FMO DATABASE

FMODB ID: N132Q

Calculation Name: 4L1N-A-Xray322

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4L1N

Chain ID: A

ChEMBL ID:

UniProt ID: A0PXY7

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	162
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1642330.532264
FMO2-HF: Nuclear repulsion	1578086.418998
FMO2-HF: Total energy	-64244.113267
FMO2-MP2: Total energy	-64433.256216

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:79:ACE )

Summations of interaction energy for fragment #1(A:79:ACE )

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.
2.667	3.467	-0.007	-0.376	-0.417	0

Interaction energy analysis for fragmet #1(A:79:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.014

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].
3	A	81	ASN	0	-0.068	-0.020	3.819	1.271	2.071	-0.007	-0.376	-0.417
4	A	82	SER	0	-0.059	-0.060	6.648	0.448	0.448	0.000	0.000	0.000
5	A	83	LYS	1	0.950	0.964	8.023	0.296	0.296	0.000	0.000	0.000
6	A	84	LYS	1	0.865	0.921	10.736	0.111	0.111	0.000	0.000	0.000
7	A	85	MET	0	-0.015	0.008	12.828	0.030	0.030	0.000	0.000	0.000
8	A	86	PHE	0	0.038	0.025	16.027	0.024	0.024	0.000	0.000	0.000
9	A	87	LEU	0	-0.009	-0.004	16.875	-0.006	-0.006	0.000	0.000	0.000
10	A	88	LYS	1	0.857	0.921	18.931	0.096	0.096	0.000	0.000	0.000
11	A	89	LYS	1	0.910	0.961	20.569	0.061	0.061	0.000	0.000	0.000
12	A	90	GLU	-1	-0.919	-0.967	24.043	-0.054	-0.054	0.000	0.000	0.000
13	A	91	LEU	0	-0.027	0.001	26.237	0.005	0.005	0.000	0.000	0.000
14	A	92	GLY	0	0.032	0.024	29.756	0.001	0.001	0.000	0.000	0.000
15	A	93	LYS	1	0.954	0.967	32.832	0.043	0.043	0.000	0.000	0.000
16	A	94	ASN	0	-0.023	-0.004	34.650	-0.004	-0.004	0.000	0.000	0.000
17	A	95	SER	0	-0.013	0.001	33.009	-0.001	-0.001	0.000	0.000	0.000
18	A	96	LYS	1	0.949	0.936	34.567	0.041	0.041	0.000	0.000	0.000
19	A	97	PRO	0	0.011	0.031	32.965	0.002	0.002	0.000	0.000	0.000
20	A	98	THR	0	-0.078	-0.035	34.884	0.003	0.003	0.000	0.000	0.000
21	A	99	PHE	0	0.016	0.004	36.372	0.002	0.002	0.000	0.000	0.000
22	A	100	ALA	0	0.025	0.017	32.879	-0.003	-0.003	0.000	0.000	0.000
23	A	101	THR	0	-0.008	0.019	30.941	0.002	0.002	0.000	0.000	0.000
24	A	102	LYS	1	0.963	0.969	33.796	0.061	0.061	0.000	0.000	0.000
25	A	103	TRP	0	-0.024	-0.016	28.855	-0.003	-0.003	0.000	0.000	0.000
26	A	104	LYS	1	0.962	1.000	28.899	0.113	0.113	0.000	0.000	0.000
27	A	105	ASN	0	-0.022	-0.029	28.764	-0.003	-0.003	0.000	0.000	0.000
28	A	106	SER	0	-0.003	0.011	25.085	-0.009	-0.009	0.000	0.000	0.000
29	A	107	SER	0	0.013	0.002	25.392	0.012	0.012	0.000	0.000	0.000
30	A	108	ASN	0	0.060	0.032	24.283	0.013	0.013	0.000	0.000	0.000
31	A	109	ASN	0	-0.009	-0.001	27.930	0.008	0.008	0.000	0.000	0.000
32	A	110	LYS	1	0.890	0.957	24.015	0.121	0.121	0.000	0.000	0.000
33	A	111	PHE	0	0.039	0.014	22.195	0.008	0.008	0.000	0.000	0.000
34	A	112	SER	0	0.003	-0.007	26.786	0.002	0.002	0.000	0.000	0.000
