FMO DATABASE

FMODB ID: 4333N

Calculation Name: 5RUF-A-Xray89

Preferred Name:

Target Type:

Ligand Name: 6-chloro-1,3-benzothiazol-2-amine

ligand 3-letter code: 54T

PDB ID: 5RUF

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2021-10-07

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	208
LigandCharge	54T=1
Software	ABINIT-MP - Open Ver.1 Rev. 16 beta / 20190613

Total energy (hartree)

FMO2-HF: Electronic energy	-1802069.759504
FMO2-HF: Nuclear repulsion	1735267.325155
FMO2-HF: Total energy	-66802.434349
FMO2-MP2: Total energy	-66996.010292

3D Structure

Snapshot

Ligand structure

54T

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.
-79.315	-74.441	49.787	-19.413	-35.248	0.148

Interactive mode: IFIE and PIEDA for fragment #208(A:201:54T )

Summations of interaction energy for fragment #208(A:201:54T )

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.
-79.315	-74.441	49.787	-19.413	-35.248	-0.148

Interaction energy analysis for fragmet #208(A:201:54T )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.853 / q_NPA : 0.953

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	3	VAL	0	0.014	-0.005	24.336	0.002	0.002	0.000	0.000	0.000	0.000
2	A	4	ASN	0	-0.014	-0.017	19.702	-0.477	-0.477	0.000	0.000	0.000	0.000
3	A	5	SER	0	0.029	0.004	17.526	0.184	0.184	0.000	0.000	0.000	0.000
4	A	6	PHE	0	-0.041	0.005	12.834	-0.955	-0.955	0.000	0.000	0.000	0.000
5	A	7	SER	0	0.028	0.011	15.671	0.852	0.852	0.000	0.000	0.000	0.000
6	A	8	GLY	0	0.011	-0.005	15.503	-1.460	-1.460	0.000	0.000	0.000	0.000
7	A	9	TYR	0	-0.060	-0.042	11.757	-1.131	-1.131	0.000	0.000	0.000	0.000
8	A	10	LEU	0	0.004	0.013	15.886	1.059	1.059	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.809	0.897	17.060	12.144	12.144	0.000	0.000	0.000	0.000
10	A	12	LEU	0	-0.049	-0.015	15.253	0.227	0.227	0.000	0.000	0.000	0.000
11	A	13	THR	0	0.035	0.007	19.503	0.498	0.498	0.000	0.000	0.000	0.000
12	A	14	ASP	-1	-0.858	-0.890	21.847	-11.544	-11.544	0.000	0.000	0.000	0.000
13	A	15	ASN	0	-0.004	-0.008	19.817	0.199	0.199	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.008	0.016	15.249	-0.819	-0.819	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.034	0.024	15.798	0.671	0.671	0.000	0.000	0.000	0.000
16	A	18	ILE	0	0.023	0.012	11.162	-1.392	-1.392	0.000	0.000	0.000	0.000
17	A	19	LYS	1	0.832	0.902	11.040	25.712	25.712	0.000	0.000	0.000	0.000
18	A	20	ASN	0	-0.042	-0.018	8.567	-0.597	-0.597	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.002	-0.010	7.840	1.272	1.272	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.761	-0.869	1.852	-136.644	-143.113	26.447	-10.335	-9.644	-0.124
21	A	23	ILE	0	0.033	0.001	2.836	1.953	2.653	1.944	-0.646	-1.998	-0.003
22	A	24	VAL	0	0.026	0.021	2.417	6.447	8.109	1.106	-0.737	-2.030	-0.004
23	A	25	GLU	-1	-0.832	-0.903	4.152	-33.766	-33.607	0.000	-0.033	-0.125	0.000
24	A	26	GLU	-1	-0.774	-0.852	6.239	-20.641	-20.641	0.000	0.000	0.000	0.000
25	A	27	ALA	0	-0.011	-0.013	7.461	3.831	3.831	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.832	0.906	6.633	39.483	39.483	0.000	0.000	0.000	0.000
27	A	29	LYS	1	0.830	0.914	10.071	26.772	26.772	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.041	-0.029	11.937	1.607	1.607	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.875	0.963	12.739	21.393	21.393	0.000	0.000	0.000	0.000
30	A	32	PRO	0	0.005	0.017	12.323	1.330	1.330	0.000	0.000	0.000	0.000
