FMO DATABASE

FMODB ID: 4J9NN

Calculation Name: 2NWV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2NWV

Chain ID: A

ChEMBL ID:

UniProt ID: Q3M7V9

Base Structure: X-ray

Registration Date: 2023-09-21

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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-952970.353055
FMO2-HF: Nuclear repulsion	906731.916651
FMO2-HF: Total energy	-46238.436404
FMO2-MP2: Total energy	-46375.153632

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:ASP)

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

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.
10.685	2.577	24.016	-5.467	-10.443	0.104

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.866 / q_NPA : -0.948

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	VAL	0	0.041	0.010	2.811	5.397	2.872	0.411	3.679	-1.566	0.006
4	A	5	ALA	0	-0.033	-0.008	2.403	-17.512	-14.492	3.447	-2.958	-3.509	0.041
5	A	6	GLU	-1	-0.796	-0.891	1.680	23.650	14.347	20.077	-5.941	-4.833	0.051
6	A	7	TYR	0	-0.038	-0.059	3.565	-14.758	-14.058	0.081	-0.247	-0.535	0.006
7	A	8	ARG	1	0.861	0.905	6.037	-43.022	-43.022	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.792	0.887	6.207	-48.394	-48.394	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.030	0.015	7.861	-4.428	-4.428	0.000	0.000	0.000	0.000
10	A	11	ILE	0	0.014	0.007	9.865	-3.452	-3.452	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.798	0.892	10.898	-29.458	-29.458	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.086	-0.021	12.315	-0.028	-0.028	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.055	0.023	13.799	-1.623	-1.623	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.006	-0.008	15.709	-1.406	-1.406	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.026	-0.034	16.582	-1.263	-1.263	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.883	-0.930	17.112	17.083	17.083	0.000	0.000	0.000	0.000
17	A	18	TYR	0	-0.044	-0.051	19.751	-0.632	-0.632	0.000	0.000	0.000	0.000
18	A	19	ASP	-1	-0.811	-0.856	21.546	12.166	12.166	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.053	-0.046	22.117	-1.144	-1.144	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.007	0.002	22.440	-0.633	-0.633	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.038	-0.028	25.648	-0.677	-0.677	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.819	0.905	27.608	-11.205	-11.205	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.043	-0.021	28.885	-0.060	-0.060	0.000	0.000	0.000	0.000
24	A	25	SER	0	-0.022	0.007	30.742	-0.179	-0.179	0.000	0.000	0.000	0.000
25	A	26	PRO	0	-0.033	-0.012	32.373	-0.191	-0.191	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.903	-0.931	33.662	8.470	8.470	0.000	0.000	0.000	0.000
27	A	28	THR	0	-0.058	-0.055	34.804	0.027	0.027	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.040	-0.027	30.772	0.125	0.125	0.000	0.000	0.000	0.000
29	A	30	TYR	0	-0.005	-0.011	32.158	-0.351	-0.351	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.881	-0.928	31.247	10.418	10.418	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.017	-0.047	26.134	-0.169	-0.169	0.000	0.000	0.000	0.000
32	A	33	CYS	0	-0.109	-0.055	25.519	-0.219	-0.219	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.047	0.037	19.478	0.232	0.232	0.000	0.000	0.000	0.000
34	A	35	VAL	0	-0.056	-0.035	20.317	-0.304	-0.304	0.000	0.000	0.000	0.000
35	A	36	PHE	0	0.031	0.011	14.996	0.751	0.751	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.783	-0.867	16.015	17.867	17.867	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.786	-0.890	10.498	28.838	28.838	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.076	-0.022	12.282	1.515	1.515	0.000	0.000	0.000	0.000
39	A	40	HIS	1	0.788	0.851	14.941	-16.728	-16.728	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.753	-0.808	10.572	30.152	30.152	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.053	-0.025	13.534	-1.089	-1.089	0.000	0.000	0.000	0.000
42	A	43	TYR	0	0.009	-0.026	10.926	0.251	0.251	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.020	-0.012	16.513	-0.427	-0.427	0.000	0.000	0.000	0.000
44	A	45	TRP	0	0.013	0.009	19.997	0.391	0.391	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.038	-0.027	22.133	-0.478	-0.478	0.000	0.000	0.000	0.000
46	A	47	ALA	0	0.091	0.061	25.785	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	VAL	0	-0.101	-0.073	28.799	-0.189	-0.189	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.750	-0.862	31.596	9.067	9.067	0.000	0.000	0.000	0.000
49	A	50	TRP	0	-0.087	-0.052	35.018	-0.108	-0.108	0.000	0.000	0.000	0.000
50	A	51	GLN	0	0.082	0.054	38.760	0.135	0.135	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.006	-0.005	40.997	-0.159	-0.159	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.008	-0.016	43.251	0.051	0.051	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.946	0.984	39.489	-7.964	-7.964	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.878	0.943	34.418	-9.018	-9.018	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.024	-0.001	33.520	-0.067	-0.067	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.935	0.955	28.921	-10.678	-10.678	0.000	0.000	0.000	0.000