35	A	113	ALA	0	0.044	0.023	25.285	-0.001	-0.001	0.000	0.000	0.000
36	A	114	CYS	0	-0.051	-0.006	27.363	0.006	0.006	0.000	0.000	0.000
37	A	115	ILE	0	0.034	0.020	27.123	-0.005	-0.005	0.000	0.000	0.000
38	A	116	GLU	-1	-0.758	-0.897	29.415	-0.050	-0.050	0.000	0.000	0.000
39	A	117	GLY	0	-0.001	-0.008	31.009	-0.002	-0.002	0.000	0.000	0.000
40	A	118	LYS	1	0.821	0.907	30.548	0.070	0.070	0.000	0.000	0.000
41	A	119	GLY	0	0.053	0.037	34.598	0.001	0.001	0.000	0.000	0.000
42	A	120	GLU	-1	-0.965	-1.000	35.510	-0.058	-0.058	0.000	0.000	0.000
43	A	121	ASN	0	-0.041	-0.032	35.522	-0.006	-0.006	0.000	0.000	0.000
44	A	122	ALA	0	0.008	0.004	31.671	-0.003	-0.003	0.000	0.000	0.000
45	A	123	LEU	0	-0.008	-0.018	33.521	-0.002	-0.002	0.000	0.000	0.000
46	A	124	GLU	-1	-0.929	-0.937	36.302	-0.043	-0.043	0.000	0.000	0.000
47	A	125	GLU	-1	-0.865	-0.928	34.991	-0.046	-0.046	0.000	0.000	0.000
48	A	126	GLY	0	0.037	0.027	33.473	0.002	0.002	0.000	0.000	0.000
49	A	127	VAL	0	-0.095	-0.052	27.162	-0.005	-0.005	0.000	0.000	0.000
50	A	128	GLY	0	0.005	0.011	29.093	0.003	0.003	0.000	0.000	0.000
51	A	129	LYS	1	0.893	0.946	26.271	0.051	0.051	0.000	0.000	0.000
52	A	130	ILE	0	-0.016	0.001	21.755	0.000	0.000	0.000	0.000	0.000
53	A	131	TYR	0	0.012	-0.003	24.956	0.003	0.003	0.000	0.000	0.000
54	A	132	ILE	0	-0.007	-0.001	21.827	-0.006	-0.006	0.000	0.000	0.000
55	A	133	LYS	1	0.906	0.954	25.870	0.082	0.082	0.000	0.000	0.000
56	A	134	ASN	0	0.020	0.008	24.932	-0.005	-0.005	0.000	0.000	0.000
57	A	135	LEU	0	-0.026	-0.030	27.519	0.009	0.009	0.000	0.000	0.000
58	A	136	LYS	1	0.858	0.949	29.034	0.087	0.087	0.000	0.000	0.000
59	A	137	GLU	-1	-0.894	-0.948	27.206	-0.058	-0.058	0.000	0.000	0.000
60	A	138	GLN	0	-0.021	-0.012	30.361	0.002	0.002	0.000	0.000	0.000
61	A	139	SER	0	-0.030	-0.010	27.184	0.006	0.006	0.000	0.000	0.000
62	A	140	LYS	1	0.848	0.915	28.267	0.046	0.046	0.000	0.000	0.000
63	A	141	TRP	0	-0.005	-0.005	21.055	0.015	0.015	0.000	0.000	0.000
64	A	142	GLU	-1	-0.825	-0.915	25.086	-0.065	-0.065	0.000	0.000	0.000
65	A	143	LEU	0	-0.049	-0.018	18.853	-0.002	-0.002	0.000	0.000	0.000
66	A	144	ASP	-1	-0.816	-0.928	21.941	-0.071	-0.071	0.000	0.000	0.000
67	A	145	LEU	0	-0.054	-0.028	20.043	-0.008	-0.008	0.000	0.000	0.000
68	A	146	ASP	-1	-0.921	-0.955	18.302	-0.036	-0.036	0.000	0.000	0.000
69	A	147	GLN	0	-0.014	-0.025	20.441	-0.007	-0.007	0.000	0.000	0.000
70	A	148	ASP	-1	-0.892	-0.934	23.110	-0.015	-0.015	0.000	0.000	0.000
71	A	149	GLN	0	-0.055	-0.027	25.746	0.001	0.001	0.000	0.000	0.000
72	A	150	GLN	0	0.044	0.022	27.099	-0.008	-0.008	0.000	0.000	0.000
73	A	151	LYS	1	0.959	0.978	26.061	0.048	0.048	0.000	0.000	0.000
74	A	152	ASN	0	-0.021	-0.003	24.006	-0.001	-0.001	0.000	0.000	0.000
75	A	153	THR	0	0.075	0.032	26.215	0.006	0.006	0.000	0.000	0.000
76	A	154	PRO	0	-0.042	0.007	23.908	-0.008	-0.008	0.000	0.000	0.000
77	A	155	LYS	1	0.898	0.961	25.344	0.085	0.085	0.000	0.000	0.000