31	A	33	THR	0	0.035	-0.002	15.323	-0.180	-0.180	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.016	-0.014	14.670	0.177	0.177	0.000	0.000	0.000	0.000
33	A	35	VAL	0	0.003	0.007	8.915	-0.643	-0.643	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.008	0.003	10.036	0.960	0.960	0.000	0.000	0.000	0.000
35	A	37	ASN	0	-0.011	-0.030	8.460	-5.553	-5.553	0.000	0.000	0.000	0.000
36	A	38	ALA	0	-0.012	0.016	6.749	2.195	2.195	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.049	0.043	8.631	-0.979	-0.979	0.000	0.000	0.000	0.000
38	A	40	ASN	0	-0.003	-0.019	11.812	1.742	1.742	0.000	0.000	0.000	0.000
39	A	41	VAL	0	0.045	0.022	14.041	-0.108	-0.108	0.000	0.000	0.000	0.000
40	A	42	TYR	0	0.009	0.006	17.277	0.447	0.447	0.000	0.000	0.000	0.000
41	A	43	LEU	0	-0.005	0.009	15.278	-0.086	-0.086	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.981	1.007	15.597	16.308	16.308	0.000	0.000	0.000	0.000
43	A	45	HIS	0	0.026	0.016	10.882	-2.281	-2.281	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.046	0.035	11.159	-1.106	-1.106	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.045	0.010	7.128	-0.840	-0.840	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.001	0.009	3.533	1.144	1.685	0.054	-0.188	-0.407	0.001
47	A	49	VAL	0	0.001	-0.019	2.198	-9.275	-7.790	2.912	-0.747	-3.650	-0.005
48	A	50	ALA	0	0.027	0.029	4.290	-1.939	-1.638	0.013	0.003	-0.318	0.000
49	A	51	GLY	0	-0.014	0.004	7.530	1.171	1.171	0.000	0.000	0.000	0.000
50	A	52	ALA	0	-0.024	-0.012	2.724	-0.358	0.500	1.908	-0.674	-2.092	0.002
51	A	53	LEU	0	0.016	-0.005	4.853	1.184	1.481	-0.001	-0.019	-0.277	0.000
52	A	54	ASN	0	0.067	0.013	6.614	3.885	3.885	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.958	0.988	6.965	36.856	36.856	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.031	-0.005	6.013	2.501	2.501	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.044	-0.011	8.093	2.920	2.920	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.031	-0.020	11.206	1.703	1.703	0.000	0.000	0.000	0.000
57	A	59	ASN	0	-0.005	0.000	12.443	0.541	0.541	0.000	0.000	0.000	0.000
58	A	60	ALA	0	0.040	0.030	14.250	1.046	1.046	0.000	0.000	0.000	0.000
59	A	61	MET	0	-0.001	0.007	10.697	0.098	0.098	0.000	0.000	0.000	0.000
60	A	62	GLN	0	-0.061	-0.033	14.484	-0.723	-0.723	0.000	0.000	0.000	0.000
61	A	63	VAL	0	0.034	0.028	16.046	0.860	0.860	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.722	-0.837	17.424	-16.427	-16.427	0.000	0.000	0.000	0.000
63	A	65	SER	0	0.004	-0.010	16.443	0.389	0.389	0.000	0.000	0.000	0.000
64	A	66	ASP	-1	-0.818	-0.900	18.856	-15.599	-15.599	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.816	-0.856	21.460	-11.724	-11.724	0.000	0.000	0.000	0.000
66	A	68	TYR	0	0.037	0.006	21.083	0.522	0.522	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.041	-0.026	19.990	0.520	0.520	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.025	0.002	23.519	0.494	0.494	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.037	-0.007	26.468	0.629	0.629	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.090	-0.052	24.864	0.727	0.727	0.000	0.000	0.000	0.000
71	A	73	GLY	0	0.013	0.021	25.802	0.233	0.233	0.000	0.000	0.000	0.000
72	A	74	PRO	0	-0.062	-0.037	21.853	-0.474	-0.474	0.000	0.000	0.000	0.000
