FMO DATABASE

FMODB ID: MNM8Z

Calculation Name: 3LWG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3LWG

Chain ID: A

ChEMBL ID:

UniProt ID: D5MNX9

Base Structure: X-ray

Registration Date: 2023-09-20

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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-958699.716528
FMO2-HF: Nuclear repulsion	911936.104339
FMO2-HF: Total energy	-46763.612189
FMO2-MP2: Total energy	-46896.966704

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:10:GLU)

Summations of interaction energy for fragment #1(A:10:GLU)

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.
8.825	11.685	0.023	-1.258	-1.624	0.004

Interaction energy analysis for fragmet #1(A:10:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.932 / q_NPA : -0.973

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	12	LEU	0	-0.012	0.008	3.269	-8.682	-6.207	0.025	-1.179	-1.321	0.004
4	A	13	LEU	0	-0.074	-0.043	4.866	0.532	0.648	-0.001	-0.008	-0.106	0.000
5	A	14	VAL	0	-0.021	-0.017	7.715	-2.561	-2.561	0.000	0.000	0.000	0.000
6	A	15	CYS	0	0.017	0.000	8.644	1.415	1.415	0.000	0.000	0.000	0.000
7	A	16	THR	0	0.038	0.026	7.284	-0.544	-0.544	0.000	0.000	0.000	0.000
8	A	17	ARG	1	0.886	0.933	9.536	-17.845	-17.845	0.000	0.000	0.000	0.000
9	A	18	LEU	0	-0.005	0.014	11.785	-1.361	-1.361	0.000	0.000	0.000	0.000
10	A	19	ASP	-1	-0.789	-0.886	11.543	19.401	19.401	0.000	0.000	0.000	0.000
11	A	20	GLN	0	0.045	0.020	8.510	-0.368	-0.368	0.000	0.000	0.000	0.000
12	A	21	ASN	0	-0.019	-0.012	13.174	-1.095	-1.095	0.000	0.000	0.000	0.000
13	A	22	LEU	0	-0.021	-0.021	16.148	-0.871	-0.871	0.000	0.000	0.000	0.000
14	A	23	CYS	0	-0.082	-0.033	15.214	-0.684	-0.684	0.000	0.000	0.000	0.000
15	A	24	ALA	0	0.038	0.011	14.943	-0.705	-0.705	0.000	0.000	0.000	0.000
16	A	25	GLU	-1	-0.834	-0.907	11.993	20.081	20.081	0.000	0.000	0.000	0.000
17	A	26	LEU	0	-0.038	-0.030	5.818	-0.614	-0.614	0.000	0.000	0.000	0.000
18	A	27	ILE	0	-0.033	-0.003	9.348	1.140	1.140	0.000	0.000	0.000	0.000
19	A	28	SER	0	-0.026	-0.020	8.882	0.974	0.974	0.000	0.000	0.000	0.000
20	A	29	PHE	0	-0.004	-0.012	4.046	-1.874	-1.605	-0.001	-0.071	-0.197	0.000
21	A	30	GLY	0	0.035	0.027	8.925	1.845	1.845	0.000	0.000	0.000	0.000
22	A	31	SER	0	-0.048	-0.039	10.959	-1.030	-1.030	0.000	0.000	0.000	0.000
23	A	32	GLY	0	0.023	0.018	14.242	-1.059	-1.059	0.000	0.000	0.000	0.000
24	A	33	LYS	1	0.931	0.958	14.129	-17.384	-17.384	0.000	0.000	0.000	0.000
25	A	34	ALA	0	-0.009	-0.009	11.570	1.536	1.536	0.000	0.000	0.000	0.000
26	A	35	THR	0	-0.008	0.001	11.988	-1.176	-1.176	0.000	0.000	0.000	0.000
27	A	36	VAL	0	-0.024	-0.003	11.524	1.747	1.747	0.000	0.000	0.000	0.000
28	A	37	CYS	0	0.013	0.020	13.678	-1.268	-1.268	0.000	0.000	0.000	0.000
29	A	38	LEU	0	-0.010	0.000	16.130	0.583	0.583	0.000	0.000	0.000	0.000
30	A	39	THR	0	0.020	-0.003	18.632	-0.457	-0.457	0.000	0.000	0.000	0.000
31	A	40	PRO	0	-0.061	-0.022	20.590	0.190	0.190	0.000	0.000	0.000	0.000
32	A	41	LYS	1	0.867	0.904	17.125	-15.983	-15.983	0.000	0.000	0.000	0.000
33	A	42	GLU	-1	-0.732	-0.870	24.030	10.736	10.736	0.000	0.000	0.000	0.000
34	A	43	PHE	0	-0.063	-0.024	20.595	-0.270	-0.270	0.000	0.000	0.000	0.000
