FMO DATABASE

FMODB ID: XQ8YY

Calculation Name: 2V7F-A-Xray13

Preferred Name:

Target Type:

Ligand Name: chloride ion

ligand 3-letter code: CL

PDB ID: 2V7F

Chain ID: A

ChEMBL ID:

UniProt ID: Q9V0G8

Base Structure: X-ray

Registration Date: 2018-02-14

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	151
LigandCharge	CL-=-1
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1434346.815181
FMO2-HF: Nuclear repulsion	1375104.824178
FMO2-HF: Total energy	-59241.991003
FMO2-MP2: Total energy	-59419.757628

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:1:ACE)

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

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.
-1.633	-1.172	2.893	-1.742	-1.613	-0.007

Interaction energy analysis for fragmet #1(A:1:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.034 / q_NPA : -0.034

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	3	THR	0	-0.019	-0.004	3.837	1.417	2.024	-0.010	-0.266	-0.331	0.000
4	A	4	VAL	0	0.002	-0.021	6.971	-0.011	-0.011	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.073	-0.044	10.282	0.119	0.119	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.830	-0.890	7.113	-1.770	-1.770	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.023	-0.016	8.477	-0.012	-0.012	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.027	0.028	11.185	0.078	0.078	0.000	0.000	0.000	0.000
9	A	9	GLY	0	-0.022	-0.035	14.526	0.006	0.006	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.878	-0.932	16.381	-0.234	-0.234	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.070	0.022	15.026	0.016	0.016	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.011	0.017	10.610	0.025	0.025	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.067	-0.046	13.830	0.045	0.045	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.889	-0.937	17.003	-0.121	-0.121	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.766	0.844	13.258	0.207	0.207	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.013	-0.019	13.193	0.039	0.039	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.010	-0.006	15.368	0.032	0.032	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.002	-0.006	17.460	0.031	0.031	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.858	0.917	11.387	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.057	-0.040	17.124	0.016	0.016	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.823	0.909	19.568	0.042	0.042	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.954	-0.961	18.428	0.060	0.060	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.087	-0.033	17.591	0.010	0.010	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.054	0.024	21.888	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.923	-0.978	24.093	0.020	0.020	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.092	-0.046	21.716	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.962	0.987	25.110	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.019	-0.006	27.605	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.077	-0.032	29.778	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.878	-0.934	32.709	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	31	TRP	0	-0.088	-0.078	32.686	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.010	-0.016	31.972	0.000	0.000	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.091	0.044	33.333	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	34	PHE	0	-0.034	0.003	35.957	0.001	0.001	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.108	-0.049	36.126	0.000	0.000	0.000	0.000	0.000	0.000
36	A	36	LYS	1	1.017	1.000	37.433	0.027	0.027	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.046	-0.024	38.210	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.050	0.023	35.382	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.710	0.828	28.120	0.084	0.084	0.000	0.000	0.000	0.000
40	A	40	HIS	0	0.069	0.035	34.135	0.002	0.002	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.912	0.931	31.447	0.073	0.073	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.785	-0.861	31.737	-0.058	-0.058	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.896	0.940	29.862	0.049	0.049	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.034	0.026	26.793	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	PRO	0	0.119	0.046	24.269	0.002	0.002	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.843	-0.888	24.389	-0.105	-0.105	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.081	-0.055	25.657	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.895	-0.945	28.594	-0.035	-0.035	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.826	-0.884	24.735	-0.041	-0.041	0.000	0.000	0.000	0.000
50	A	50	TRP	0	-0.002	-0.011	25.407	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	TRP	0	-0.026	-0.030	26.055	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.070	0.034	21.999	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.087	0.036	21.444	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.829	0.936	21.993	0.075	0.075	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.023	-0.004	21.138	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.066	0.046	17.834	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.044	-0.003	18.245	-0.020	-0.020	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.040	-0.031	20.063	-0.012	-0.012	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.026	0.015	15.949	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.994	1.000	14.789	0.324	0.324	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.848	0.926	16.774	0.165	0.165	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.015	-0.018	19.672	0.002	0.002	0.000	0.000	0.000	0.000
63	A	63	TYR	0	-0.097	-0.073	9.581	0.010	0.010	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.076	-0.028	15.007	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.863	-0.923	17.657	-0.158	-0.158	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.088	-0.018	20.235	0.018	0.018	0.000	0.000	0.000	0.000