73	A	75	LEU	0	-0.011	-0.003	17.125	0.429	0.429	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.981	0.983	21.004	11.220	11.220	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.036	0.009	16.488	-0.595	-0.595	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.010	0.017	17.054	0.648	0.648	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.028	-0.006	18.395	0.242	0.242	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.018	-0.044	17.106	-0.848	-0.848	0.000	0.000	0.000	0.000
79	A	81	CYS	0	-0.035	0.010	17.526	0.577	0.577	0.000	0.000	0.000	0.000
80	A	82	VAL	0	0.012	0.009	17.526	-1.093	-1.093	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.003	0.009	17.104	0.707	0.707	0.000	0.000	0.000	0.000
82	A	84	SER	0	0.033	0.014	17.686	-0.482	-0.482	0.000	0.000	0.000	0.000
83	A	85	GLY	0	-0.013	0.007	14.022	-1.074	-1.074	0.000	0.000	0.000	0.000
84	A	86	HIS	0	-0.029	-0.032	13.220	-1.667	-1.667	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.021	-0.024	11.083	0.543	0.543	0.000	0.000	0.000	0.000
86	A	88	LEU	0	-0.022	-0.022	7.774	-0.917	-0.917	0.000	0.000	0.000	0.000
87	A	89	ALA	0	-0.009	-0.005	11.298	-0.571	-0.571	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.855	0.947	14.064	14.209	14.209	0.000	0.000	0.000	0.000
89	A	91	HIS	0	0.036	0.016	16.888	1.020	1.020	0.000	0.000	0.000	0.000
90	A	92	CYS	0	-0.023	-0.009	12.477	-1.947	-1.947	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.026	0.009	14.052	1.153	1.153	0.000	0.000	0.000	0.000
92	A	94	HIS	0	0.053	0.003	12.954	-2.485	-2.485	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.016	0.003	12.509	1.559	1.559	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.043	0.006	12.415	-1.460	-1.460	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.054	0.034	12.224	1.027	1.027	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.004	0.005	13.185	-0.359	-0.359	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.024	-0.010	11.663	-0.702	-0.702	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.069	0.027	12.702	0.886	0.886	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.056	-0.027	10.881	1.507	1.507	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.813	0.906	14.517	17.013	17.013	0.000	0.000	0.000	0.000
101	A	103	GLY	0	0.004	0.011	17.135	0.564	0.564	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.787	-0.842	16.016	-15.023	-15.023	0.000	0.000	0.000	0.000
103	A	105	ASP	-1	-0.809	-0.908	18.008	-11.876	-11.876	0.000	0.000	0.000	0.000
104	A	106	ILE	0	0.048	0.010	14.531	-0.465	-0.465	0.000	0.000	0.000	0.000
105	A	107	GLN	0	0.002	0.002	17.710	-0.499	-0.499	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.037	-0.021	18.214	-0.050	-0.050	0.000	0.000	0.000	0.000
107	A	109	LEU	0	-0.037	-0.026	12.468	-0.472	-0.472	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.881	0.937	16.263	11.534	11.534	0.000	0.000	0.000	0.000
109	A	111	SER	0	0.031	0.010	18.979	-0.062	-0.062	0.000	0.000	0.000	0.000
110	A	112	ALA	0	0.016	0.006	14.890	-0.108	-0.108	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.027	-0.005	11.485	-0.838	-0.838	0.000	0.000	0.000	0.000
112	A	114	GLU	-1	-0.849	-0.910	16.641	-11.823	-11.823	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.059	-0.022	17.165	0.596	0.596	0.000	0.000	0.000	0.000
114	A	116	PHE	0	0.033	-0.010	11.516	-0.267	-0.267	0.000	0.000	0.000	0.000
115	A	117	ASN	0	-0.023	-0.003	17.608	0.142	0.142	0.000	0.000	0.000	0.000
116	A	118	GLN	0	-0.033	0.010	20.786	0.703	0.703	0.000	0.000	0.000	0.000