35	A	44	MET	0	-0.066	-0.001	19.745	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	45	LEU	0	-0.003	0.008	25.880	0.032	0.032	0.000	0.000	0.000	0.000
37	A	46	ALA	0	-0.109	-0.044	29.517	0.085	0.085	0.000	0.000	0.000	0.000
38	A	47	GLU	-1	-0.898	-0.941	32.105	7.975	7.975	0.000	0.000	0.000	0.000
39	A	48	ASP	-1	-0.959	-0.994	33.312	8.407	8.407	0.000	0.000	0.000	0.000
40	A	49	ASP	-1	-0.947	-0.972	33.877	8.465	8.465	0.000	0.000	0.000	0.000
41	A	50	VAL	0	-0.046	-0.019	31.068	0.166	0.166	0.000	0.000	0.000	0.000
42	A	51	VAL	0	-0.004	-0.008	24.912	0.059	0.059	0.000	0.000	0.000	0.000
43	A	52	HIS	0	0.037	0.019	27.374	-0.164	-0.164	0.000	0.000	0.000	0.000
44	A	53	ALA	0	0.057	0.009	26.220	0.435	0.435	0.000	0.000	0.000	0.000
45	A	54	GLY	0	-0.029	-0.011	25.116	0.320	0.320	0.000	0.000	0.000	0.000
46	A	55	PHE	0	0.020	0.012	21.101	0.464	0.464	0.000	0.000	0.000	0.000
47	A	56	ILE	0	0.003	0.021	20.919	0.665	0.665	0.000	0.000	0.000	0.000
48	A	57	VAL	0	0.026	-0.002	21.508	0.426	0.426	0.000	0.000	0.000	0.000
49	A	58	GLY	0	0.012	0.027	19.593	0.409	0.409	0.000	0.000	0.000	0.000
50	A	59	ALA	0	0.040	0.016	16.714	0.882	0.882	0.000	0.000	0.000	0.000
51	A	60	ALA	0	0.015	0.016	16.473	0.801	0.801	0.000	0.000	0.000	0.000
52	A	61	SER	0	-0.031	-0.043	17.711	0.223	0.223	0.000	0.000	0.000	0.000
53	A	62	PHE	0	-0.008	-0.014	9.040	0.505	0.505	0.000	0.000	0.000	0.000
54	A	63	ALA	0	0.067	0.036	12.952	1.228	1.228	0.000	0.000	0.000	0.000
55	A	64	ALA	0	-0.003	-0.011	14.229	0.429	0.429	0.000	0.000	0.000	0.000
56	A	65	LEU	0	-0.004	-0.014	13.227	0.122	0.122	0.000	0.000	0.000	0.000
57	A	66	CYS	0	-0.048	-0.022	9.883	1.385	1.385	0.000	0.000	0.000	0.000
58	A	67	ALA	0	-0.017	0.007	11.028	0.871	0.871	0.000	0.000	0.000	0.000
59	A	68	LEU	0	-0.039	-0.021	13.684	-0.208	-0.208	0.000	0.000	0.000	0.000
60	A	69	ASN	0	0.010	0.004	7.594	0.178	0.178	0.000	0.000	0.000	0.000
61	A	70	LYS	1	0.910	0.960	11.429	-18.151	-18.151	0.000	0.000	0.000	0.000
62	A	71	LYS	1	1.005	1.008	11.071	-18.591	-18.591	0.000	0.000	0.000	0.000
63	A	72	ASN	0	-0.046	-0.019	12.521	-0.173	-0.173	0.000	0.000	0.000	0.000
64	A	73	SER	0	0.004	-0.008	14.223	-0.864	-0.864	0.000	0.000	0.000	0.000
65	A	74	LEU	0	0.002	0.000	16.672	0.324	0.324	0.000	0.000	0.000	0.000
66	A	75	ILE	0	0.012	0.012	18.081	-0.283	-0.283	0.000	0.000	0.000	0.000
67	A	76	SER	0	-0.082	-0.059	20.993	-0.055	-0.055	0.000	0.000	0.000	0.000
68	A	77	SER	0	-0.029	-0.040	24.685	-0.465	-0.465	0.000	0.000	0.000	0.000
69	A	78	MET	0	0.006	-0.001	23.050	0.437	0.437	0.000	0.000	0.000	0.000
70	A	79	LYS	1	0.862	0.949	26.413	-9.998	-9.998	0.000	0.000	0.000	0.000
71	A	80	VAL	0	0.009	-0.006	26.297	0.335	0.335	0.000	0.000	0.000	0.000
72	A	81	ASN	0	-0.051	-0.023	28.160	-0.462	-0.462	0.000	0.000	0.000	0.000
73	A	82	LEU	0	0.018	0.000	27.273	0.315	0.315	0.000	0.000	0.000	0.000
74	A	83	LEU	0	-0.046	-0.023	29.420	-0.316	-0.316	0.000	0.000	0.000	0.000
75	A	84	ALA	0	0.002	0.005	30.702	-0.295	-0.295	0.000	0.000	0.000	0.000
76	A	85	PRO	0	0.003	0.004	30.581	0.234	0.234	0.000	0.000	0.000	0.000
77	A	86	ILE	0	0.002	0.005	25.177	0.196	0.196	0.000	0.000	0.000	0.000
78	A	87	GLU	-1	-0.847	-0.918	28.732	9.150	9.150	0.000	0.000	0.000	0.000