78	A	156	TYR	0	0.041	0.003	26.351	0.010	0.010	0.000	0.000	0.000
79	A	157	ILE	0	-0.019	-0.005	23.957	-0.013	-0.013	0.000	0.000	0.000
80	A	158	ASP	-1	-0.835	-0.932	24.279	-0.119	-0.119	0.000	0.000	0.000
81	A	159	TRP	0	-0.041	-0.019	21.717	-0.020	-0.020	0.000	0.000	0.000
82	A	160	PHE	0	0.001	0.007	16.476	0.002	0.002	0.000	0.000	0.000
83	A	161	ASP	-1	-0.803	-0.910	17.014	-0.344	-0.344	0.000	0.000	0.000
84	A	162	ASP	-1	-0.878	-0.937	20.596	-0.156	-0.156	0.000	0.000	0.000
85	A	163	ASN	0	-0.061	-0.036	16.926	0.037	0.037	0.000	0.000	0.000
86	A	164	ASN	0	-0.053	-0.051	14.653	-0.052	-0.052	0.000	0.000	0.000
87	A	165	LEU	0	0.021	0.014	17.934	0.025	0.025	0.000	0.000	0.000
88	A	166	MET	0	-0.029	-0.009	18.790	-0.041	-0.041	0.000	0.000	0.000
89	A	167	VAL	0	-0.012	-0.024	20.180	0.025	0.025	0.000	0.000	0.000
90	A	168	VAL	0	0.023	0.023	21.263	-0.014	-0.014	0.000	0.000	0.000
91	A	169	ILE	0	-0.026	-0.002	19.986	0.010	0.010	0.000	0.000	0.000
92	A	170	SER	0	0.044	0.026	23.746	-0.001	-0.001	0.000	0.000	0.000
93	A	171	ARG	1	0.932	0.954	26.081	0.067	0.067	0.000	0.000	0.000
94	A	172	ALA	0	-0.021	-0.034	29.201	-0.002	-0.002	0.000	0.000	0.000
95	A	173	HIS	0	-0.032	-0.011	30.848	0.002	0.002	0.000	0.000	0.000
96	A	174	GLY	0	-0.001	0.006	33.892	-0.002	-0.002	0.000	0.000	0.000
97	A	175	THR	0	0.018	-0.002	36.168	-0.003	-0.003	0.000	0.000	0.000
98	A	176	VAL	0	0.062	0.046	34.094	-0.002	-0.002	0.000	0.000	0.000
99	A	177	SER	0	-0.034	-0.012	31.339	-0.003	-0.003	0.000	0.000	0.000
100	A	178	GLN	0	-0.009	-0.016	32.077	-0.005	-0.005	0.000	0.000	0.000
101	A	179	GLY	0	0.030	0.001	28.767	-0.005	-0.005	0.000	0.000	0.000
102	A	180	GLY	0	-0.067	-0.038	25.791	0.007	0.007	0.000	0.000	0.000
103	A	181	ILE	0	-0.036	0.004	19.542	-0.003	-0.003	0.000	0.000	0.000
104	A	182	LEU	0	0.026	0.024	20.648	0.001	0.001	0.000	0.000	0.000
105	A	183	TYR	0	0.045	-0.001	15.690	-0.016	-0.016	0.000	0.000	0.000
106	A	184	LYS	1	0.954	0.993	12.409	0.637	0.637	0.000	0.000	0.000
107	A	185	VAL	0	-0.007	-0.017	14.513	-0.053	-0.053	0.000	0.000	0.000
108	A	186	ASN	0	0.055	0.032	12.414	0.089	0.089	0.000	0.000	0.000
109	A	187	ILE	0	-0.018	-0.015	15.269	0.031	0.031	0.000	0.000	0.000
110	A	188	GLU	-1	-0.843	-0.886	16.214	-0.096	-0.096	0.000	0.000	0.000
111	A	189	THR	0	0.047	0.005	11.751	0.019	0.019	0.000	0.000	0.000
112	A	190	GLY	0	0.017	0.022	14.372	0.027	0.027	0.000	0.000	0.000
113	A	191	GLN	0	-0.032	-0.017	7.799	0.122	0.122	0.000	0.000	0.000
114	A	192	ALA	0	0.015	0.001	12.009	-0.016	-0.016	0.000	0.000	0.000
115	A	193	THR	0	0.027	0.001	9.433	-0.045	-0.045	0.000	0.000	0.000
116	A	194	GLU	-1	-0.946	-0.966	12.431	-0.183	-0.183	0.000	0.000	0.000
117	A	195	LEU	0	-0.075	-0.035	14.892	-0.042	-0.042	0.000	0.000	0.000
118	A	196	TYR	0	0.023	-0.003	17.498	0.016	0.016	0.000	0.000	0.000
119	A	197	ASN	0	0.011	0.015	18.731	0.031	0.031	0.000	0.000	0.000
120	A	198	THR	0	-0.025	-0.032	21.018	-0.002	-0.002	0.000	0.000	0.000