117	A	119	HIS	0	-0.041	-0.030	18.610	-0.091	-0.091	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.869	-0.928	20.245	-12.128	-12.128	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.008	-0.010	17.440	-0.060	-0.060	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.036	0.025	14.016	-0.335	-0.335	0.000	0.000	0.000	0.000
121	A	123	LEU	0	-0.021	0.012	9.020	0.017	0.017	0.000	0.000	0.000	0.000
122	A	124	ALA	0	0.028	-0.003	9.145	-0.438	-0.438	0.000	0.000	0.000	0.000
123	A	125	PRO	0	-0.047	-0.005	4.640	-1.395	-1.295	-0.001	-0.010	-0.089	0.000
124	A	126	LEU	0	0.044	0.017	6.472	2.396	2.396	0.000	0.000	0.000	0.000
125	A	127	LEU	0	0.002	0.020	7.043	-1.558	-1.558	0.000	0.000	0.000	0.000
126	A	128	SER	0	0.035	-0.012	9.021	0.953	0.953	0.000	0.000	0.000	0.000
127	A	129	ALA	0	-0.002	0.021	5.682	0.659	0.679	-0.001	-0.004	-0.015	0.000
128	A	130	GLY	0	0.016	0.015	3.598	-1.660	-1.250	0.090	-0.144	-0.355	0.000
129	A	131	ILE	0	0.011	-0.016	4.521	1.551	1.725	0.002	-0.021	-0.156	0.000
130	A	132	PHE	0	-0.070	-0.023	6.865	1.585	1.585	0.000	0.000	0.000	0.000
131	A	133	GLY	0	0.030	0.023	8.363	1.436	1.436	0.000	0.000	0.000	0.000
132	A	134	ALA	0	0.007	0.008	9.922	1.175	1.175	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.795	-0.898	10.014	-17.408	-17.408	0.000	0.000	0.000	0.000
134	A	136	PRO	0	-0.020	-0.023	8.004	0.129	0.129	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.030	0.011	10.061	-0.131	-0.131	0.000	0.000	0.000	0.000
136	A	138	HIS	0	0.037	0.024	13.576	0.486	0.486	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.011	-0.024	10.412	0.376	0.376	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.018	-0.005	12.382	-0.029	-0.029	0.000	0.000	0.000	0.000
139	A	141	ARG	1	0.853	0.922	13.634	13.093	13.093	0.000	0.000	0.000	0.000
140	A	142	VAL	0	0.017	0.016	15.688	0.468	0.468	0.000	0.000	0.000	0.000
141	A	143	CYS	0	-0.040	-0.004	13.312	0.488	0.488	0.000	0.000	0.000	0.000
142	A	144	VAL	0	0.015	0.015	16.049	0.387	0.387	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.806	-0.893	18.796	-11.727	-11.727	0.000	0.000	0.000	0.000
144	A	146	THR	0	-0.115	-0.063	18.803	0.786	0.786	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.060	-0.018	16.054	0.325	0.325	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.945	0.981	19.505	11.676	11.676	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.037	0.004	19.678	0.245	0.245	0.000	0.000	0.000	0.000
148	A	150	ASN	0	-0.012	0.004	19.284	-0.238	-0.238	0.000	0.000	0.000	0.000
149	A	151	VAL	0	0.016	0.003	13.085	-0.628	-0.628	0.000	0.000	0.000	0.000
150	A	152	TYR	0	0.026	0.026	13.340	0.694	0.694	0.000	0.000	0.000	0.000
151	A	153	LEU	0	0.021	-0.006	9.817	-1.876	-1.876	0.000	0.000	0.000	0.000
152	A	154	ALA	0	-0.007	-0.006	6.529	0.509	0.509	0.000	0.000	0.000	0.000
153	A	155	VAL	0	0.003	0.011	5.650	-2.713	-2.713	0.000	0.000	0.000	0.000
154	A	156	PHE	0	-0.012	-0.028	2.813	-11.641	-4.294	5.491	-2.658	-10.180	-0.018
155	A	157	ASP	-1	-0.845	-0.922	4.938	-28.192	-27.997	0.000	-0.025	-0.170	0.000
156	A	158	LYS	1	0.885	0.927	7.463	21.979	21.979	0.000	0.000	0.000	0.000
157	A	159	ASN	0	0.000	-0.002	10.993	2.087	2.087	0.000	0.000	0.000	0.000
158	A	160	LEU	0	-0.008	-0.008	6.512	1.340	1.340	0.000	0.000	0.000	0.000
159	A	161	TYR	0	-0.008	-0.007	10.038	1.282	1.282	0.000	0.000	0.000	0.000
160	A	162	ASP	-1	-0.768	-0.860	11.295	-17.845	-17.845	0.000	0.000	0.000	0.000
161	A	163	LYS	1	0.952	0.993	13.026	17.838	17.838	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.045	-0.019	9.412	0.775	0.775	0.000	0.000	0.000	0.000
