FMO DATABASE

FMODB ID: R8M48

Calculation Name: 1L2W-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1L2W

Chain ID: A

ChEMBL ID:

UniProt ID: P08008

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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-996212.198654
FMO2-HF: Nuclear repulsion	947990.677882
FMO2-HF: Total energy	-48221.520772
FMO2-MP2: Total energy	-48361.98341

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:0:MET)

Summations of interaction energy for fragment #1(A:0:MET)

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.
-13.706	-14.517	31.313	-13.083	-17.42	-0.068

Interaction energy analysis for fragmet #1(A:0:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.032 / q_NPA : -0.021

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

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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	2	TYR	0	0.030	0.018	3.250	-1.211	0.998	0.045	-0.926	-1.329	-0.002
4	A	3	SER	0	-0.001	-0.011	5.596	0.439	0.439	0.000	0.000	0.000	0.000
5	A	4	PHE	0	0.029	0.030	2.233	-1.777	-0.388	3.673	-1.314	-3.748	-0.004
6	A	5	GLU	-1	-0.855	-0.942	2.452	-7.461	-6.596	3.255	-1.712	-2.409	-0.021
7	A	6	GLN	0	-0.023	-0.006	4.853	0.426	0.505	-0.001	-0.005	-0.073	0.000
8	A	7	ALA	0	0.028	0.018	7.580	0.189	0.189	0.000	0.000	0.000	0.000
9	A	8	ILE	0	0.009	0.007	6.446	0.095	0.095	0.000	0.000	0.000	0.000
10	A	9	THR	0	-0.029	-0.021	8.288	0.066	0.066	0.000	0.000	0.000	0.000
11	A	10	GLN	0	-0.026	-0.015	10.531	0.040	0.040	0.000	0.000	0.000	0.000
12	A	11	LEU	0	-0.008	-0.002	12.019	0.043	0.043	0.000	0.000	0.000	0.000
13	A	12	PHE	0	0.026	-0.014	11.075	0.039	0.039	0.000	0.000	0.000	0.000
14	A	13	GLN	0	-0.039	-0.006	14.021	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	14	GLN	0	-0.012	0.017	16.481	0.028	0.028	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.006	0.008	15.625	0.017	0.017	0.000	0.000	0.000	0.000
17	A	16	SER	0	-0.078	-0.030	18.706	0.013	0.013	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.022	-0.004	14.758	0.016	0.016	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.036	-0.020	14.774	-0.033	-0.033	0.000	0.000	0.000	0.000
20	A	19	ILE	0	-0.002	-0.015	10.166	0.057	0.057	0.000	0.000	0.000	0.000
21	A	20	PRO	0	-0.016	0.000	8.544	-0.023	-0.023	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.902	-0.944	9.395	-0.244	-0.244	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.072	-0.046	5.577	-0.187	-0.187	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.024	0.003	3.444	-0.033	0.388	0.012	-0.075	-0.358	0.000
25	A	24	GLU	-1	-0.945	-0.969	2.806	-1.213	0.133	0.272	-0.744	-0.874	-0.009
26	A	25	PRO	0	0.037	-0.024	2.677	-0.861	-0.531	6.027	-3.014	-3.343	0.010
27	A	26	VAL	0	-0.035	-0.003	3.615	0.699	-2.336	-0.011	3.456	-0.410	-0.001
28	A	27	ILE	0	0.028	0.030	6.323	-0.371	-0.371	0.000	0.000	0.000	0.000
29	A	28	GLY	0	0.044	0.027	8.822	-0.203	-0.203	0.000	0.000	0.000	0.000
30	A	29	VAL	0	-0.018	-0.020	12.535	-0.095	-0.095	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.870	0.949	15.120	-0.292	-0.292	0.000	0.000	0.000	0.000
32	A	31	VAL	0	0.035	0.016	18.351	-0.030	-0.030	0.000	0.000	0.000	0.000
33	A	32	GLY	0	0.031	0.022	20.967	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	33	GLU	-1	-0.919	-0.969	24.069	0.173	0.173	0.000	0.000	0.000	0.000
