FMO DATABASE

FMODB ID: XV2L1

Calculation Name: 2NLV-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2NLV

Chain ID: A

ChEMBL ID:

UniProt ID: Q3M6F6

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	116
LigandCharge	CL-=-1
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-959297.557826
FMO2-HF: Nuclear repulsion	910951.490587
FMO2-HF: Total energy	-48346.067238
FMO2-MP2: Total energy	-48481.292176

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:GLY)

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

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.
-63.347	-60.664	0.993	-1.291	-2.384	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.872 / q_NPA : 0.919

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	ASP	-1	-0.842	-0.916	3.801	-40.485	-39.267	-0.004	-0.466	-0.748	-0.002
4	A	3	LYS	1	0.880	0.947	2.452	67.564	68.702	0.998	-0.727	-1.409	-0.007
5	A	4	LEU	0	0.028	0.026	4.122	6.881	7.208	-0.001	-0.098	-0.227	0.000
6	A	5	VAL	0	0.057	0.019	5.683	6.190	6.190	0.000	0.000	0.000	0.000
7	A	6	LYS	1	0.961	0.987	7.686	37.528	37.528	0.000	0.000	0.000	0.000
8	A	7	TYR	0	-0.056	-0.078	7.192	3.059	3.059	0.000	0.000	0.000	0.000
9	A	8	GLN	0	-0.026	-0.023	9.670	2.547	2.547	0.000	0.000	0.000	0.000
10	A	9	GLU	-1	-0.944	-0.968	11.711	-18.511	-18.511	0.000	0.000	0.000	0.000
11	A	10	LEU	0	-0.049	-0.015	11.996	2.002	2.002	0.000	0.000	0.000	0.000
12	A	11	VAL	0	0.008	0.012	13.349	1.579	1.579	0.000	0.000	0.000	0.000
13	A	12	LYS	1	0.957	0.982	15.031	21.840	21.840	0.000	0.000	0.000	0.000
14	A	13	LYS	1	0.961	1.001	17.410	17.111	17.111	0.000	0.000	0.000	0.000
15	A	14	LEU	0	-0.031	0.004	18.519	1.073	1.073	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.019	0.001	19.091	0.812	0.812	0.000	0.000	0.000	0.000
17	A	16	THR	0	0.009	-0.001	21.490	0.810	0.810	0.000	0.000	0.000	0.000
18	A	17	ASN	0	-0.059	-0.027	23.055	0.600	0.600	0.000	0.000	0.000	0.000
19	A	18	TYR	0	-0.048	-0.089	22.507	0.481	0.481	0.000	0.000	0.000	0.000
20	A	19	ALA	0	0.030	0.017	25.679	0.442	0.442	0.000	0.000	0.000	0.000
21	A	20	SER	0	-0.085	-0.046	27.494	0.499	0.499	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.933	-0.948	29.338	-10.322	-10.322	0.000	0.000	0.000	0.000
23	A	22	ASP	-1	-0.886	-0.940	31.098	-9.378	-9.378	0.000	0.000	0.000	0.000
24	A	23	VAL	0	-0.038	-0.016	32.529	0.198	0.198	0.000	0.000	0.000	0.000
25	A	24	SER	0	-0.136	-0.072	35.179	0.361	0.361	0.000	0.000	0.000	0.000
26	A	25	ASP	-1	-0.824	-0.930	37.067	-7.532	-7.532	0.000	0.000	0.000	0.000
27	A	26	GLN	0	-0.067	-0.044	38.647	-0.141	-0.141	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.944	-0.947	40.024	-7.486	-7.486	0.000	0.000	0.000	0.000
29	A	28	VAL	0	-0.123	-0.082	35.227	-0.047	-0.047	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.858	-0.915	33.291	-9.479	-9.479	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.025	-0.020	29.135	-0.123	-0.123	0.000	0.000	0.000	0.000
32	A	31	GLN	0	-0.009	-0.008	28.123	-0.390	-0.390	0.000	0.000	0.000	0.000
33	A	32	LEU	0	-0.005	-0.014	22.980	-0.425	-0.425	0.000	0.000	0.000	0.000
