FMO DATABASE

FMODB ID: XMMMZ

Calculation Name: 2NT4-A-Xray13

Preferred Name:

Target Type:

Ligand Name: chloride ion

ligand 3-letter code: CL

PDB ID: 2NT4

Chain ID: A

ChEMBL ID:

UniProt ID: O68522

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. 1.20171117

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	128
LigandResidueName
LigandFragmentNumber	0
LigandCharge	CL-=-1
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1048690.188166
FMO2-HF: Nuclear repulsion	1000771.284573
FMO2-HF: Total energy	-47918.903592
FMO2-MP2: Total energy	-48059.341147

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:ACE)

Summations of interaction energy for fragment #1(A:-2: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.
-0.919	0.893	-0.011	-0.869	-0.931	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.019 / q_NPA : -0.001

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	0	HIS	0	-0.066	-0.027	3.631	-0.494	1.318	-0.011	-0.869	-0.931	-0.003
4	A	1	MET	0	-0.073	-0.015	5.682	0.071	0.071	0.000	0.000	0.000	0.000
5	A	2	SER	0	-0.016	-0.015	9.280	0.090	0.090	0.000	0.000	0.000	0.000
6	A	3	LYS	1	0.789	0.876	12.228	0.331	0.331	0.000	0.000	0.000	0.000
7	A	4	LYS	1	0.868	0.934	14.754	0.154	0.154	0.000	0.000	0.000	0.000
8	A	5	ILE	0	0.007	0.008	17.617	-0.006	-0.006	0.000	0.000	0.000	0.000
9	A	6	LEU	0	-0.004	0.007	20.111	0.012	0.012	0.000	0.000	0.000	0.000
10	A	7	ILE	0	-0.010	-0.009	21.933	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	8	VAL	0	-0.014	-0.016	25.446	0.004	0.004	0.000	0.000	0.000	0.000
12	A	9	GLU	-1	-0.736	-0.877	28.865	0.001	0.001	0.000	0.000	0.000	0.000
13	A	10	SER	0	0.006	-0.005	30.723	0.002	0.002	0.000	0.000	0.000	0.000
14	A	11	ASP	-1	-0.920	-0.944	31.760	0.022	0.022	0.000	0.000	0.000	0.000
15	A	12	THR	0	0.042	-0.005	29.660	0.001	0.001	0.000	0.000	0.000	0.000
16	A	13	ALA	0	-0.007	0.016	28.503	0.005	0.005	0.000	0.000	0.000	0.000
17	A	14	LEU	0	-0.004	0.000	26.894	0.005	0.005	0.000	0.000	0.000	0.000
18	A	15	SER	0	0.007	-0.026	25.839	0.001	0.001	0.000	0.000	0.000	0.000
19	A	16	ALA	0	0.019	0.017	24.031	0.003	0.003	0.000	0.000	0.000	0.000
20	A	17	THR	0	-0.048	-0.019	22.629	0.011	0.011	0.000	0.000	0.000	0.000
21	A	18	LEU	0	-0.032	-0.028	21.576	0.005	0.005	0.000	0.000	0.000	0.000
22	A	19	ARG	1	0.916	0.952	19.792	-0.059	-0.059	0.000	0.000	0.000	0.000
23	A	20	SER	0	-0.004	0.010	18.176	0.012	0.012	0.000	0.000	0.000	0.000
24	A	21	ALA	0	0.000	-0.002	16.681	0.017	0.017	0.000	0.000	0.000	0.000
25	A	22	LEU	0	-0.046	-0.029	15.802	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	23	GLU	-1	-0.900	-0.956	14.085	0.086	0.086	0.000	0.000	0.000	0.000
27	A	24	GLY	0	-0.037	-0.004	12.240	0.039	0.039	0.000	0.000	0.000	0.000
28	A	25	ARG	1	0.849	0.921	10.605	0.029	0.029	0.000	0.000	0.000	0.000
29	A	26	GLY	0	0.086	0.045	9.279	-0.077	-0.077	0.000	0.000	0.000	0.000
30	A	27	PHE	0	-0.033	-0.031	10.167	-0.058	-0.058	0.000	0.000	0.000	0.000
31	A	28	THR	0	-0.038	-0.014	13.290	0.037	0.037	0.000	0.000	0.000	0.000
32	A	29	VAL	0	-0.016	-0.017	15.254	-0.022	-0.022	0.000	0.000	0.000	0.000
33	A	30	ASP	-1	-0.853	-0.912	18.680	0.022	0.022	0.000	0.000	0.000	0.000
34	A	31	GLU	-1	-0.880	-0.940	22.114	0.027	0.027	0.000	0.000	0.000	0.000
35	A	32	THR	0	-0.002	0.007	25.419	0.003	0.003	0.000	0.000	0.000	0.000
36	A	33	THR	0	0.022	0.005	29.098	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	34	ASP	-1	-0.888	-0.938	32.272	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	35	GLY	0	0.052	0.014	33.749	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.901	0.962	35.105	0.007	0.007	0.000	0.000	0.000	0.000
