FMO DATABASE

FMODB ID: R12R8

Calculation Name: 7KG3-A-Xray89

Preferred Name:

Target Type:

Ligand Name: 2-(n-morpholino)-ethanesulfonic acid

ligand 3-letter code: MES

PDB ID: 7KG3

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2020-12-21

Reference: T. Ohyama, K. Kamisaka, C. Watanabe, T. Honma et. al., FMO-based interaction energy analysis of SARS-Cov-2 related protein and ligand complexes, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHLSideSolv
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	Waters within average of the temperature factors of receptor.
Procedure	Auto-FMO protocol ver. 1.20200406

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	181
LigandResidueName	MES
LigandFragmentNumber	181
LigandCharge	MES=-1
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1700828.821192
FMO2-HF: Nuclear repulsion	1636766.750108
FMO2-HF: Total energy	-64062.071084
FMO2-MP2: Total energy	-64249.342939

3D Structure

Snapshot

Ligand structure

MES

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.
-180.576	-187.310	86.551	-28.592	-51.230	-0.109

Interactive mode: IFIE and PIEDA for fragment #181(A:203:MES )

Summations of interaction energy for fragment #181(A:203:MES )

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.
-180.576	-187.31	86.551	-28.592	-51.23	0.109

Interaction energy analysis for fragmet #181(A:203:MES )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.891 / q_NPA : -0.876