79	A	88	ILE	0	-0.009	-0.016	26.348	0.494	0.494	0.000	0.000	0.000	0.000
80	A	89	LYS	1	0.728	0.837	24.115	-11.251	-11.251	0.000	0.000	0.000	0.000
81	A	90	GLN	0	-0.003	0.019	25.374	0.210	0.210	0.000	0.000	0.000	0.000
82	A	91	GLU	-1	-0.853	-0.913	20.316	14.880	14.880	0.000	0.000	0.000	0.000
83	A	92	ILE	0	0.000	0.005	21.563	-0.211	-0.211	0.000	0.000	0.000	0.000
84	A	93	TYR	0	-0.002	-0.023	16.830	1.045	1.045	0.000	0.000	0.000	0.000
85	A	94	PHE	0	0.003	-0.010	17.224	-0.732	-0.732	0.000	0.000	0.000	0.000
86	A	95	ASN	0	-0.022	-0.012	16.495	2.007	2.007	0.000	0.000	0.000	0.000
87	A	96	ALA	0	0.031	0.017	15.594	-0.769	-0.769	0.000	0.000	0.000	0.000
88	A	97	THR	0	-0.063	-0.051	16.861	0.599	0.599	0.000	0.000	0.000	0.000
89	A	98	ILE	0	-0.036	-0.001	16.831	-0.595	-0.595	0.000	0.000	0.000	0.000
90	A	99	THR	0	-0.001	-0.005	20.102	-0.148	-0.148	0.000	0.000	0.000	0.000
91	A	100	HIS	0	-0.009	-0.005	23.390	-0.246	-0.246	0.000	0.000	0.000	0.000
92	A	101	THR	0	0.017	-0.010	20.952	0.524	0.524	0.000	0.000	0.000	0.000
93	A	102	SER	0	-0.020	-0.003	23.342	-0.545	-0.545	0.000	0.000	0.000	0.000
94	A	103	SER	0	0.001	-0.005	20.380	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	104	LYS	1	0.929	0.964	20.773	-10.460	-10.460	0.000	0.000	0.000	0.000
96	A	105	LYS	1	0.897	0.941	22.770	-10.357	-10.357	0.000	0.000	0.000	0.000
97	A	106	SER	0	-0.004	0.014	20.602	-0.042	-0.042	0.000	0.000	0.000	0.000
98	A	107	THR	0	-0.022	-0.011	22.689	-0.348	-0.348	0.000	0.000	0.000	0.000
99	A	108	ILE	0	0.006	0.013	17.705	0.212	0.212	0.000	0.000	0.000	0.000
100	A	109	ARG	1	0.790	0.896	21.021	-11.032	-11.032	0.000	0.000	0.000	0.000
101	A	110	VAL	0	-0.024	-0.027	18.779	0.698	0.698	0.000	0.000	0.000	0.000
102	A	111	GLU	-1	-0.802	-0.883	20.996	10.284	10.284	0.000	0.000	0.000	0.000
103	A	112	GLY	0	0.030	0.016	20.946	0.722	0.722	0.000	0.000	0.000	0.000
104	A	113	GLU	-1	-0.884	-0.929	22.279	12.156	12.156	0.000	0.000	0.000	0.000
105	A	114	PHE	0	0.026	0.006	23.094	0.455	0.455	0.000	0.000	0.000	0.000
106	A	115	MET	0	-0.009	-0.013	25.336	-0.244	-0.244	0.000	0.000	0.000	0.000
107	A	116	GLU	-1	-0.929	-0.962	24.562	11.219	11.219	0.000	0.000	0.000	0.000
108	A	117	ILE	0	-0.037	0.000	26.302	-0.271	-0.271	0.000	0.000	0.000	0.000
109	A	118	LYS	1	0.795	0.878	26.088	-10.115	-10.115	0.000	0.000	0.000	0.000
110	A	119	VAL	0	0.031	0.009	25.817	-0.360	-0.360	0.000	0.000	0.000	0.000
111	A	120	PHE	0	-0.025	-0.009	22.817	-0.127	-0.127	0.000	0.000	0.000	0.000
112	A	121	GLU	-1	-0.797	-0.897	25.161	10.047	10.047	0.000	0.000	0.000	0.000
113	A	122	GLY	0	0.035	0.013	24.866	-0.329	-0.329	0.000	0.000	0.000	0.000
114	A	123	ASP	-1	-0.875	-0.901	24.310	10.794	10.794	0.000	0.000	0.000	0.000
115	A	124	PHE	0	0.038	0.007	21.066	-0.227	-0.227	0.000	0.000	0.000	0.000
116	A	125	GLU	-1	-0.822	-0.851	22.444	10.701	10.701	0.000	0.000	0.000	0.000
117	A	126	ILE	0	0.014	-0.001	17.549	0.236	0.236	0.000	0.000	0.000	0.000
118	A	127	LEU	0	-0.014	-0.001	21.341	-0.297	-0.297	0.000	0.000	0.000	0.000
119	A	128	VAL	0	-0.003	-0.019	16.974	0.734	0.734	0.000	0.000	0.000	0.000
120	A	129	PHE	0	-0.007	0.003	19.027	-0.325	-0.325	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:GLU)