40	A	37	GLY	0	-0.008	-0.010	34.997	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	38	SER	0	-0.013	-0.005	31.339	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	39	VAL	0	-0.005	-0.009	31.233	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	40	GLU	-1	-0.810	-0.903	32.170	-0.029	-0.029	0.000	0.000	0.000	0.000
44	A	41	GLN	0	-0.035	-0.005	26.683	0.000	0.000	0.000	0.000	0.000	0.000
45	A	42	ILE	0	0.034	0.016	27.292	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	43	ARG	1	0.768	0.868	27.726	0.029	0.029	0.000	0.000	0.000	0.000
47	A	44	ARG	1	0.873	0.944	29.045	0.011	0.011	0.000	0.000	0.000	0.000
48	A	45	ASP	-1	-0.860	-0.944	24.161	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	46	ARG	1	0.696	0.848	23.397	0.052	0.052	0.000	0.000	0.000	0.000
50	A	47	PRO	0	-0.017	-0.002	21.386	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	48	ASP	-1	-0.810	-0.911	18.001	-0.147	-0.147	0.000	0.000	0.000	0.000
52	A	49	LEU	0	-0.017	-0.003	20.554	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	50	VAL	0	-0.011	-0.002	22.457	0.008	0.008	0.000	0.000	0.000	0.000
54	A	51	VAL	0	-0.003	0.008	23.050	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	52	LEU	0	-0.024	-0.017	25.870	0.005	0.005	0.000	0.000	0.000	0.000
56	A	53	ALA	0	0.043	0.024	29.645	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	54	VAL	0	-0.056	-0.029	32.088	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	55	ASP	-1	-0.903	-0.975	35.594	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	56	LEU	0	-0.041	-0.002	33.034	0.002	0.002	0.000	0.000	0.000	0.000
60	A	57	SER	0	0.039	0.014	36.982	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	58	ALA	0	-0.024	-0.033	39.043	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	59	GLY	0	-0.010	0.000	41.966	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	60	GLN	0	-0.051	-0.020	37.937	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	61	ASN	0	0.089	0.035	38.588	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	62	GLY	0	0.078	0.029	34.905	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	63	TYR	0	0.022	0.004	35.382	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	64	LEU	0	-0.053	-0.026	37.609	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	65	ILE	0	-0.027	-0.005	33.534	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	66	CYS	0	0.047	0.036	33.277	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	67	GLY	0	-0.005	-0.009	34.572	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	68	LYS	1	0.884	0.931	37.085	0.019	0.019	0.000	0.000	0.000	0.000
72	A	69	LEU	0	0.056	0.034	30.731	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	70	LYS	1	0.834	0.926	29.646	0.057	0.057	0.000	0.000	0.000	0.000
74	A	71	LYS	1	0.831	0.913	35.121	0.028	0.028	0.000	0.000	0.000	0.000
75	A	72	ASP	-1	-0.815	-0.888	34.786	-0.039	-0.039	0.000	0.000	0.000	0.000
76	A	73	ASP	-1	-0.941	-0.994	34.741	-0.047	-0.047	0.000	0.000	0.000	0.000
77	A	74	ASP	-1	-0.874	-0.916	31.360	-0.062	-0.062	0.000	0.000	0.000	0.000
78	A	75	LEU	0	-0.026	-0.010	29.790	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	76	LYS	1	0.910	0.975	30.305	0.050	0.050	0.000	0.000	0.000	0.000
80	A	77	ASN	0	-0.056	-0.043	28.123	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	78	VAL	0	0.006	0.022	24.906	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	79	PRO	0	0.004	0.011	22.831	0.009	0.009	0.000	0.000	0.000	0.000
83	A	80	ILE	0	-0.021	-0.026	25.460	0.005	0.005	0.000	0.000	0.000	0.000