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].
1	A	2	PRO	1	0.811	0.885	22.197	-12.728	-12.728	0.000	0.000	0.000	0.000
2	A	3	VAL	0	0.055	0.040	23.984	-0.398	-0.398	0.000	0.000	0.000	0.000
3	A	4	ASN	0	0.021	0.014	21.209	0.597	0.597	0.000	0.000	0.000	0.000
4	A	5	SER	0	0.051	0.035	22.830	-0.197	-0.197	0.000	0.000	0.000	0.000
5	A	6	PHE	0	-0.016	-0.007	16.956	0.134	0.134	0.000	0.000	0.000	0.000
6	A	7	SER	0	0.027	0.004	21.886	-0.572	-0.572	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.006	-0.005	21.949	0.558	0.558	0.000	0.000	0.000	0.000
8	A	9	TYR	0	-0.066	-0.046	16.044	0.619	0.619	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.019	0.024	20.311	-0.838	-0.838	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.835	0.922	20.507	-11.725	-11.725	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.004	0.000	17.140	-0.260	-0.260	0.000	0.000	0.000	0.000
12	A	13	THR	0	0.042	0.014	20.667	-0.400	-0.400	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.865	-0.948	22.860	12.033	12.033	0.000	0.000	0.000	0.000
14	A	15	ASN	0	-0.056	-0.037	19.217	-0.608	-0.608	0.000	0.000	0.000	0.000
15	A	16	VAL	0	0.017	0.026	15.974	0.906	0.906	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.004	0.003	17.759	-1.150	-1.150	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.012	0.011	14.004	1.475	1.475	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.821	0.896	15.556	-17.165	-17.165	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.053	-0.016	15.093	0.443	0.443	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.008	-0.022	14.616	-1.392	-1.392	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.821	-0.910	12.902	24.337	24.337	0.000	0.000	0.000	0.000
22	A	23	ILE	0	0.058	0.020	8.985	-1.532	-1.532	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.007	0.007	11.658	-1.196	-1.196	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.819	-0.904	14.050	15.127	15.127	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.792	-0.860	15.204	15.356	15.356	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.040	0.024	14.849	-1.000	-1.000	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.797	0.871	16.897	-17.442	-17.442	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.849	0.921	19.429	-16.504	-16.504	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.030	-0.001	19.046	-0.650	-0.650	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.831	0.923	19.313	-15.574	-15.574	0.000	0.000	0.000	0.000
31	A	32	PRO	0	0.052	0.031	16.715	-0.731	-0.731	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.020	-0.023	19.322	-0.390	-0.390	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.009	-0.007	14.529	-0.168	-0.168	0.000	0.000	0.000	0.000
34	A	35	VAL	0	-0.014	0.003	11.418	0.033	0.033	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.007	0.009	8.347	-0.256	-0.256	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.027	-0.040	4.804	4.822	4.963	-0.001	-0.004	-0.136	0.000
37	A	38	ALA	0	-0.008	0.020	2.676	-3.924	-2.354	1.553	-1.050	-2.073	0.013
38	A	39	ALA	0	0.051	0.016	2.391	-3.062	-1.196	4.057	-2.133	-3.791	-0.033
39	A	40	ASN	0	0.029	-0.008	1.903	-9.687	-10.527	11.346	-3.859	-6.647	0.021
40	A	41	VAL	0	0.025	0.005	3.748	-2.365	-2.014	0.015	-0.040	-0.326	0.000
41	A	42	TYR	0	-0.012	-0.001	6.511	-2.320	-2.320	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.005	0.012	5.520	-1.645	-1.645	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.853	0.928	4.899	-23.867	-23.640	-0.001	-0.035	-0.192	0.000
44	A	45	HIS	0	0.036	0.001	2.336	8.819	10.092	1.756	-1.194	-1.835	-0.012
45	A	46	GLY	0	0.006	0.001	2.632	-3.347	-2.703	0.296	-0.057	-0.884	-0.001
46	A	47	GLY	0	0.013	-0.001	2.869	-3.482	-2.838	0.069	-0.182	-0.530	0.000
47	A	48	GLY	0	0.010	0.017	2.983	1.564	2.760	0.182	-0.557	-0.821	-0.006
48	A	49	VAL	0	0.047	0.018	4.285	-7.263	-6.887	0.000	-0.039	-0.337	0.000
49	A	50	ALA	0	0.058	0.045	2.463	-7.278	-6.832	1.498	-0.533	-1.410	-0.002
50	A	51	GLY	0	0.006	0.005	4.177	-4.195	-4.039	0.000	-0.036	-0.120	0.000
51	A	52	ALA	0	-0.032	-0.011	5.818	-3.230	-3.230	0.000	0.000	0.000	0.000
52	A	53	LEU	0	0.047	0.015	7.145	-3.003	-3.003	0.000	0.000	0.000	0.000
53	A	54	ASN	0	0.069	0.021	7.198	-3.062	-3.062	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.948	0.983	9.061	-19.863	-19.863	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.021	0.002	11.502	-1.515	-1.515	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.058	-0.020	11.809	-1.180	-1.180	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.048	-0.033	14.111	-0.746	-0.746	0.000	0.000	0.000	0.000
58	A	59	ASN	0	0.041	0.040	10.999	0.320	0.320	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.017	0.018	12.542	0.045	0.045	0.000	0.000	0.000	0.000
