FMO DATABASE

FMODB ID: KG8Q3

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	OptAll
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	-996509.979587
FMO2-HF: Nuclear repulsion	948287.619056
FMO2-HF: Total energy	-48222.360531
FMO2-MP2: Total energy	-48362.771783

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.
-18.123	-10.254	17.532	-8.173	-17.225	-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 : -0.028 / q_NPA : -0.002

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	0.043	0.025	3.306	-0.855	1.296	0.043	-1.021	-1.172	-0.002
4	A	3	SER	0	-0.005	-0.009	5.465	0.555	0.555	0.000	0.000	0.000	0.000
5	A	4	PHE	0	0.051	0.031	2.306	-1.775	-0.091	3.540	-1.135	-4.089	-0.005
6	A	5	GLU	-1	-0.871	-0.944	2.420	-6.839	-5.423	2.256	-1.321	-2.351	-0.014
7	A	6	GLN	0	-0.002	0.004	4.843	0.670	0.760	-0.001	-0.007	-0.082	0.000
8	A	7	ALA	0	0.013	0.010	7.832	0.258	0.258	0.000	0.000	0.000	0.000
9	A	8	ILE	0	0.017	0.010	6.481	0.167	0.167	0.000	0.000	0.000	0.000
10	A	9	THR	0	-0.027	-0.028	8.206	0.150	0.150	0.000	0.000	0.000	0.000
11	A	10	GLN	0	-0.060	-0.037	10.388	0.108	0.108	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.008	0.006	11.851	0.059	0.059	0.000	0.000	0.000	0.000
13	A	12	PHE	0	0.021	-0.009	11.470	0.054	0.054	0.000	0.000	0.000	0.000
14	A	13	GLN	0	-0.028	-0.009	13.988	0.013	0.013	0.000	0.000	0.000	0.000
15	A	14	GLN	0	-0.013	0.010	16.470	0.036	0.036	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.004	0.009	15.898	0.020	0.020	0.000	0.000	0.000	0.000
17	A	16	SER	0	-0.082	-0.036	18.763	0.020	0.020	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.022	0.002	14.896	0.019	0.019	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.035	-0.027	15.124	-0.039	-0.039	0.000	0.000	0.000	0.000
20	A	19	ILE	0	0.005	-0.008	10.412	0.059	0.059	0.000	0.000	0.000	0.000
21	A	20	PRO	0	-0.007	0.005	8.658	-0.023	-0.023	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.908	-0.944	9.336	-0.078	-0.078	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.088	-0.060	5.969	-0.077	-0.077	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.025	0.008	3.498	-0.075	0.300	0.009	-0.073	-0.312	0.000
25	A	24	GLU	-1	-0.904	-0.950	3.018	-0.435	1.035	0.153	-0.823	-0.800	-0.008
26	A	25	PRO	0	0.015	-0.027	2.737	-1.456	-0.669	6.314	-2.958	-4.143	0.011
27	A	26	VAL	0	-0.057	-0.015	3.570	0.499	-2.691	0.009	3.584	-0.402	-0.001
28	A	27	ILE	0	0.036	0.041	6.587	-0.392	-0.392	0.000	0.000	0.000	0.000
29	A	28	GLY	0	0.045	0.031	8.815	-0.236	-0.236	0.000	0.000	0.000	0.000
30	A	29	VAL	0	-0.022	-0.027	12.527	-0.070	-0.070	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.788	0.903	15.214	-0.286	-0.286	0.000	0.000	0.000	0.000
32	A	31	VAL	0	0.027	0.012	18.109	-0.029	-0.029	0.000	0.000	0.000	0.000
33	A	32	GLY	0	0.047	0.030	20.881	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	33	GLU	-1	-0.894	-0.956	23.884	0.169	0.169	0.000	0.000	0.000	0.000
35	A	34	PHE	0	0.052	0.035	20.746	0.027	0.027	0.000	0.000	0.000	0.000
36	A	35	ALA	0	0.002	-0.013	18.103	0.008	0.008	0.000	0.000	0.000	0.000
37	A	36	CYS	0	-0.031	0.026	14.949	-0.013	-0.013	0.000	0.000	0.000	0.000
38	A	37	HIS	0	0.004	0.014	11.001	0.173	0.173	0.000	0.000	0.000	0.000
39	A	38	ILE	0	0.018	0.005	7.923	-0.182	-0.182	0.000	0.000	0.000	0.000