67	A	67	PRO	0	0.007	-0.008	21.464	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.007	-0.005	23.474	0.000	0.000	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.058	0.034	25.951	0.007	0.007	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.019	-0.007	28.734	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.687	-0.811	30.374	-0.053	-0.053	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.947	0.988	25.089	0.103	0.103	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.041	0.025	24.126	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.807	0.891	28.075	0.049	0.049	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.041	-0.032	31.218	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	76	TYR	0	0.016	0.018	24.027	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	77	TYR	0	0.014	-0.017	22.644	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.084	-0.013	29.106	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.067	0.027	32.831	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.873	0.907	34.918	0.058	0.058	0.000	0.000	0.000	0.000
81	A	81	LYS	1	1.022	1.016	36.992	0.045	0.045	0.000	0.000	0.000	0.000
82	A	82	ASN	0	0.033	0.005	38.578	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.848	0.935	30.675	0.086	0.086	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.035	0.032	36.552	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	85	HIS	0	0.026	0.009	33.937	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	86	ALA	0	-0.023	-0.038	37.713	0.003	0.003	0.000	0.000	0.000	0.000
87	A	87	PRO	0	-0.026	-0.018	36.376	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.868	-0.924	37.966	-0.026	-0.026	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.907	0.975	40.590	0.035	0.035	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.024	-0.001	40.367	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	91	TYR	0	-0.056	-0.020	34.174	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	92	LYS	1	1.010	1.001	38.942	0.034	0.034	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.055	0.017	36.149	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.035	0.015	33.186	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.060	0.006	32.235	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.047	-0.030	32.947	0.001	0.001	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.042	0.041	28.892	0.002	0.002	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.031	0.003	27.399	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.933	0.950	28.400	0.032	0.032	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.980	1.017	29.708	0.026	0.026	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.041	0.016	24.932	0.003	0.003	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.024	-0.015	24.243	0.002	0.002	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.007	-0.005	25.943	0.005	0.005	0.000	0.000	0.000	0.000
104	A	104	GLN	0	0.028	0.019	25.652	0.002	0.002	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.022	0.012	19.893	0.005	0.005	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.871	-0.934	22.188	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.021	0.006	24.537	0.007	0.007	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.054	0.040	20.942	0.007	0.007	0.000	0.000	0.000	0.000
109	A	109	GLY	0	-0.007	0.005	20.671	0.013	0.013	0.000	0.000	0.000	0.000
110	A	110	PHE	0	-0.010	-0.007	16.419	0.005	0.005	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.017	-0.010	18.504	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.847	-0.922	21.260	0.010	0.010	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.844	0.901	24.154	0.004	0.004	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.081	0.048	24.931	0.006	0.006	0.000	0.000	0.000	0.000
115	A	115	PRO	0	0.029	-0.007	27.819	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	116	GLY	0	0.023	0.017	31.312	0.000	0.000	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.912	0.969	27.166	0.042	0.042	0.000	0.000	0.000	0.000
118	A	118	GLY	0	-0.002	-0.004	27.404	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.801	0.885	23.794	0.043	0.043	0.000	0.000	0.000	0.000
120	A	120	VAL	0	0.046	0.027	20.731	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	121	ILE	0	-0.010	0.003	14.927	0.008	0.008	0.000	0.000	0.000	0.000
122	A	122	THR	0	0.023	0.010	18.026	0.003	0.003	0.000	0.000	0.000	0.000
123	A	123	PRO	0	0.041	0.005	14.649	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.879	0.954	13.501	-0.049	-0.049	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.078	0.023	13.889	0.008	0.008	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.927	0.964	10.746	0.131	0.131	0.000	0.000	0.000	0.000
127	A	127	SER	0	0.036	0.018	9.143	-0.025	-0.025	0.000	0.000	0.000	0.000
128	A	128	PHE	0	-0.030	-0.008	9.011	0.029	0.029	0.000	0.000	0.000	0.000
129	A	129	LEU	0	0.005	-0.012	10.325	-0.015	-0.015	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.755	-0.865	5.836	-0.563	-0.563	0.000	0.000	0.000	0.000
131	A	131	LYS	1	0.924	0.970	5.348	-0.625	-0.625	0.000	0.000	0.000	0.000
132	A	132	ILE	0	0.030	0.017	6.610	-0.012	-0.012	0.000	0.000	0.000	0.000
133	A	133	ALA	0	0.003	0.005	6.686	0.007	0.007	0.000	0.000	0.000	0.000
134	A	134	THR	0	-0.037	-0.021	2.472	-0.830	-1.144	2.904	-1.438	-1.152	-0.007
135	A	135	GLU	-1	-0.882	-0.930	4.404	0.265	0.326	-0.001	-0.011	-0.050	0.000
136	A	136	LEU	0	0.029	0.023	7.559	0.003	0.003	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.898	0.956	5.831	1.260	1.260	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.950	0.968	3.884	-1.392	-1.285	0.000	-0.027	-0.080	0.000
139	A	139	GLU	-1	-0.737	-0.824	7.932	-0.106	-0.106	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.056	-0.036	11.126	0.032	0.032	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.938	-0.989	8.472	-0.600	-0.600	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.973	-0.959	11.542	0.023	0.023	0.000	0.000	0.000	0.000
143	A	143	ILE	0	0.005	-0.008	13.510	0.023	0.023	0.000	0.000	0.000	0.000
144	A	144	ILE	0	-0.051	-0.031	15.608	0.018	0.018	0.000	0.000	0.000	0.000
145	A	145	PRO	0	-0.062	-0.038	15.001	0.020	0.020	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.899	-0.935	17.484	-0.067	-0.067	0.000	0.000	0.000	0.000
147	A	147	LEU	0	-0.094	-0.018	20.001	0.018	0.018	0.000	0.000	0.000	0.000
148	A	148	LYS	1	0.855	0.919	22.398	0.054	0.054	0.000	0.000	0.000	0.000
149	A	149	LYS	1	0.917	0.950	25.560	0.092	0.092	0.000	0.000	0.000	0.000
150	A	150	TYR	-1	-0.842	-0.909	27.560	-0.060	-0.060	0.000	0.000	0.000	0.000
151	A	1151	CL-	-1	-0.854	-0.902	31.595	-0.037	-0.037	0.000	0.000	0.000	0.000

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