121	A	199	LYS	1	0.882	0.940	17.831	0.144	0.144	0.000	0.000	0.000
122	A	200	ASP	-1	-0.805	-0.907	23.780	-0.058	-0.058	0.000	0.000	0.000
123	A	201	ASN	0	-0.051	-0.024	27.578	-0.005	-0.005	0.000	0.000	0.000
124	A	202	LYS	1	0.926	0.970	29.134	0.051	0.051	0.000	0.000	0.000
125	A	203	LYS	1	0.909	0.980	28.722	0.081	0.081	0.000	0.000	0.000
126	A	204	GLN	0	0.015	0.022	27.904	-0.010	-0.010	0.000	0.000	0.000
127	A	205	VAL	0	-0.014	0.000	23.969	0.002	0.002	0.000	0.000	0.000
128	A	206	VAL	0	0.051	0.020	27.102	0.000	0.000	0.000	0.000	0.000
129	A	207	TYR	0	-0.044	-0.021	27.666	-0.002	-0.002	0.000	0.000	0.000
130	A	208	ALA	0	0.000	-0.007	24.736	-0.005	-0.005	0.000	0.000	0.000
131	A	209	VAL	0	0.025	0.023	26.739	0.002	0.002	0.000	0.000	0.000
132	A	210	LYS	1	0.886	0.965	20.112	0.231	0.231	0.000	0.000	0.000
133	A	211	LYS	1	0.946	0.969	25.587	0.124	0.124	0.000	0.000	0.000
134	A	212	GLY	0	-0.020	-0.006	24.717	0.002	0.002	0.000	0.000	0.000
135	A	213	ASP	-1	-0.856	-0.942	21.516	-0.191	-0.191	0.000	0.000	0.000
136	A	214	LYS	1	0.929	0.973	21.944	0.131	0.131	0.000	0.000	0.000
137	A	215	ILE	0	-0.018	-0.024	20.181	0.000	0.000	0.000	0.000	0.000
138	A	216	ASP	-1	-0.823	-0.872	24.459	-0.119	-0.119	0.000	0.000	0.000
139	A	217	VAL	0	-0.050	-0.055	23.546	-0.003	-0.003	0.000	0.000	0.000
140	A	218	GLN	0	0.044	0.068	26.847	0.006	0.006	0.000	0.000	0.000
141	A	219	ILE	0	-0.045	-0.029	27.067	-0.006	-0.006	0.000	0.000	0.000
142	A	220	LEU	0	0.042	0.026	30.124	0.005	0.005	0.000	0.000	0.000
143	A	221	VAL	0	-0.067	-0.052	31.996	-0.003	-0.003	0.000	0.000	0.000
144	A	222	TYR	0	0.018	0.008	34.008	0.004	0.004	0.000	0.000	0.000
145	A	223	GLU	-1	-0.834	-0.901	35.913	-0.055	-0.055	0.000	0.000	0.000
146	A	224	ASP	-1	-0.885	-0.953	38.153	-0.037	-0.037	0.000	0.000	0.000
147	A	225	ASP	-1	-0.909	-0.973	36.205	-0.044	-0.044	0.000	0.000	0.000
148	A	226	ASP	-1	-0.933	-0.944	38.540	-0.031	-0.031	0.000	0.000	0.000
149	A	227	LEU	0	-0.149	-0.085	35.949	-0.001	-0.001	0.000	0.000	0.000
150	A	228	LEU	0	-0.020	-0.005	39.700	-0.001	-0.001	0.000	0.000	0.000
151	A	229	GLU	-1	-0.926	-0.951	41.591	-0.040	-0.040	0.000	0.000	0.000
152	A	230	SER	0	-0.047	-0.029	37.391	-0.001	-0.001	0.000	0.000	0.000
153	A	231	HIS	1	0.804	0.886	35.197	0.064	0.064	0.000	0.000	0.000
154	A	232	GLU	-1	-0.896	-0.948	34.794	-0.078	-0.078	0.000	0.000	0.000
155	A	233	GLU	-1	-0.950	-0.982	31.357	-0.081	-0.081	0.000	0.000	0.000
156	A	234	THR	0	0.037	-0.022	30.818	-0.002	-0.002	0.000	0.000	0.000
157	A	235	LYS	1	0.853	0.939	26.841	0.101	0.101	0.000	0.000	0.000
158	A	236	THR	0	0.015	-0.006	26.685	-0.006	-0.006	0.000	0.000	0.000
159	A	237	ILE	0	-0.039	-0.014	20.016	0.001	0.001	0.000	0.000	0.000
160	A	238	THR	0	-0.034	-0.031	20.945	0.009	0.009	0.000	0.000	0.000
161	A	239	VAL	0	-0.062	-0.030	17.286	-0.022	-0.022	0.000	0.000	0.000
162	A	240	LYS	0	0.046	0.030	14.273	-0.113	-0.113	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:79:ACE )