40	A	39	THR	0	-0.007	-0.032	4.482	0.087	0.224	-0.001	-0.010	-0.126	0.000
41	A	40	GLU	-1	-0.815	-0.917	2.204	-7.731	-6.156	5.167	-3.830	-2.912	-0.029
42	A	41	HIS	0	-0.017	0.015	3.321	-2.344	-1.410	0.018	-0.449	-0.502	-0.003
43	A	42	PRO	0	0.000	-0.018	6.064	0.252	0.252	0.000	0.000	0.000	0.000
44	A	43	VAL	0	0.042	0.001	3.082	-0.428	0.012	0.025	-0.130	-0.334	0.000
45	A	44	GLY	0	-0.012	-0.005	5.242	0.530	0.530	0.000	0.000	0.000	0.000
46	A	45	GLN	0	-0.060	-0.026	6.596	0.426	0.426	0.000	0.000	0.000	0.000
47	A	46	ILE	0	0.044	0.037	5.884	-0.081	-0.081	0.000	0.000	0.000	0.000
48	A	47	LEU	0	-0.042	-0.010	7.968	0.033	0.033	0.000	0.000	0.000	0.000
49	A	48	MET	0	-0.032	0.001	9.121	0.182	0.182	0.000	0.000	0.000	0.000
50	A	49	PHE	0	0.003	-0.006	10.180	-0.078	-0.078	0.000	0.000	0.000	0.000
51	A	50	THR	0	-0.005	-0.035	14.344	0.050	0.050	0.000	0.000	0.000	0.000
52	A	51	LEU	0	0.012	0.014	17.271	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	52	PRO	0	-0.059	-0.009	20.345	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	53	SER	0	0.020	-0.010	23.432	0.006	0.006	0.000	0.000	0.000	0.000
55	A	54	LEU	0	-0.014	-0.010	26.153	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	55	ASP	-1	-0.777	-0.891	29.264	0.082	0.082	0.000	0.000	0.000	0.000
57	A	56	ASN	0	-0.067	-0.041	33.008	0.001	0.001	0.000	0.000	0.000	0.000
58	A	57	ASN	0	-0.081	-0.040	34.981	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	58	ASP	-1	-0.850	-0.923	32.225	0.058	0.058	0.000	0.000	0.000	0.000
60	A	59	GLU	-1	-0.878	-0.953	34.240	0.055	0.055	0.000	0.000	0.000	0.000
61	A	60	LYS	1	0.810	0.895	32.584	-0.050	-0.050	0.000	0.000	0.000	0.000
62	A	61	GLU	-1	-0.801	-0.894	32.291	0.044	0.044	0.000	0.000	0.000	0.000
63	A	62	THR	0	-0.009	0.018	33.271	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	63	LEU	0	0.018	0.004	29.098	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	64	LEU	0	-0.015	-0.012	27.736	0.001	0.001	0.000	0.000	0.000	0.000
66	A	65	SER	0	-0.042	-0.036	28.855	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	66	HIS	0	-0.033	-0.004	26.948	-0.015	-0.015	0.000	0.000	0.000	0.000
68	A	67	ASN	0	-0.003	-0.014	24.702	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	68	ILE	0	-0.045	0.007	25.764	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	69	PHE	0	0.033	0.019	25.735	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	70	SER	0	-0.036	-0.031	25.231	0.007	0.007	0.000	0.000	0.000	0.000
72	A	71	GLN	0	-0.017	-0.017	26.303	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	72	ASP	-1	-0.788	-0.888	21.829	-0.098	-0.098	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.040	-0.027	17.795	0.010	0.010	0.000	0.000	0.000	0.000
75	A	74	LEU	0	-0.013	-0.009	16.388	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	75	LYS	1	0.841	0.922	19.146	0.033	0.033	0.000	0.000	0.000	0.000
77	A	76	PRO	0	-0.047	-0.003	19.100	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	77	ILE	0	-0.051	-0.021	19.602	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.019	0.008	20.369	0.026	0.026	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.080	-0.047	19.814	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	80	TRP	0	0.008	-0.017	22.053	0.011	0.011	0.000	0.000	0.000	0.000
