FMO DATABASE

FMODB ID: QVM5Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-995768.857318
FMO2-HF: Nuclear repulsion	947546.727531
FMO2-HF: Total energy	-48222.129788
FMO2-MP2: Total energy	-48362.529361

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.
-17.956	-10.636	16.776	-7.664	-16.431	-0.051

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 : -0.031 / q_NPA : -0.004

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	2	TYR	0	0.036	0.020	3.062	-1.711	0.847	0.140	-1.281	-1.416	-0.003
4	A	3	SER	0	0.002	-0.010	5.585	0.440	0.440	0.000	0.000	0.000	0.000
5	A	4	PHE	0	0.033	0.032	2.319	-1.859	0.184	3.038	-1.178	-3.903	-0.005
6	A	5	GLU	-1	-0.864	-0.947	2.342	-7.017	-5.588	2.544	-1.466	-2.506	-0.016
7	A	6	GLN	0	-0.020	-0.001	4.689	0.552	0.655	-0.001	-0.011	-0.092	0.000
8	A	7	ALA	0	0.022	0.015	7.637	0.233	0.233	0.000	0.000	0.000	0.000
9	A	8	ILE	0	0.006	0.005	6.358	0.154	0.154	0.000	0.000	0.000	0.000
10	A	9	THR	0	-0.026	-0.026	8.150	0.134	0.134	0.000	0.000	0.000	0.000
11	A	10	GLN	0	-0.052	-0.028	10.335	0.069	0.069	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.001	0.001	11.890	0.059	0.059	0.000	0.000	0.000	0.000
13	A	12	PHE	0	0.026	-0.013	11.379	0.053	0.053	0.000	0.000	0.000	0.000
14	A	13	GLN	0	-0.039	-0.006	13.894	0.012	0.012	0.000	0.000	0.000	0.000
15	A	14	GLN	0	-0.019	0.010	16.326	0.031	0.031	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.004	0.007	15.644	0.020	0.020	0.000	0.000	0.000	0.000
17	A	16	SER	0	-0.085	-0.032	18.583	0.020	0.020	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.021	-0.001	14.749	0.023	0.023	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.029	-0.016	15.011	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	19	ILE	0	0.003	-0.017	10.206	0.047	0.047	0.000	0.000	0.000	0.000
21	A	20	PRO	0	-0.014	0.002	8.706	-0.017	-0.017	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.906	-0.945	9.510	-0.123	-0.123	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.079	-0.051	6.117	-0.135	-0.135	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.018	0.004	3.562	-0.050	0.293	0.006	-0.058	-0.291	0.000
25	A	24	GLU	-1	-0.937	-0.963	3.106	-0.188	0.975	0.089	-0.628	-0.624	-0.006
26	A	25	PRO	0	0.039	-0.024	2.690	-1.269	-0.837	6.547	-3.293	-3.686	0.011
27	A	26	VAL	0	-0.046	-0.004	3.579	0.954	-2.507	-0.015	3.917	-0.440	-0.001
28	A	27	ILE	0	0.019	0.023	6.322	-0.326	-0.326	0.000	0.000	0.000	0.000
29	A	28	GLY	0	0.052	0.033	8.900	-0.207	-0.207	0.000	0.000	0.000	0.000
30	A	29	VAL	0	-0.017	-0.021	12.600	-0.084	-0.084	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.867	0.943	15.224	-0.263	-0.263	0.000	0.000	0.000	0.000
32	A	31	VAL	0	0.037	0.017	18.218	-0.029	-0.029	0.000	0.000	0.000	0.000
33	A	32	GLY	0	0.047	0.033	20.905	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	33	GLU	-1	-0.915	-0.963	24.098	0.158	0.158	0.000	0.000	0.000	0.000
35	A	34	PHE	0	0.017	0.010	20.777	0.019	0.019	0.000	0.000	0.000	0.000
36	A	35	ALA	0	-0.026	-0.009	17.969	0.007	0.007	0.000	0.000	0.000	0.000
37	A	36	CYS	0	-0.047	0.004	15.169	-0.022	-0.022	0.000	0.000	0.000	0.000
38	A	37	HIS	0	0.009	0.013	11.038	0.175	0.175	0.000	0.000	0.000	0.000
39	A	38	ILE	0	0.013	0.006	7.875	-0.185	-0.185	0.000	0.000	0.000	0.000