163	A	165	VAL	0	0.010	0.010	13.887	0.723	0.723	0.000	0.000	0.000	0.000
164	A	166	SER	0	-0.043	-0.029	16.664	0.919	0.919	0.000	0.000	0.000	0.000
165	A	167	SER	0	-0.104	-0.071	16.394	0.644	0.644	0.000	0.000	0.000	0.000
166	A	168	PHE	0	-0.016	-0.004	17.145	0.141	0.141	0.000	0.000	0.000	0.000
167	A	169	LEU	-1	-0.879	-0.925	19.159	-11.655	-11.655	0.000	0.000	0.000	0.000
168	A	302	HOH	0	-0.064	-0.050	26.999	-0.017	-0.017	0.000	0.000	0.000	0.000
169	A	339	HOH	0	-0.075	-0.061	22.213	-0.049	-0.049	0.000	0.000	0.000	0.000
170	A	342	HOH	0	-0.049	-0.036	13.168	0.427	0.427	0.000	0.000	0.000	0.000
171	A	345	HOH	0	-0.014	-0.015	4.205	-0.456	-0.342	0.005	-0.032	-0.088	0.000
172	A	346	HOH	0	-0.054	-0.044	22.007	0.126	0.126	0.000	0.000	0.000	0.000
173	A	347	HOH	0	0.007	-0.005	8.062	0.156	0.156	0.000	0.000	0.000	0.000
174	A	348	HOH	0	-0.020	-0.022	24.661	-0.015	-0.015	0.000	0.000	0.000	0.000
175	A	359	HOH	0	-0.057	-0.038	25.249	0.165	0.165	0.000	0.000	0.000	0.000
176	A	360	HOH	0	0.008	-0.007	23.083	0.147	0.147	0.000	0.000	0.000	0.000
177	A	362	HOH	0	-0.011	-0.014	10.799	-0.240	-0.240	0.000	0.000	0.000	0.000
178	A	363	HOH	0	-0.014	-0.036	15.344	-0.423	-0.423	0.000	0.000	0.000	0.000
179	A	364	HOH	0	-0.030	-0.010	12.048	0.179	0.179	0.000	0.000	0.000	0.000
180	A	365	HOH	0	0.016	0.003	19.835	-0.019	-0.019	0.000	0.000	0.000	0.000
181	A	370	HOH	0	-0.064	-0.049	10.007	0.197	0.197	0.000	0.000	0.000	0.000
182	A	372	HOH	0	-0.025	-0.011	10.084	-0.015	-0.015	0.000	0.000	0.000	0.000
183	A	374	HOH	0	-0.031	-0.038	13.790	-0.239	-0.239	0.000	0.000	0.000	0.000
184	A	378	HOH	0	-0.028	-0.022	7.766	-0.582	-0.582	0.000	0.000	0.000	0.000
185	A	381	HOH	0	-0.027	-0.017	20.996	-0.098	-0.098	0.000	0.000	0.000	0.000
186	A	383	HOH	0	-0.031	-0.033	4.582	1.437	1.497	0.000	-0.023	-0.037	0.000
187	A	389	HOH	0	-0.007	-0.015	19.093	0.301	0.301	0.000	0.000	0.000	0.000
188	A	392	HOH	0	-0.048	-0.037	9.201	1.108	1.108	0.000	0.000	0.000	0.000
189	A	403	HOH	0	-0.018	-0.026	15.619	0.118	0.118	0.000	0.000	0.000	0.000
190	A	404	HOH	0	0.003	-0.002	20.675	-0.185	-0.185	0.000	0.000	0.000	0.000
191	A	405	HOH	0	-0.020	-0.020	21.753	0.219	0.219	0.000	0.000	0.000	0.000
192	A	409	HOH	0	0.005	-0.005	5.011	-0.253	-0.223	0.000	-0.003	-0.027	0.000
193	A	410	HOH	0	0.029	0.020	7.102	-1.333	-1.333	0.000	0.000	0.000	0.000
194	A	412	HOH	0	0.000	0.002	24.065	-0.099	-0.099	0.000	0.000	0.000	0.000
195	A	414	HOH	0	-0.021	-0.039	25.601	-0.142	-0.142	0.000	0.000	0.000	0.000
196	A	416	HOH	0	0.014	-0.010	12.517	0.027	0.027	0.000	0.000	0.000	0.000
197	A	419	HOH	0	-0.061	-0.058	15.518	-0.091	-0.091	0.000	0.000	0.000	0.000
198	A	421	HOH	0	0.030	0.013	21.035	0.003	0.003	0.000	0.000	0.000	0.000
199	A	424	HOH	0	-0.019	-0.019	15.908	0.109	0.109	0.000	0.000	0.000	0.000
200	A	428	HOH	0	0.024	0.013	14.005	-0.752	-0.752	0.000	0.000	0.000	0.000
201	A	431	HOH	0	-0.007	-0.011	24.487	-0.105	-0.105	0.000	0.000	0.000	0.000
202	A	447	HOH	0	-0.010	-0.028	2.267	-0.453	-3.581	6.873	-1.814	-1.931	0.004
203	A	448	HOH	0	0.044	0.024	2.466	1.013	0.914	2.940	-1.275	-1.566	-0.001
204	A	451	HOH	0	-0.013	-0.017	4.635	-1.670	-1.553	0.005	-0.028	-0.093	0.000
205	A	455	HOH	0	-0.032	-0.024	18.991	-0.309	-0.309	0.000	0.000	0.000	0.000
206	A	457	HOH	0	0.021	0.011	23.394	0.068	0.068	0.000	0.000	0.000	0.000
207	A	484	HOH	0	0.012	0.008	10.465	-0.747	-0.747	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #208(A:201:54T )