82	A	81	ASP	-1	-0.841	-0.907	19.155	0.321	0.321	0.000	0.000	0.000	0.000
83	A	82	GLU	-1	-0.890	-0.946	21.198	0.172	0.172	0.000	0.000	0.000	0.000
84	A	83	VAL	0	-0.112	-0.050	19.373	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	84	GLY	0	-0.017	-0.014	21.023	0.012	0.012	0.000	0.000	0.000	0.000
86	A	85	GLY	0	-0.049	-0.012	21.966	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	86	HIS	0	-0.006	-0.006	21.281	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	87	PRO	0	0.031	0.029	22.641	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	88	VAL	0	-0.014	-0.028	16.821	0.031	0.031	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.013	0.015	19.063	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	90	TRP	0	0.005	-0.008	14.767	0.017	0.017	0.000	0.000	0.000	0.000
92	A	91	ASN	0	0.010	-0.022	14.929	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.876	0.932	10.448	0.230	0.230	0.000	0.000	0.000	0.000
94	A	93	GLN	0	0.052	0.044	11.749	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	94	PRO	0	-0.002	-0.012	10.746	-0.081	-0.081	0.000	0.000	0.000	0.000
96	A	95	LEU	0	-0.013	-0.002	5.453	0.060	0.060	0.000	0.000	0.000	0.000
97	A	96	ASN	0	-0.038	-0.028	9.340	-0.043	-0.043	0.000	0.000	0.000	0.000
98	A	97	SER	0	-0.077	-0.056	12.200	0.079	0.079	0.000	0.000	0.000	0.000
99	A	98	LEU	0	-0.012	0.023	10.437	0.040	0.040	0.000	0.000	0.000	0.000
100	A	99	ASP	-1	-0.745	-0.858	14.416	-0.161	-0.161	0.000	0.000	0.000	0.000
101	A	100	ASN	0	-0.093	-0.055	17.595	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	101	ASN	0	-0.080	-0.027	16.486	-0.025	-0.025	0.000	0.000	0.000	0.000
103	A	102	SER	0	-0.002	-0.021	14.677	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	103	LEU	0	0.032	0.011	9.040	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	104	TYR	0	-0.058	-0.047	13.604	0.059	0.059	0.000	0.000	0.000	0.000
106	A	105	THR	0	0.026	-0.016	16.979	0.040	0.040	0.000	0.000	0.000	0.000
107	A	106	GLN	0	-0.019	-0.001	11.754	-0.031	-0.031	0.000	0.000	0.000	0.000
108	A	107	LEU	0	0.054	0.021	14.653	0.039	0.039	0.000	0.000	0.000	0.000
109	A	108	GLU	-1	-0.881	-0.924	16.600	0.019	0.019	0.000	0.000	0.000	0.000
110	A	109	MET	0	0.009	-0.001	19.678	0.013	0.013	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.058	-0.021	15.244	0.010	0.010	0.000	0.000	0.000	0.000
112	A	111	VAL	0	0.006	-0.005	19.158	0.014	0.014	0.000	0.000	0.000	0.000
113	A	112	GLN	0	0.035	0.025	21.560	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	113	GLY	0	-0.051	-0.026	22.861	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.001	-0.007	22.122	0.002	0.002	0.000	0.000	0.000	0.000
116	A	115	GLU	-1	-0.914	-0.969	24.124	0.079	0.079	0.000	0.000	0.000	0.000
117	A	116	ARG	1	0.853	0.929	25.931	-0.048	-0.048	0.000	0.000	0.000	0.000
118	A	117	LEU	0	-0.029	-0.014	24.561	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	118	GLN	0	-0.023	-0.011	27.160	0.015	0.015	0.000	0.000	0.000	0.000
120	A	119	THR	0	-0.065	-0.019	29.709	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	120	SER	0	-0.035	-0.002	32.910	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	121	SER	0	-0.051	-0.027	35.383	-0.007	-0.007	0.000	0.000	0.000	0.000

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