FMO DATABASE

FMODB ID: R9QR8

Calculation Name: 1LCL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1LCL

Chain ID: A

ChEMBL ID:

UniProt ID: Q05315

Base Structure: X-ray

Registration Date: 2023-06-22

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	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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1403168.786439
FMO2-HF: Nuclear repulsion	1345283.23745
FMO2-HF: Total energy	-57885.548989
FMO2-MP2: Total energy	-58052.445657

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-10.946	-4.877	3.29	-3.964	-5.395	0.012

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / q_NPA : -0.013

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	4	LEU	0	-0.017	0.003	3.821	-2.701	-0.722	0.013	-0.887	-1.104	0.002
4	A	5	PRO	0	-0.010	0.006	3.480	-2.451	-2.014	0.007	-0.284	-0.161	-0.002
5	A	6	VAL	0	0.026	0.002	4.443	0.895	0.976	-0.001	-0.005	-0.075	0.000
6	A	7	PRO	0	-0.007	-0.025	6.752	-0.114	-0.114	0.000	0.000	0.000	0.000
7	A	8	TYR	0	-0.081	-0.039	8.017	-0.184	-0.184	0.000	0.000	0.000	0.000
8	A	9	THR	0	0.017	-0.013	9.787	0.228	0.228	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.874	-0.908	13.420	-0.092	-0.092	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.021	0.005	15.403	0.040	0.040	0.000	0.000	0.000	0.000
11	A	12	ALA	0	-0.042	-0.041	18.747	0.024	0.024	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.006	0.001	20.781	-0.012	-0.012	0.000	0.000	0.000	0.000
13	A	14	LEU	0	-0.002	-0.001	20.633	0.025	0.025	0.000	0.000	0.000	0.000
14	A	15	SER	0	0.028	0.016	24.656	-0.010	-0.010	0.000	0.000	0.000	0.000
15	A	16	THR	0	0.061	0.011	26.581	0.016	0.016	0.000	0.000	0.000	0.000
16	A	17	GLY	0	-0.065	-0.045	27.172	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.005	0.014	22.615	0.011	0.011	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.011	-0.008	18.643	0.002	0.002	0.000	0.000	0.000	0.000
19	A	20	VAL	0	0.017	0.025	14.981	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.032	-0.021	12.980	0.006	0.006	0.000	0.000	0.000	0.000
21	A	22	ILE	0	0.005	-0.002	9.355	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.872	0.949	8.216	-1.567	-1.567	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.079	0.035	5.391	0.339	0.339	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.908	0.968	5.725	-2.087	-2.087	0.000	0.000	0.000	0.000
25	A	26	PRO	0	0.038	0.029	6.928	0.030	0.030	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.014	-0.002	4.933	0.189	0.189	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.016	0.002	8.759	-0.123	-0.123	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.016	0.003	12.358	0.060	0.060	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.067	0.005	13.936	-0.055	-0.055	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.017	0.016	17.506	-0.034	-0.034	0.000	0.000	0.000	0.000
31	A	32	ASN	0	-0.013	-0.019	16.438	-0.028	-0.028	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-1.011	-1.002	17.969	0.079	0.079	0.000	0.000	0.000	0.000
33	A	34	PRO	0	-0.002	0.041	12.929	-0.032	-0.032	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.001	-0.038	14.151	0.031	0.031	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.004	0.004	10.624	0.032	0.032	0.000	0.000	0.000	0.000
36	A	37	GLN	0	-0.038	-0.030	13.165	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	38	VAL	0	0.000	0.004	13.468	-0.019	-0.019	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.759	-0.864	15.698	-0.039	-0.039	0.000	0.000	0.000	0.000
39	A	40	PHE	0	-0.001	-0.008	17.365	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	41	HIS	1	0.896	0.938	18.782	0.129	0.129	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.054	0.018	22.237	0.003	0.003	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.899	-0.955	24.147	-0.090	-0.090	0.000	0.000	0.000	0.000
43	A	44	MET	0	0.005	-0.007	18.359	0.007	0.007	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.920	0.985	20.133	0.136	0.136	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.849	-0.917	17.170	-0.334	-0.334	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.878	-0.963	20.242	-0.180	-0.180	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.069	-0.038	22.923	0.028	0.028	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.802	-0.896	24.254	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.092	-0.039	21.242	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.016	0.008	24.385	0.010	0.010	0.000	0.000	0.000	0.000
51	A	52	PHE	0	-0.017	-0.016	20.257	0.015	0.015	0.000	0.000	0.000	0.000
52	A	53	HIS	0	-0.081	-0.024	20.363	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	PHE	0	0.024	0.006	16.185	0.016	0.016	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.009	-0.016	17.632	0.010	0.010	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.020	0.010	15.688	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	57	CYS	0	-0.017	0.022	16.758	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	58	PHE	0	0.027	-0.016	11.932	0.019	0.019	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.024	-0.004	17.344	-0.028	-0.028	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.845	0.904	19.716	-0.221	-0.221	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.879	0.947	21.738	-0.096	-0.096	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.012	0.022	19.679	0.012	0.012	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.023	-0.006	21.642	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	64	MET	0	-0.002	0.003	22.136	0.013	0.013	0.000	0.000	0.000	0.000
64	A	65	ASN	0	0.014	-0.006	24.276	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	66	SER	0	0.001	-0.012	25.302	0.008	0.008	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.874	0.943	22.698	0.094	0.094	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.852	-0.924	27.645	0.003	0.003	0.000	0.000	0.000	0.000