60	A	61	MET	0	0.007	0.016	8.614	0.710	0.710	0.000	0.000	0.000	0.000
61	A	62	GLN	0	-0.015	-0.008	6.667	2.048	2.048	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.009	0.009	9.749	-0.241	-0.241	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.742	-0.846	13.103	16.966	16.966	0.000	0.000	0.000	0.000
64	A	65	SER	0	-0.012	-0.018	8.987	0.425	0.425	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.857	-0.918	10.172	19.545	19.545	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.937	-0.953	12.122	13.170	13.170	0.000	0.000	0.000	0.000
67	A	68	TYR	0	0.042	0.010	12.443	-0.491	-0.491	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.023	-0.021	10.088	-0.255	-0.255	0.000	0.000	0.000	0.000
69	A	70	ALA	0	-0.041	-0.009	13.554	-0.421	-0.421	0.000	0.000	0.000	0.000
70	A	71	THR	0	-0.034	-0.003	16.278	-0.831	-0.831	0.000	0.000	0.000	0.000
71	A	72	ASN	0	-0.103	-0.066	15.849	-0.885	-0.885	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.017	0.010	15.353	-0.063	-0.063	0.000	0.000	0.000	0.000
73	A	74	PRO	0	-0.055	-0.036	11.345	0.623	0.623	0.000	0.000	0.000	0.000
74	A	75	LEU	0	0.014	0.007	8.403	-0.792	-0.792	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.954	0.964	11.429	-16.825	-16.825	0.000	0.000	0.000	0.000
76	A	77	VAL	0	0.018	0.009	8.137	1.181	1.181	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.014	0.014	9.059	-2.065	-2.065	0.000	0.000	0.000	0.000
78	A	79	GLY	0	-0.015	0.003	10.578	-1.517	-1.517	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.034	-0.052	10.202	2.275	2.275	0.000	0.000	0.000	0.000
80	A	81	CYS	0	-0.028	0.004	11.417	-1.173	-1.173	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.014	0.002	12.249	1.251	1.251	0.000	0.000	0.000	0.000
82	A	83	LEU	0	0.006	0.017	11.126	-0.870	-0.870	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.041	0.013	14.802	-0.025	-0.025	0.000	0.000	0.000	0.000
84	A	85	GLY	0	-0.020	0.009	14.183	1.256	1.256	0.000	0.000	0.000	0.000
85	A	86	HIS	0	-0.006	-0.029	13.622	-0.426	-0.426	0.000	0.000	0.000	0.000
86	A	87	ASN	0	0.000	-0.006	16.408	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.023	-0.016	12.462	-0.335	-0.335	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.002	0.002	15.717	0.032	0.032	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.881	0.966	17.608	-13.572	-13.572	0.000	0.000	0.000	0.000
90	A	91	HIS	0	0.005	0.003	16.598	-0.960	-0.960	0.000	0.000	0.000	0.000
91	A	92	CYS	0	0.001	0.004	9.963	0.923	0.923	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.018	0.009	11.929	-0.700	-0.700	0.000	0.000	0.000	0.000
93	A	94	HIS	0	0.034	-0.003	7.608	4.935	4.935	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.007	-0.001	7.501	-2.649	-2.649	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.039	0.000	5.202	6.127	6.127	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.058	0.032	4.366	-6.254	-6.108	-0.001	-0.025	-0.120	0.000
97	A	98	PRO	0	0.009	0.006	5.441	0.734	0.783	-0.001	-0.003	-0.046	0.000
98	A	99	ASN	0	0.008	-0.005	5.545	7.475	7.475	0.000	0.000	0.000	0.000
99	A	100	VAL	0	0.051	0.016	6.422	-4.458	-4.458	0.000	0.000	0.000	0.000
100	A	101	ASN	0	0.022	0.024	7.203	-5.316	-5.316	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.784	0.890	8.241	-27.908	-27.908	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.020	0.008	10.343	-1.683	-1.683	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.826	-0.875	8.295	29.528	29.528	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.809	-0.909	11.601	21.090	21.090	0.000	0.000	0.000	0.000
105	A	106	ILE	0	0.049	0.017	9.955	1.815	1.815	0.000	0.000	0.000	0.000
106	A	107	GLN	0	0.025	0.018	11.521	1.431	1.431	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.042	-0.033	10.515	-0.317	-0.317	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.003	-0.015	6.468	1.377	1.377	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.863	0.948	9.895	-17.966	-17.966	0.000	0.000	0.000	0.000
110	A	111	SER	0	0.029	0.010	12.510	-0.742	-0.742	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.037	-0.021	7.969	-0.338	-0.338	0.000	0.000	0.000	0.000
112	A	113	TYR	0	0.057	-0.001	8.693	0.431	0.431	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.891	-0.952	11.646	16.479	16.479	0.000	0.000	0.000	0.000
114	A	115	ASN	0	-0.053	-0.012	11.595	-2.533	-2.533	0.000	0.000	0.000	0.000
115	A	116	PHE	0	0.022	-0.015	9.335	-0.569	-0.569	0.000	0.000	0.000	0.000
116	A	117	ASN	0	-0.027	-0.010	14.689	-1.404	-1.404	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.067	-0.018	17.610	-0.936	-0.936	0.000	0.000	0.000	0.000
118	A	119	HIS	0	-0.048	-0.032	16.587	-0.895	-0.895	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.845	-0.915	19.536	13.743	13.743	0.000	0.000	0.000	0.000