35	A	34	PHE	0	0.037	0.012	20.905	0.020	0.020	0.000	0.000	0.000	0.000
36	A	35	ALA	0	-0.039	-0.018	17.990	0.008	0.008	0.000	0.000	0.000	0.000
37	A	36	CYS	0	-0.039	-0.006	15.267	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	37	HIS	0	0.011	0.012	11.088	0.175	0.175	0.000	0.000	0.000	0.000
39	A	38	ILE	0	0.020	0.011	7.842	-0.184	-0.184	0.000	0.000	0.000	0.000
40	A	39	THR	0	0.007	-0.016	4.750	0.154	0.280	-0.001	-0.007	-0.118	0.000
41	A	40	GLU	-1	-0.814	-0.883	1.951	-2.672	-7.819	18.041	-8.555	-4.339	-0.040
42	A	41	HIS	0	-0.045	-0.002	3.755	-1.160	-0.738	0.001	-0.161	-0.262	-0.001
43	A	42	PRO	0	-0.043	-0.031	6.268	0.234	0.234	0.000	0.000	0.000	0.000
44	A	43	VAL	0	0.054	0.000	3.865	-0.240	-0.056	0.000	-0.026	-0.157	0.000
45	A	44	GLY	0	-0.030	-0.019	5.440	0.440	0.440	0.000	0.000	0.000	0.000
46	A	45	GLN	0	-0.063	-0.028	6.779	0.349	0.349	0.000	0.000	0.000	0.000
47	A	46	ILE	0	0.035	0.026	6.154	-0.160	-0.160	0.000	0.000	0.000	0.000
48	A	47	LEU	0	-0.032	-0.012	8.324	0.014	0.014	0.000	0.000	0.000	0.000
49	A	48	MET	0	-0.021	0.002	9.645	0.177	0.177	0.000	0.000	0.000	0.000
50	A	49	PHE	0	-0.006	-0.015	10.696	-0.076	-0.076	0.000	0.000	0.000	0.000
51	A	50	THR	0	0.006	-0.011	14.849	0.055	0.055	0.000	0.000	0.000	0.000
52	A	51	LEU	0	-0.002	0.005	17.672	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	52	PRO	0	-0.047	-0.011	20.645	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	53	SER	0	0.021	0.005	23.718	0.010	0.010	0.000	0.000	0.000	0.000
55	A	54	LEU	0	-0.018	-0.019	26.634	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	55	ASP	-1	-0.762	-0.867	29.464	0.095	0.095	0.000	0.000	0.000	0.000
57	A	56	ASN	0	-0.063	-0.043	33.169	0.002	0.002	0.000	0.000	0.000	0.000
58	A	57	ASN	0	-0.095	-0.044	35.264	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	58	ASP	-1	-0.886	-0.926	33.311	0.080	0.080	0.000	0.000	0.000	0.000
60	A	59	GLU	-1	-0.950	-0.981	34.947	0.065	0.065	0.000	0.000	0.000	0.000
61	A	60	LYS	1	0.930	0.956	32.934	-0.067	-0.067	0.000	0.000	0.000	0.000
62	A	61	GLU	-1	-0.865	-0.952	32.675	0.059	0.059	0.000	0.000	0.000	0.000
63	A	62	THR	0	0.017	0.030	33.571	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.023	0.009	29.412	0.000	0.000	0.000	0.000	0.000	0.000
65	A	64	LEU	0	-0.011	-0.021	28.239	0.001	0.001	0.000	0.000	0.000	0.000
66	A	65	SER	0	-0.035	-0.030	29.239	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	66	HIS	0	-0.007	0.014	27.203	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	67	ASN	0	-0.017	-0.003	24.726	0.000	0.000	0.000	0.000	0.000	0.000
69	A	68	ILE	0	-0.041	0.012	26.084	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	69	PHE	0	0.023	0.012	25.808	0.000	0.000	0.000	0.000	0.000	0.000
71	A	70	SER	0	-0.002	-0.016	25.437	0.003	0.003	0.000	0.000	0.000	0.000
72	A	71	GLN	0	-0.028	-0.025	26.325	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	72	ASP	-1	-0.809	-0.902	22.027	-0.049	-0.049	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.040	-0.034	18.084	0.012	0.012	0.000	0.000	0.000	0.000
75	A	74	LEU	0	-0.004	0.007	16.304	0.002	0.002	0.000	0.000	0.000	0.000
76	A	75	LYS	1	0.837	0.926	19.228	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	76	PRO	0	-0.025	-0.016	19.703	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	77	ILE	0	-0.037	-0.010	19.614	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.020	0.003	20.659	0.028	0.028	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.097	-0.058	20.070	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	80	TRP	0	0.067	0.022	22.442	0.008	0.008	0.000	0.000	0.000	0.000