68	A	69	TYR	0	0.000	-0.012	30.683	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.006	0.011	29.046	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.013	-0.007	29.987	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	72	TRP	0	-0.006	-0.009	22.589	0.006	0.006	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.892	0.959	29.513	0.005	0.005	0.000	0.000	0.000	0.000
73	A	74	GLN	0	0.013	0.006	31.216	0.005	0.005	0.000	0.000	0.000	0.000
74	A	75	GLN	0	0.029	0.022	27.080	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.020	0.021	27.687	0.001	0.001	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.927	-0.980	26.473	0.099	0.099	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.001	0.002	24.796	0.003	0.003	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.992	0.978	24.962	-0.127	-0.127	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.032	0.000	24.409	0.017	0.017	0.000	0.000	0.000	0.000
80	A	81	MET	0	0.010	0.030	19.467	0.027	0.027	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.048	0.032	19.212	0.008	0.008	0.000	0.000	0.000	0.000
82	A	83	PHE	0	-0.016	-0.012	13.980	0.042	0.042	0.000	0.000	0.000	0.000
83	A	84	GLN	0	-0.020	-0.010	15.716	-0.069	-0.069	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.808	-0.922	14.828	0.544	0.544	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.027	0.017	12.256	0.010	0.010	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.050	-0.013	11.799	0.189	0.189	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.951	-0.980	7.019	3.279	3.279	0.000	0.000	0.000	0.000
88	A	89	PHE	0	-0.034	-0.022	9.313	-0.267	-0.267	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.898	-0.968	10.338	1.071	1.071	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.037	-0.007	12.632	-0.138	-0.138	0.000	0.000	0.000	0.000
91	A	92	SER	0	0.008	0.000	14.396	0.014	0.014	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.014	0.003	17.133	-0.034	-0.034	0.000	0.000	0.000	0.000
93	A	94	SER	0	0.000	-0.006	19.530	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.007	0.006	22.770	-0.012	-0.012	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.025	-0.013	25.368	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	97	PRO	0	-0.030	-0.032	28.713	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.807	-0.904	31.963	0.105	0.105	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.932	0.977	28.383	-0.134	-0.134	0.000	0.000	0.000	0.000
99	A	100	TYR	0	0.020	0.024	23.252	0.007	0.007	0.000	0.000	0.000	0.000
100	A	101	GLN	0	0.014	-0.004	24.083	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.020	-0.006	18.659	0.013	0.013	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.021	-0.003	19.481	-0.026	-0.026	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.024	0.007	15.878	0.048	0.048	0.000	0.000	0.000	0.000
104	A	105	ASN	0	0.033	0.005	14.913	0.063	0.063	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.034	0.018	17.339	-0.033	-0.033	0.000	0.000	0.000	0.000
106	A	107	GLN	0	0.018	0.019	20.394	-0.024	-0.024	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.022	-0.021	21.764	0.012	0.012	0.000	0.000	0.000	0.000
108	A	109	SER	0	-0.057	-0.041	21.420	0.003	0.003	0.000	0.000	0.000	0.000
109	A	110	TYR	0	0.004	-0.028	19.586	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.026	-0.009	24.255	0.006	0.006	0.000	0.000	0.000	0.000
111	A	112	PHE	0	0.002	-0.005	25.497	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.849	-0.927	27.301	0.097	0.097	0.000	0.000	0.000	0.000
113	A	114	HIS	0	-0.082	-0.040	26.691	-0.012	-0.012	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.831	0.917	29.597	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.005	0.000	29.261	-0.008	-0.008	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.941	0.983	29.822	0.001	0.001	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.084	0.023	26.306	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.878	-0.952	26.626	0.040	0.040	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.092	-0.036	28.756	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.066	-0.026	21.961	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.891	0.955	23.523	0.069	0.069	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.038	0.008	17.752	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	124	VAL	0	-0.018	0.007	14.998	0.035	0.035	0.000	0.000	0.000	0.000
124	A	125	GLN	0	0.015	-0.002	13.439	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.042	-0.014	9.930	0.096	0.096	0.000	0.000	0.000	0.000
126	A	127	TRP	0	0.001	-0.023	9.963	-0.205	-0.205	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.866	0.942	11.024	0.240	0.240	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.803	-0.896	9.533	-0.128	-0.128	0.000	0.000	0.000	0.000
129	A	130	ILE	0	-0.027	-0.011	6.947	0.202	0.202	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.018	0.005	2.219	-1.723	-0.319	1.696	-1.324	-1.776	0.011
131	A	132	LEU	0	-0.001	-0.012	3.046	-1.631	-0.549	0.070	-0.427	-0.726	-0.002
132	A	133	THR	0	0.004	-0.002	2.552	-1.902	-0.899	1.504	-1.000	-1.507	0.003
133	A	134	LYS	1	0.910	0.958	4.357	-2.201	-2.118	0.001	-0.037	-0.046	0.000
134	A	135	PHE	0	0.052	0.027	8.056	-0.081	-0.081	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.055	-0.035	10.730	-0.050	-0.050	0.000	0.000	0.000	0.000
136	A	137	VAL	0	0.076	0.055	14.347	0.024	0.024	0.000	0.000	0.000	0.000
137	A	138	SER	0	-0.042	-0.024	17.825	-0.011	-0.011	0.000	0.000	0.000	0.000
138	A	139	TYR	0	0.032	0.022	19.401	-0.017	-0.017	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.020	0.001	23.027	-0.015	-0.015	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.926	0.980	25.974	-0.124	-0.124	0.000	0.000	0.000	0.000
141	A	142	ARG	1	0.939	0.981	27.866	-0.083	-0.083	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)