALA	0	0.050	0.033	25.241	-0.058	-0.058	0.000	0.000	0.000	0.000
67	A	69	SER	0	-0.006	-0.001	27.043	-0.072	-0.072	0.000	0.000	0.000	0.000
68	A	70	TRP	0	0.039	0.006	29.874	0.139	0.139	0.000	0.000	0.000	0.000
69	A	71	LEU	0	0.087	0.036	31.554	0.142	0.142	0.000	0.000	0.000	0.000
70	A	72	ASN	0	0.000	0.017	28.490	0.190	0.190	0.000	0.000	0.000	0.000
71	A	73	LEU	0	0.005	0.001	25.067	0.290	0.290	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.840	-0.917	28.551	9.467	9.467	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.844	-0.931	31.442	9.224	9.224	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.037	-0.016	26.150	0.048	0.048	0.000	0.000	0.000	0.000
75	A	77	LEU	0	-0.044	-0.027	27.229	0.279	0.279	0.000	0.000	0.000	0.000
76	A	78	GLN	0	-0.054	-0.040	29.139	-0.107	-0.107	0.000	0.000	0.000	0.000
77	A	79	ALA	0	-0.017	0.013	27.491	-0.171	-0.171	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.058	-0.015	26.032	0.218	0.218	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.049	-0.031	28.570	-0.463	-0.463	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.068	0.008	31.082	0.089	0.089	0.000	0.000	0.000	0.000
81	A	83	ASN	0	0.010	0.003	33.793	-0.184	-0.184	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.039	-0.021	28.510	0.022	0.022	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.930	0.992	29.149	-9.317	-9.317	0.000	0.000	0.000	0.000
84	A	86	SER	0	0.069	0.040	29.771	0.330	0.330	0.000	0.000	0.000	0.000
85	A	87	ALA	0	0.072	0.036	28.688	0.112	0.112	0.000	0.000	0.000	0.000
86	A	88	PHE	0	0.003	0.008	22.148	0.299	0.299	0.000	0.000	0.000	0.000
87	A	89	LEU	0	0.046	0.019	25.485	0.463	0.463	0.000	0.000	0.000	0.000
88	A	90	HIS	1	0.866	0.917	27.039	-9.782	-9.782	0.000	0.000	0.000	0.000
89	A	91	GLN	0	0.006	0.011	21.893	-0.346	-0.346	0.000	0.000	0.000	0.000
90	A	92	LEU	0	-0.034	-0.019	21.081	0.628	0.628	0.000	0.000	0.000	0.000
91	A	93	ILE	0	0.038	0.030	22.737	0.429	0.429	0.000	0.000	0.000	0.000
92	A	94	ALA	0	-0.012	0.000	24.640	0.155	0.155	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.826	0.911	17.677	-16.496	-16.496	0.000	0.000	0.000	0.000
94	A	96	LEU	0	0.002	0.003	19.378	0.611	0.611	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.945	0.965	21.209	-10.551	-10.551	0.000	0.000	0.000	0.000
96	A	98	SER	0	-0.041	-0.009	20.439	0.070	0.070	0.000	0.000	0.000	0.000
97	A	99	ARG	1	0.860	0.890	11.864	-22.500	-22.500	0.000	0.000	0.000	0.000
98	A	100	HIS	0	-0.032	0.003	18.571	0.193	0.193	0.000	0.000	0.000	0.000
99	A	101	LEU	0	-0.010	-0.014	21.158	-0.154	-0.154	0.000	0.000	0.000	0.000
100	A	102	GLN	0	0.002	-0.004	15.869	1.001	1.001	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.002	0.022	17.220	0.329	0.329	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.019	-0.011	18.488	-0.020	-0.020	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.860	-0.937	17.553	13.967	13.967	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.039	-0.021	13.628	0.298	0.298	0.000	0.000	0.000	0.000
105	A	107	ASN	0	-0.043	-0.031	17.473	-0.110	-0.110	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.859	0.947	18.621	-14.052	-14.052	0.000	0.000	0.000	0.000
107	A	109	ILE	0	0.082	0.031	13.756	-0.309	-0.309	0.000	0.000	0.000	0.000
108	A	110	GLY	0	-0.022	-0.018	17.406	-0.162	-0.162	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.048	-0.027	18.911	-0.603	-0.603	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.995	-0.977	17.925	15.398	15.398	0.000	0.000	0.000	0.000
111	A	113	PRO	0	-0.014	-0.017	20.684	0.314	0.314	0.000	0.000	0.000	0.000
112	A	114	LEU	0	0.011	0.004	17.139	0.469	0.469	0.000	0.000	0.000	0.000
113	A	115	ASP	-1	-0.870	-0.916	21.259	10.917	10.917	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.066	-0.050	17.214	0.539	0.539	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.025	-0.042	21.584	-0.091	-0.091	0.000	0.000	0.000	0.000