84	A	81	VAL	0	0.049	0.022	23.952	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	82	ILE	0	-0.049	-0.025	27.158	0.005	0.005	0.000	0.000	0.000	0.000
86	A	83	ILE	0	0.010	0.008	27.377	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	84	GLY	0	0.071	0.004	30.522	0.002	0.002	0.000	0.000	0.000	0.000
88	A	85	ASN	0	0.042	0.029	33.936	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	86	PRO	0	0.033	0.004	35.125	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	87	ASP	-1	-0.927	-0.950	36.734	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	88	GLY	0	-0.021	-0.005	39.393	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	89	PHE	0	0.003	0.007	32.971	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	90	ALA	0	-0.022	-0.018	37.208	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	91	GLN	0	-0.037	-0.034	39.383	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	92	PHE	0	0.038	0.022	34.876	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	93	ARG	1	0.961	0.983	34.300	0.031	0.031	0.000	0.000	0.000	0.000
97	A	94	LYS	1	0.908	0.963	37.671	0.024	0.024	0.000	0.000	0.000	0.000
98	A	95	LEU	0	-0.036	0.003	40.073	0.001	0.001	0.000	0.000	0.000	0.000
99	A	96	LYS	1	0.947	0.964	39.534	0.033	0.033	0.000	0.000	0.000	0.000
100	A	97	ALA	0	-0.039	-0.002	37.341	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	98	HIS	0	-0.048	-0.027	34.028	0.001	0.001	0.000	0.000	0.000	0.000
102	A	99	ALA	0	0.040	-0.008	30.644	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	100	ASP	-1	-0.833	-0.897	27.430	-0.066	-0.066	0.000	0.000	0.000	0.000
104	A	101	GLU	-1	-0.847	-0.911	25.579	-0.055	-0.055	0.000	0.000	0.000	0.000
105	A	102	TYR	0	-0.052	-0.048	28.544	0.005	0.005	0.000	0.000	0.000	0.000
106	A	103	VAL	0	0.005	0.000	25.788	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	104	ALA	0	-0.007	-0.010	29.241	0.002	0.002	0.000	0.000	0.000	0.000
108	A	105	LYS	1	0.794	0.885	30.946	0.000	0.000	0.000	0.000	0.000	0.000
109	A	106	PRO	0	-0.036	-0.044	32.334	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	107	VAL	0	0.023	0.025	25.955	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	108	ASP	-1	-0.879	-0.921	24.413	0.022	0.022	0.000	0.000	0.000	0.000
112	A	109	ALA	0	0.027	-0.011	21.603	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	110	ASP	-1	-0.877	-0.937	20.189	0.023	0.023	0.000	0.000	0.000	0.000
114	A	111	GLN	0	-0.033	-0.022	20.831	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	112	LEU	0	-0.014	-0.003	21.486	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	113	VAL	0	0.024	0.003	16.187	-0.013	-0.013	0.000	0.000	0.000	0.000
117	A	114	GLU	-1	-0.968	-0.988	18.204	-0.089	-0.089	0.000	0.000	0.000	0.000
118	A	115	ARG	1	0.881	0.945	19.671	0.031	0.031	0.000	0.000	0.000	0.000
119	A	116	ALA	0	-0.013	-0.001	18.597	-0.010	-0.010	0.000	0.000	0.000	0.000
120	A	117	GLY	0	0.011	0.002	16.351	-0.018	-0.018	0.000	0.000	0.000	0.000
121	A	118	ALA	0	-0.043	-0.014	17.053	-0.029	-0.029	0.000	0.000	0.000	0.000
122	A	119	LEU	0	-0.046	-0.017	19.906	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	120	ILE	0	-0.012	0.004	16.888	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	121	GLY	0	0.002	0.021	15.173	-0.042	-0.042	0.000	0.000	0.000	0.000
125	A	122	PHE	0	0.016	-0.022	10.935	0.040	0.040	0.000	0.000	0.000	0.000
126	A	123	PRO	0	-0.003	0.004	9.915	-0.075	-0.075	0.000	0.000	0.000	0.000
127	A	124	GLU	-2	-1.755	-1.832	4.890	-0.788	-0.788	0.000	0.000	0.000	0.000
128	A	125	CL-	-1	-0.847	-0.882	34.989	-0.004	-0.004	0.000	0.000	0.000	0.000

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