34	A	33	ILE	0	-0.018	0.004	22.464	-0.087	-0.087	0.000	0.000	0.000	0.000
35	A	34	LEU	0	-0.018	-0.025	18.774	-0.975	-0.975	0.000	0.000	0.000	0.000
36	A	35	ASP	-1	-0.785	-0.870	17.878	-17.205	-17.205	0.000	0.000	0.000	0.000
37	A	36	THR	0	0.036	-0.031	14.380	-0.600	-0.600	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.954	-0.945	13.398	-20.404	-20.404	0.000	0.000	0.000	0.000
39	A	38	ARG	1	0.787	0.863	13.645	15.733	15.733	0.000	0.000	0.000	0.000
40	A	39	ASN	0	-0.002	0.029	10.270	-0.652	-0.652	0.000	0.000	0.000	0.000
41	A	40	HIS	1	0.858	0.910	13.869	18.020	18.020	0.000	0.000	0.000	0.000
42	A	41	TYR	0	-0.020	-0.017	12.655	0.326	0.326	0.000	0.000	0.000	0.000
43	A	42	GLN	0	0.033	-0.002	18.654	0.453	0.453	0.000	0.000	0.000	0.000
44	A	43	TRP	0	0.033	0.029	22.221	-0.230	-0.230	0.000	0.000	0.000	0.000
45	A	44	MET	0	-0.037	-0.015	25.150	0.116	0.116	0.000	0.000	0.000	0.000
46	A	45	ASN	0	-0.042	-0.004	28.373	0.083	0.083	0.000	0.000	0.000	0.000
47	A	46	VAL	0	-0.010	-0.017	31.392	0.087	0.087	0.000	0.000	0.000	0.000
48	A	47	GLY	0	0.026	0.016	34.171	0.081	0.081	0.000	0.000	0.000	0.000
49	A	48	TRP	0	-0.050	-0.027	37.945	0.038	0.038	0.000	0.000	0.000	0.000
50	A	49	GLN	0	0.110	0.071	39.976	-0.126	-0.126	0.000	0.000	0.000	0.000
51	A	50	GLY	0	0.033	0.012	43.336	0.115	0.115	0.000	0.000	0.000	0.000
52	A	51	LEU	0	-0.040	-0.038	45.561	-0.072	-0.072	0.000	0.000	0.000	0.000
53	A	52	ASN	0	-0.052	-0.019	42.842	0.002	0.002	0.000	0.000	0.000	0.000
54	A	53	ARG	1	0.908	0.967	36.238	8.604	8.604	0.000	0.000	0.000	0.000
55	A	54	ILE	0	-0.025	-0.008	35.348	-0.051	-0.051	0.000	0.000	0.000	0.000
56	A	55	TYR	0	-0.011	-0.020	30.198	-0.074	-0.074	0.000	0.000	0.000	0.000
57	A	56	ARG	1	0.937	0.979	31.443	9.856	9.856	0.000	0.000	0.000	0.000
58	A	57	CYS	0	-0.025	-0.006	25.235	-0.294	-0.294	0.000	0.000	0.000	0.000
59	A	58	VAL	0	-0.008	0.005	27.442	0.092	0.092	0.000	0.000	0.000	0.000
60	A	59	ILE	0	0.035	0.012	21.139	-0.136	-0.136	0.000	0.000	0.000	0.000
61	A	60	HIS	0	-0.012	-0.018	18.972	0.608	0.608	0.000	0.000	0.000	0.000
62	A	61	PHE	0	0.010	-0.006	15.631	-0.241	-0.241	0.000	0.000	0.000	0.000
63	A	62	ASP	-1	-0.792	-0.864	14.891	-17.534	-17.534	0.000	0.000	0.000	0.000
64	A	63	ILE	0	-0.043	-0.020	8.377	-1.101	-1.101	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.880	0.945	10.783	19.784	19.784	0.000	0.000	0.000	0.000
66	A	65	ASP	-1	-0.884	-0.939	8.152	-28.747	-28.747	0.000	0.000	0.000	0.000
67	A	66	GLY	0	-0.088	-0.048	5.200	-3.960	-3.960	0.000	0.000	0.000	0.000
68	A	67	LYS	1	0.882	0.955	6.107	25.341	25.341	0.000	0.000	0.000	0.000
69	A	68	ILE	0	0.003	0.003	9.202	1.228	1.228	0.000	0.000	0.000	0.000
70	A	69	TRP	0	0.003	0.004	11.993	1.709	1.709	0.000	0.000	0.000	0.000
71	A	70	LEU	0	0.008	0.002	15.247	0.214	0.214	0.000	0.000	0.000	0.000
72	A	71	GLN	0	-0.038	-0.048	18.064	0.793	0.793	0.000	0.000	0.000	0.000
73	A	72	GLN	0	0.011	0.006	20.980	0.504	0.504	0.000	0.000	0.000	0.000
74	A	73	ASN	0	0.020	0.002	23.272	-0.408	-0.408	0.000	0.000	0.000	0.000
75	A	74	LEU	0	-0.077	-0.016	25.542	0.372	0.372	0.000	0.000	0.000	0.000
76	A	75	THR	0	-0.043	-0.033	26.873	0.369	0.369	0.000	0.000	0.000	0.000