40	A	39	THR	0	0.004	-0.024	4.590	0.089	0.221	-0.001	-0.008	-0.122	0.000
41	A	40	GLU	-1	-0.808	-0.901	2.315	-8.230	-6.296	4.427	-3.460	-2.902	-0.030
42	A	41	HIS	0	-0.033	0.004	3.773	-1.250	-0.833	0.001	-0.156	-0.262	-0.001
43	A	42	PRO	0	-0.019	-0.021	6.303	0.232	0.232	0.000	0.000	0.000	0.000
44	A	43	VAL	0	0.046	-0.004	3.601	-0.213	0.014	0.001	-0.042	-0.187	0.000
45	A	44	GLY	0	-0.026	-0.014	5.208	0.529	0.529	0.000	0.000	0.000	0.000
46	A	45	GLN	0	-0.075	-0.031	6.653	0.440	0.440	0.000	0.000	0.000	0.000
47	A	46	ILE	0	0.039	0.024	5.963	-0.146	-0.146	0.000	0.000	0.000	0.000
48	A	47	LEU	0	-0.037	-0.011	8.219	0.032	0.032	0.000	0.000	0.000	0.000
49	A	48	MET	0	-0.015	0.008	9.503	0.168	0.168	0.000	0.000	0.000	0.000
50	A	49	PHE	0	-0.006	-0.013	10.475	-0.071	-0.071	0.000	0.000	0.000	0.000
51	A	50	THR	0	0.008	-0.026	14.715	0.055	0.055	0.000	0.000	0.000	0.000
52	A	51	LEU	0	0.006	0.014	17.554	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	52	PRO	0	-0.047	-0.009	20.528	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	53	SER	0	0.022	0.006	23.595	0.011	0.011	0.000	0.000	0.000	0.000
55	A	54	LEU	0	-0.013	-0.016	26.329	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	55	ASP	-1	-0.777	-0.896	29.334	0.080	0.080	0.000	0.000	0.000	0.000
57	A	56	ASN	0	-0.050	-0.036	33.038	0.001	0.001	0.000	0.000	0.000	0.000
58	A	57	ASN	0	-0.088	-0.033	35.131	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	58	ASP	-1	-0.882	-0.943	32.851	0.054	0.054	0.000	0.000	0.000	0.000
60	A	59	GLU	-1	-0.949	-0.971	34.802	0.052	0.052	0.000	0.000	0.000	0.000
61	A	60	LYS	1	0.850	0.893	32.948	-0.046	-0.046	0.000	0.000	0.000	0.000
62	A	61	GLU	-1	-0.805	-0.896	32.683	0.040	0.040	0.000	0.000	0.000	0.000
63	A	62	THR	0	0.012	0.027	33.743	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.029	0.020	29.265	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	64	LEU	0	-0.021	-0.025	28.256	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	65	SER	0	-0.029	-0.026	29.261	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	66	HIS	0	0.003	0.019	27.122	-0.015	-0.015	0.000	0.000	0.000	0.000
68	A	67	ASN	0	-0.012	-0.011	24.851	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	68	ILE	0	-0.038	0.015	26.121	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	69	PHE	0	0.025	0.018	25.814	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	70	SER	0	0.004	-0.018	25.534	0.006	0.006	0.000	0.000	0.000	0.000
72	A	71	GLN	0	-0.024	-0.020	26.294	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	72	ASP	-1	-0.804	-0.895	21.951	-0.101	-0.101	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.042	-0.033	17.915	0.012	0.012	0.000	0.000	0.000	0.000
75	A	74	LEU	0	-0.009	0.003	16.458	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	75	LYS	1	0.813	0.908	19.256	0.034	0.034	0.000	0.000	0.000	0.000
77	A	76	PRO	0	-0.031	-0.018	19.453	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	77	ILE	0	-0.052	-0.020	19.652	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.022	0.010	20.567	0.026	0.026	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.082	-0.050	20.004	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	80	TRP	0	0.036	0.014	22.439	0.011	0.011	0.000	0.000	0.000	0.000