57	A	58	TYR	0	-0.029	0.000	29.355	-0.147	-0.147	0.000	0.000	0.000	0.000
58	A	59	THR	0	0.025	0.020	23.978	0.077	0.077	0.000	0.000	0.000	0.000
59	A	60	TYR	0	0.018	0.011	24.319	-0.265	-0.265	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.032	0.022	18.765	0.084	0.084	0.000	0.000	0.000	0.000
61	A	62	HIS	0	-0.092	-0.046	18.840	-0.425	-0.425	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.026	0.012	13.694	-0.033	-0.033	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.925	0.963	15.074	-17.718	-17.718	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.011	0.022	8.126	-0.031	-0.031	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.778	0.890	12.122	-17.262	-17.262	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.073	-0.052	13.681	0.186	0.186	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.882	-0.938	8.090	32.618	32.618	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.792	0.919	8.973	-19.300	-19.300	0.000	0.000	0.000	0.000
69	A	70	ILE	0	0.039	0.020	9.517	-0.076	-0.076	0.000	0.000	0.000	0.000
70	A	71	TYR	0	-0.010	-0.029	12.615	-2.314	-2.314	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.037	0.010	16.180	0.151	0.151	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.870	-0.950	18.313	15.133	15.133	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.874	-0.932	21.048	11.235	11.235	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.766	-0.870	21.597	15.119	15.119	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.128	-0.073	23.518	-0.575	-0.575	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.048	-0.038	22.566	-0.290	-0.290	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.955	-0.965	25.552	10.146	10.146	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.875	-0.924	22.955	13.190	13.190	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.031	0.036	22.803	0.111	0.111	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.005	-0.037	16.519	0.602	0.602	0.000	0.000	0.000	0.000
81	A	82	ALA	0	-0.010	-0.011	17.187	0.898	0.898	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.043	-0.027	17.524	0.740	0.740	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.812	-0.888	16.577	17.175	17.175	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.002	-0.011	11.951	1.061	1.061	0.000	0.000	0.000	0.000
85	A	86	MET	0	-0.037	-0.009	13.491	0.982	0.982	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.803	0.904	15.293	-14.881	-14.881	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.029	-0.010	12.358	0.214	0.214	0.000	0.000	0.000	0.000
88	A	89	GLY	0	-0.014	0.004	11.284	2.111	2.111	0.000	0.000	0.000	0.000
89	A	90	VAL	0	-0.055	-0.019	9.428	1.540	1.540	0.000	0.000	0.000	0.000
90	A	91	THR	0	0.029	0.010	9.953	-2.784	-2.784	0.000	0.000	0.000	0.000
91	A	92	ASN	0	0.067	0.011	12.516	1.077	1.077	0.000	0.000	0.000	0.000
92	A	93	ASN	0	-0.051	-0.032	11.608	-1.517	-1.517	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.821	-0.898	8.325	27.926	27.926	0.000	0.000	0.000	0.000
94	A	95	ILE	0	0.024	0.028	11.847	1.094	1.094	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.037	-0.019	14.911	-1.064	-1.064	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.039	0.027	17.797	0.306	0.306	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.040	-0.033	19.843	-0.737	-0.737	0.000	0.000	0.000	0.000
98	A	99	PHE	0	0.066	0.044	21.530	-0.519	-0.519	0.000	0.000	0.000	0.000
99	A	100	HIS	0	-0.022	-0.007	24.295	-0.445	-0.445	0.000	0.000	0.000	0.000
100	A	101	PRO	0	0.035	0.013	25.556	0.420	0.420	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.019	-0.008	24.968	0.129	0.129	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.943	-0.966	25.798	10.457	10.457	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.010	-0.010	27.628	-0.266	-0.266	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.894	0.968	21.719	-13.557	-13.557	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.893	0.969	23.759	-10.174	-10.174	0.000	0.000	0.000	0.000
106	A	107	PHE	0	-0.051	-0.029	24.978	-0.221	-0.221	0.000	0.000	0.000	0.000
107	A	108	THR	0	-0.041	-0.016	23.092	-0.049	-0.049	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.898	-0.938	21.762	12.497	12.497	0.000	0.000	0.000	0.000
109	A	110	PHE	0	-0.016	-0.017	17.554	0.761	0.761	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.005	0.017	15.951	-0.549	-0.549	0.000	0.000	0.000	0.000
111	A	112	THR	0	0.004	-0.019	18.029	-0.522	-0.522	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.011	0.016	15.383	-0.208	-0.208	0.000	0.000	0.000	0.000

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