77	A	76	ASP	-1	-0.919	-0.952	29.357	-9.957	-9.957	0.000	0.000	0.000	0.000
78	A	77	ARG	1	0.861	0.909	23.997	12.641	12.641	0.000	0.000	0.000	0.000
79	A	78	ASN	0	-0.010	-0.013	23.074	-0.553	-0.553	0.000	0.000	0.000	0.000
80	A	79	PRO	0	0.067	0.025	20.362	-0.444	-0.444	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.000	0.004	18.329	-0.873	-0.873	0.000	0.000	0.000	0.000
82	A	81	GLU	-1	-0.767	-0.826	18.432	-15.745	-15.745	0.000	0.000	0.000	0.000
83	A	82	GLU	-1	-0.783	-0.843	20.448	-13.752	-13.752	0.000	0.000	0.000	0.000
84	A	83	LEU	0	0.020	-0.005	14.653	-0.632	-0.632	0.000	0.000	0.000	0.000
85	A	84	VAL	0	-0.012	0.005	15.732	-1.019	-1.019	0.000	0.000	0.000	0.000
86	A	85	MET	0	-0.080	-0.019	17.031	-0.310	-0.310	0.000	0.000	0.000	0.000
87	A	86	MET	0	-0.077	-0.044	16.233	0.349	0.349	0.000	0.000	0.000	0.000
88	A	87	GLY	0	-0.033	-0.011	13.726	-1.168	-1.168	0.000	0.000	0.000	0.000
89	A	88	VAL	0	-0.073	-0.043	10.784	-2.521	-2.521	0.000	0.000	0.000	0.000
90	A	89	PRO	0	-0.005	0.012	9.463	1.966	1.966	0.000	0.000	0.000	0.000
91	A	90	ARG	1	0.916	0.937	12.642	15.428	15.428	0.000	0.000	0.000	0.000
92	A	91	GLU	-1	-0.879	-0.955	11.596	-23.035	-23.035	0.000	0.000	0.000	0.000
93	A	92	ASP	-1	-0.882	-0.914	7.748	-38.984	-38.984	0.000	0.000	0.000	0.000
94	A	93	ILE	0	-0.027	-0.011	10.831	-0.731	-0.731	0.000	0.000	0.000	0.000
95	A	94	VAL	0	0.043	0.023	13.290	0.808	0.808	0.000	0.000	0.000	0.000
96	A	95	LEU	0	-0.009	-0.017	15.878	0.342	0.342	0.000	0.000	0.000	0.000
97	A	96	GLY	0	0.036	0.023	18.878	0.579	0.579	0.000	0.000	0.000	0.000
98	A	97	LEU	0	-0.015	0.001	20.133	0.594	0.594	0.000	0.000	0.000	0.000
99	A	98	GLN	0	-0.055	-0.026	22.728	1.030	1.030	0.000	0.000	0.000	0.000
100	A	99	ALA	0	0.007	0.000	23.518	-0.315	-0.315	0.000	0.000	0.000	0.000
101	A	100	PRO	0	0.076	0.018	22.420	-0.049	-0.049	0.000	0.000	0.000	0.000
102	A	101	TYR	0	-0.004	0.001	23.002	-0.269	-0.269	0.000	0.000	0.000	0.000
103	A	102	LYS	1	0.949	0.975	25.173	11.573	11.573	0.000	0.000	0.000	0.000
104	A	103	ARG	1	0.822	0.895	18.987	15.349	15.349	0.000	0.000	0.000	0.000
105	A	104	GLN	0	0.005	0.012	20.178	-0.151	-0.151	0.000	0.000	0.000	0.000
106	A	105	TYR	0	-0.081	-0.035	21.200	0.125	0.125	0.000	0.000	0.000	0.000
107	A	106	THR	0	-0.104	-0.059	20.562	0.386	0.386	0.000	0.000	0.000	0.000
108	A	107	ASP	-1	-0.887	-0.938	21.394	-13.533	-13.533	0.000	0.000	0.000	0.000
109	A	108	TYR	0	-0.138	-0.136	16.771	-0.276	-0.276	0.000	0.000	0.000	0.000
110	A	109	GLY	0	0.019	0.020	14.673	0.085	0.085	0.000	0.000	0.000	0.000
111	A	110	VAL	0	-0.063	-0.029	14.814	1.167	1.167	0.000	0.000	0.000	0.000
112	A	111	ALA	-1	-0.862	-0.952	12.441	-25.613	-25.613	0.000	0.000	0.000	0.000
113	A	112	CL-	-1	-0.893	-0.922	17.941	-17.536	-17.536	0.000	0.000	0.000	0.000
114	A	113	CL-	-1	-0.858	-0.912	30.013	-10.753	-10.753	0.000	0.000	0.000	0.000
115	A	114	CL-	-1	-0.870	-0.913	21.208	-14.966	-14.966	0.000	0.000	0.000	0.000
116	A	115	CL-	-1	-0.902	-0.944	28.504	-11.473	-11.473	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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