120	A	121	VAL	0	0.023	0.008	19.560	0.087	0.087	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.033	0.021	13.933	0.226	0.226	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.008	0.018	13.090	-0.372	-0.372	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.017	-0.002	10.146	0.882	0.882	0.000	0.000	0.000	0.000
124	A	125	PRO	0	-0.026	0.004	5.837	-2.211	-2.211	0.000	0.000	0.000	0.000
125	A	126	LEU	0	0.037	0.020	7.154	-0.934	-0.934	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.005	-0.002	4.233	10.792	11.103	0.001	-0.057	-0.256	0.000
127	A	128	SER	0	0.011	-0.013	2.503	-13.143	-11.943	4.235	-2.553	-2.883	0.024
128	A	129	ALA	0	0.001	0.012	3.313	-7.890	-9.398	0.529	2.096	-1.117	0.003
129	A	130	GLY	0	0.017	0.017	1.956	-16.183	-19.420	7.992	-2.160	-2.596	0.022
130	A	131	ILE	0	-0.032	-0.035	2.360	-8.373	-8.361	2.669	1.266	-3.946	0.004
131	A	132	PHE	0	-0.046	-0.022	2.303	-25.967	-21.003	10.194	-3.765	-11.393	0.002
132	A	133	GLY	0	0.029	0.016	3.965	-9.170	-8.880	0.013	-0.053	-0.250	0.001
133	A	134	ALA	0	-0.015	0.012	5.167	-7.199	-7.177	-0.001	-0.001	-0.021	0.000
134	A	135	ASP	-1	-0.800	-0.911	6.959	27.315	27.315	0.000	0.000	0.000	0.000
135	A	136	PRO	0	0.001	0.000	8.349	0.472	0.472	0.000	0.000	0.000	0.000
136	A	137	ILE	0	0.013	0.000	9.361	-0.695	-0.695	0.000	0.000	0.000	0.000
137	A	138	HIS	0	0.018	0.010	10.893	-1.588	-1.588	0.000	0.000	0.000	0.000
138	A	139	SER	0	-0.018	-0.029	7.107	-2.257	-2.257	0.000	0.000	0.000	0.000
139	A	140	LEU	0	-0.003	-0.007	10.112	-0.643	-0.643	0.000	0.000	0.000	0.000
140	A	141	ARG	1	0.899	0.933	12.768	-18.937	-18.937	0.000	0.000	0.000	0.000
141	A	142	VAL	0	0.036	0.032	11.804	-1.035	-1.035	0.000	0.000	0.000	0.000
142	A	143	CYS	0	-0.007	0.015	11.677	-1.016	-1.016	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.041	-0.022	13.410	-1.316	-1.316	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-0.899	-0.935	16.841	16.150	16.150	0.000	0.000	0.000	0.000
145	A	146	THR	0	-0.150	-0.092	14.594	-1.172	-1.172	0.000	0.000	0.000	0.000
146	A	147	VAL	0	-0.079	-0.031	13.903	-0.538	-0.538	0.000	0.000	0.000	0.000
147	A	148	ARG	1	0.967	0.989	16.977	-15.736	-15.736	0.000	0.000	0.000	0.000
148	A	149	THR	0	-0.029	0.006	18.614	-0.499	-0.499	0.000	0.000	0.000	0.000
149	A	150	ASN	0	-0.020	-0.007	19.264	0.580	0.580	0.000	0.000	0.000	0.000
150	A	151	VAL	0	0.015	-0.002	13.531	0.628	0.628	0.000	0.000	0.000	0.000
151	A	152	TYR	0	-0.019	-0.007	15.833	-0.567	-0.567	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.019	-0.008	10.711	1.268	1.268	0.000	0.000	0.000	0.000
153	A	154	ALA	0	-0.026	-0.012	11.530	-1.860	-1.860	0.000	0.000	0.000	0.000
154	A	155	VAL	0	-0.006	-0.007	10.316	3.349	3.349	0.000	0.000	0.000	0.000
155	A	156	PHE	0	0.010	0.010	10.558	-1.949	-1.949	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.802	-0.905	11.881	19.532	19.532	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.873	0.929	13.765	-14.848	-14.848	0.000	0.000	0.000	0.000
158	A	159	ASN	0	-0.019	-0.016	16.501	-1.237	-1.237	0.000	0.000	0.000	0.000
159	A	160	LEU	0	-0.025	-0.014	9.820	-0.272	-0.272	0.000	0.000	0.000	0.000
160	A	161	TYR	0	0.016	0.004	14.334	-0.045	-0.045	0.000	0.000	0.000	0.000
161	A	162	ASP	-1	-0.784	-0.886	15.624	15.140	15.140	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.913	0.961	13.951	-21.826	-21.826	0.000	0.000	0.000	0.000
163	A	164	LEU	0	-0.030	-0.016	11.713	-0.112	-0.112	0.000	0.000	0.000	0.000
164	A	165	VAL	0	-0.034	-0.015	16.130	-0.485	-0.485	0.000	0.000	0.000	0.000
165	A	166	SER	0	-0.078	-0.037	19.412	-1.028	-1.028	0.000	0.000	0.000	0.000
166	A	167	SER	-1	-0.907	-0.924	17.546	15.799	15.799	0.000	0.000	0.000	0.000
167	A	309	HOH	0	-0.026	-0.030	1.769	-9.616	-16.409	13.562	-4.053	-2.716	0.026
168	A	316	HOH	0	-0.018	-0.030	1.789	-15.589	-19.292	11.394	-4.348	-3.343	0.021
169	A	322	HOH	0	-0.036	-0.031	5.743	-0.525	-0.525	0.000	0.000	0.000	0.000
170	A	328	HOH	0	-0.008	-0.032	11.994	0.702	0.702	0.000	0.000	0.000	0.000
171	A	330	HOH	0	-0.010	-0.030	18.776	0.199	0.199	0.000	0.000	0.000	0.000
172	A	332	HOH	0	-0.048	-0.041	9.162	-0.957	-0.957	0.000	0.000	0.000	0.000
173	A	342	HOH	0	-0.032	-0.026	11.849	-0.447	-0.447	0.000	0.000	0.000	0.000
174	A	343	HOH	0	-0.029	-0.032	10.579	-0.110	-0.110	0.000	0.000	0.000	0.000
175	A	350	HOH	0	-0.014	-0.022	19.753	-0.383	-0.383	0.000	0.000	0.000	0.000
176	A	355	HOH	0	-0.027	-0.023	1.677	-11.567	-19.655	14.566	-4.135	-2.343	0.035
177	A	362	HOH	0	0.035	0.021	16.105	-0.078	-0.078	0.000	0.000	0.000	0.000
178	A	363	HOH	0	-0.058	-0.042	19.147	-0.272	-0.272	0.000	0.000	0.000	0.000
179	A	394	HOH	0	-0.007	-0.028	2.430	-1.541	0.010	0.629	-1.082	-1.098	-0.009
180	A	400	HOH	0	0.008	-0.009	5.337	0.068	0.068	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #181(A:203:MES )