116	A	118	ASN	0	-0.066	-0.035	24.258	-0.172	-0.172	0.000	0.000	0.000	0.000
117	A	119	LEU	0	0.004	0.017	25.100	-0.474	-0.474	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.068	0.045	24.273	0.439	0.439	0.000	0.000	0.000	0.000
119	A	121	ALA	0	-0.006	-0.008	19.603	0.000	0.000	0.000	0.000	0.000	0.000
120	A	122	PRO	0	-0.033	-0.009	20.390	0.493	0.493	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.027	0.024	13.972	0.496	0.496	0.000	0.000	0.000	0.000
122	A	124	TYR	0	-0.022	-0.019	16.241	-0.917	-0.917	0.000	0.000	0.000	0.000
123	A	125	VAL	0	0.014	0.014	12.786	0.995	0.995	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.015	-0.007	11.014	-1.038	-1.038	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.004	-0.034	11.687	1.658	1.658	0.000	0.000	0.000	0.000
126	A	128	PRO	0	0.021	0.015	12.539	-0.814	-0.814	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.861	-0.926	15.256	12.774	12.774	0.000	0.000	0.000	0.000
128	A	130	SER	0	0.000	0.004	18.399	-0.636	-0.636	0.000	0.000	0.000	0.000
129	A	131	PHE	0	0.075	0.024	18.387	0.830	0.830	0.000	0.000	0.000	0.000
130	A	132	ALA	0	0.027	0.025	19.307	0.602	0.602	0.000	0.000	0.000	0.000
131	A	133	ALA	0	-0.005	0.007	15.044	0.749	0.749	0.000	0.000	0.000	0.000
132	A	134	ARG	1	0.780	0.850	14.622	-13.378	-13.378	0.000	0.000	0.000	0.000
133	A	135	ILE	0	0.012	0.005	15.227	0.847	0.847	0.000	0.000	0.000	0.000
134	A	136	THR	0	-0.031	-0.039	13.361	0.205	0.205	0.000	0.000	0.000	0.000
135	A	137	LEU	0	-0.050	-0.011	8.483	0.833	0.833	0.000	0.000	0.000	0.000
136	A	138	LEU	0	0.023	0.008	11.858	1.205	1.205	0.000	0.000	0.000	0.000
137	A	139	VAL	0	-0.051	-0.002	14.065	-0.062	-0.062	0.000	0.000	0.000	0.000
138	A	140	GLN	0	-0.021	-0.025	12.494	-0.287	-0.287	0.000	0.000	0.000	0.000
139	A	141	ASP	-1	-0.875	-0.922	6.668	41.654	41.654	0.000	0.000	0.000	0.000
140	A	142	LYS	1	0.908	0.953	6.672	-35.087	-35.087	0.000	0.000	0.000	0.000
141	A	143	ALA	0	-0.010	0.005	5.075	-0.659	-0.659	0.000	0.000	0.000	0.000
142	A	144	LEU	0	0.015	0.009	7.102	-1.415	-1.415	0.000	0.000	0.000	0.000
143	A	145	PRO	0	-0.031	-0.005	7.168	0.160	0.160	0.000	0.000	0.000	0.000
144	A	146	TYR	0	0.018	-0.007	8.556	-2.335	-2.335	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.010	0.006	10.952	0.986	0.986	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.881	0.952	13.614	-15.843	-15.843	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.018	-0.026	16.509	0.194	0.194	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.034	0.008	19.285	-0.542	-0.542	0.000	0.000	0.000	0.000
149	A	151	MET	0	-0.064	-0.028	21.907	0.012	0.012	0.000	0.000	0.000	0.000
150	A	152	GLU	-1	-0.808	-0.867	23.727	11.155	11.155	0.000	0.000	0.000	0.000
151	A	153	TYR	0	-0.030	-0.016	26.051	-0.144	-0.144	0.000	0.000	0.000	0.000
152	A	154	TRP	0	0.064	0.006	28.006	0.047	0.047	0.000	0.000	0.000	0.000
153	A	155	HIS	0	0.063	0.035	30.971	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	156	ALA	0	0.005	-0.001	29.442	-0.187	-0.187	0.000	0.000	0.000	0.000
155	A	157	LEU	0	-0.062	-0.028	26.273	0.171	0.171	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.980	-0.978	30.137	8.149	8.149	0.000	0.000	0.000	0.000
157	A	159	TYR	0	-0.006	-0.013	33.261	0.050	0.050	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.910	0.956	33.323	-8.769	-8.769	0.000	0.000	0.000	0.000
159	A	161	GLY	0	-0.013	0.005	35.971	-0.140	-0.140	0.000	0.000	0.000	0.000
160	A	162	GLU	-1	-0.949	-0.982	35.993	7.630	7.630	0.000	0.000	0.000	0.000
161	A	163	LEU	0	-0.049	-0.017	36.805	0.083	0.083	0.000	0.000	0.000	0.000
162	A	164	ASN	0	-0.017	0.002	31.690	0.245	0.245	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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