82	A	81	ASP	-1	-0.868	-0.921	19.170	0.317	0.317	0.000	0.000	0.000	0.000
83	A	82	GLU	-1	-0.924	-0.983	21.122	0.165	0.165	0.000	0.000	0.000	0.000
84	A	83	VAL	0	-0.095	-0.038	19.943	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	84	GLY	0	0.002	0.000	21.174	0.006	0.006	0.000	0.000	0.000	0.000
86	A	85	GLY	0	-0.047	-0.008	22.118	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	86	HIS	0	-0.006	-0.006	21.319	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	87	PRO	0	0.030	0.030	22.636	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	88	VAL	0	-0.015	-0.036	16.891	0.027	0.027	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.010	0.014	19.282	-0.035	-0.035	0.000	0.000	0.000	0.000
91	A	90	TRP	0	-0.002	-0.015	14.976	0.012	0.012	0.000	0.000	0.000	0.000
92	A	91	ASN	0	0.020	0.006	15.151	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.904	0.941	10.994	0.205	0.205	0.000	0.000	0.000	0.000
94	A	93	GLN	0	0.051	0.041	11.915	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	94	PRO	0	0.010	0.002	10.864	-0.078	-0.078	0.000	0.000	0.000	0.000
96	A	95	LEU	0	0.013	0.007	5.300	0.043	0.043	0.000	0.000	0.000	0.000
97	A	96	ASN	0	-0.048	-0.033	9.263	0.003	0.003	0.000	0.000	0.000	0.000
98	A	97	SER	0	-0.049	-0.037	11.852	0.084	0.084	0.000	0.000	0.000	0.000
99	A	98	LEU	0	-0.007	0.021	10.516	0.033	0.033	0.000	0.000	0.000	0.000
100	A	99	ASP	-1	-0.792	-0.879	14.358	-0.157	-0.157	0.000	0.000	0.000	0.000
101	A	100	ASN	0	-0.077	-0.057	17.509	0.007	0.007	0.000	0.000	0.000	0.000
102	A	101	ASN	0	-0.087	-0.036	16.135	-0.027	-0.027	0.000	0.000	0.000	0.000
103	A	102	SER	0	0.029	-0.011	14.356	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	103	LEU	0	0.018	0.011	9.150	0.004	0.004	0.000	0.000	0.000	0.000
105	A	104	TYR	0	-0.051	-0.042	13.830	0.056	0.056	0.000	0.000	0.000	0.000
106	A	105	THR	0	0.049	0.008	17.027	0.036	0.036	0.000	0.000	0.000	0.000
107	A	106	GLN	0	-0.028	-0.002	12.186	-0.030	-0.030	0.000	0.000	0.000	0.000
108	A	107	LEU	0	0.045	0.006	14.760	0.035	0.035	0.000	0.000	0.000	0.000
109	A	108	GLU	-1	-0.890	-0.934	16.705	0.013	0.013	0.000	0.000	0.000	0.000
110	A	109	MET	0	0.023	0.009	19.691	0.012	0.012	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.078	-0.026	15.528	0.009	0.009	0.000	0.000	0.000	0.000
112	A	111	VAL	0	0.020	-0.005	19.298	0.013	0.013	0.000	0.000	0.000	0.000
113	A	112	GLN	0	0.036	0.035	21.473	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	113	GLY	0	-0.048	-0.022	22.902	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.018	-0.022	21.999	0.003	0.003	0.000	0.000	0.000	0.000
116	A	115	GLU	-1	-0.920	-0.966	24.040	0.075	0.075	0.000	0.000	0.000	0.000
117	A	116	ARG	1	0.847	0.918	26.797	-0.040	-0.040	0.000	0.000	0.000	0.000
118	A	117	LEU	0	-0.049	-0.035	24.715	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	118	GLN	0	-0.042	-0.021	27.166	0.012	0.012	0.000	0.000	0.000	0.000
120	A	119	THR	0	-0.100	-0.029	29.614	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	120	SER	0	0.028	0.021	32.878	0.002	0.002	0.000	0.000	0.000	0.000
122	A	121	SER	0	-0.064	-0.028	35.645	-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)