82	A	81	ASP	-1	-0.884	-0.931	19.281	0.361	0.361	0.000	0.000	0.000	0.000
83	A	82	GLU	-1	-0.954	-1.002	21.150	0.180	0.180	0.000	0.000	0.000	0.000
84	A	83	VAL	0	-0.085	-0.030	20.054	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	84	GLY	0	0.001	0.002	21.221	0.003	0.003	0.000	0.000	0.000	0.000
86	A	85	GLY	0	-0.055	-0.010	22.171	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	86	HIS	0	0.004	0.001	21.386	-0.015	-0.015	0.000	0.000	0.000	0.000
88	A	87	PRO	0	0.023	0.028	22.701	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	88	VAL	0	-0.002	-0.025	17.010	0.028	0.028	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.007	0.014	19.414	-0.035	-0.035	0.000	0.000	0.000	0.000
91	A	90	TRP	0	-0.009	-0.015	15.063	0.022	0.022	0.000	0.000	0.000	0.000
92	A	91	ASN	0	0.033	0.024	15.294	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.932	0.949	11.295	0.110	0.110	0.000	0.000	0.000	0.000
94	A	93	GLN	0	0.043	0.033	11.919	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	94	PRO	0	0.019	0.012	10.925	-0.062	-0.062	0.000	0.000	0.000	0.000
96	A	95	LEU	0	0.038	0.010	5.387	0.040	0.040	0.000	0.000	0.000	0.000
97	A	96	ASN	0	-0.064	-0.039	9.409	0.030	0.030	0.000	0.000	0.000	0.000
98	A	97	SER	0	-0.038	-0.036	12.063	0.060	0.060	0.000	0.000	0.000	0.000
99	A	98	LEU	0	-0.022	0.020	10.436	0.032	0.032	0.000	0.000	0.000	0.000
100	A	99	ASP	-1	-0.821	-0.902	14.444	-0.102	-0.102	0.000	0.000	0.000	0.000
101	A	100	ASN	0	-0.060	-0.047	17.532	0.005	0.005	0.000	0.000	0.000	0.000
102	A	101	ASN	0	-0.091	-0.039	16.231	-0.021	-0.021	0.000	0.000	0.000	0.000
103	A	102	SER	0	-0.005	-0.037	14.271	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	103	LEU	0	0.029	0.017	9.115	0.005	0.005	0.000	0.000	0.000	0.000
105	A	104	TYR	0	-0.006	-0.006	13.773	0.054	0.054	0.000	0.000	0.000	0.000
106	A	105	THR	0	0.074	0.028	16.980	0.029	0.029	0.000	0.000	0.000	0.000
107	A	106	GLN	0	-0.024	0.000	12.232	-0.034	-0.034	0.000	0.000	0.000	0.000
108	A	107	LEU	0	0.036	0.000	14.893	0.031	0.031	0.000	0.000	0.000	0.000
109	A	108	GLU	-1	-0.935	-0.968	16.806	0.047	0.047	0.000	0.000	0.000	0.000
110	A	109	MET	0	0.024	0.005	19.780	0.007	0.007	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.079	-0.024	15.673	0.005	0.005	0.000	0.000	0.000	0.000
112	A	111	VAL	0	0.019	-0.003	19.424	0.009	0.009	0.000	0.000	0.000	0.000
113	A	112	GLN	0	0.036	0.028	21.583	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	113	GLY	0	-0.047	-0.020	23.028	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.016	-0.018	22.142	0.000	0.000	0.000	0.000	0.000	0.000
116	A	115	GLU	-1	-0.949	-0.980	24.164	0.101	0.101	0.000	0.000	0.000	0.000
117	A	116	ARG	1	0.854	0.917	27.193	-0.070	-0.070	0.000	0.000	0.000	0.000
118	A	117	LEU	0	-0.045	-0.036	24.801	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	118	GLN	0	-0.030	-0.002	27.252	0.011	0.011	0.000	0.000	0.000	0.000
120	A	119	THR	0	-0.102	-0.029	29.733	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	120	SER	0	0.028	0.018	33.001	0.002	0.002	0.000	0.000	0.000	0.000
122	A	121	SER	0	-0.070	-0.035	35.771	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:MET)