FMO DATABASE

FMODB ID: GNQ11

Calculation Name: 5RU6-A-Xray89

Preferred Name:

Target Type:

Ligand Name: naphthalene-2-carboximidamide

ligand 3-letter code: 2UP

PDB ID: 5RU6

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2021-09-27

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	210
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 16 beta / 20190613

Total energy (hartree)

FMO2-HF: Electronic energy	-1778495.041013
FMO2-HF: Nuclear repulsion	1712698.735576
FMO2-HF: Total energy	-65796.305438
FMO2-MP2: Total energy	-65988.958221

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:3:VAL )

Summations of interaction energy for fragment #1(A:3:VAL )

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.
0.032	2.325	0.233	-1.163	-1.364	-0.002

Interaction energy analysis for fragmet #1(A:3:VAL )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : -0.007

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	5	SER	0	0.028	0.004	3.032	-1.332	0.961	0.233	-1.163	-1.364	-0.002
4	A	6	PHE	0	-0.039	0.007	5.464	0.175	0.175	0.000	0.000	0.000	0.000
5	A	7	SER	0	0.027	0.010	6.723	0.102	0.102	0.000	0.000	0.000	0.000
6	A	8	GLY	0	0.007	-0.009	9.000	0.014	0.014	0.000	0.000	0.000	0.000
7	A	9	TYR	0	-0.055	-0.037	10.239	0.007	0.007	0.000	0.000	0.000	0.000
8	A	10	LEU	0	0.000	0.012	11.754	0.039	0.039	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.806	0.894	9.622	-1.099	-1.099	0.000	0.000	0.000	0.000
10	A	12	LEU	0	-0.060	-0.024	13.040	-0.050	-0.050	0.000	0.000	0.000	0.000
11	A	13	THR	0	0.027	0.001	14.526	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	14	ASP	-1	-0.872	-0.913	12.403	1.107	1.107	0.000	0.000	0.000	0.000
13	A	15	ASN	0	-0.002	-0.004	10.922	0.184	0.184	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.010	0.019	12.072	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.032	0.024	8.039	-0.012	-0.012	0.000	0.000	0.000	0.000
16	A	18	ILE	0	0.024	0.010	12.817	-0.062	-0.062	0.000	0.000	0.000	0.000
17	A	19	LYS	1	0.832	0.902	12.629	0.027	0.027	0.000	0.000	0.000	0.000
18	A	20	ASN	0	-0.054	-0.025	16.396	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.009	-0.017	17.194	-0.016	-0.016	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.817	-0.908	19.265	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.001	-0.009	18.208	-0.016	-0.016	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.024	0.019	18.733	-0.018	-0.018	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.817	-0.893	19.390	-0.106	-0.106	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.779	-0.858	12.749	-0.110	-0.110	0.000	0.000	0.000	0.000
25	A	27	ALA	0	-0.022	-0.021	14.496	-0.043	-0.043	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.826	0.903	15.636	0.057	0.057	0.000	0.000	0.000	0.000
27	A	29	LYS	1	0.823	0.913	12.005	0.165	0.165	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.041	-0.029	9.246	-0.047	-0.047	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.873	0.962	11.262	0.164	0.164	0.000	0.000	0.000	0.000
30	A	32	PRO	0	0.007	0.020	11.506	-0.059	-0.059	0.000	0.000	0.000	0.000
31	A	33	THR	0	0.026	-0.008	10.937	-0.017	-0.017	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.014	-0.013	13.565	0.022	0.022	0.000	0.000	0.000	0.000
33	A	35	VAL	0	0.005	0.008	15.301	0.019	0.019	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.006	0.002	17.888	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	37	ASN	0	-0.007	-0.027	20.275	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	38	ALA	0	-0.003	0.020	23.815	0.011	0.011	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.041	0.040	26.189	-0.009	-0.009	0.000	0.000	0.000	0.000
38	A	40	ASN	0	-0.002	-0.019	28.864	0.005	0.005	0.000	0.000	0.000	0.000
39	A	41	VAL	0	0.047	0.024	32.271	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	42	TYR	0	-0.002	-0.002	34.226	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	43	LEU	0	-0.006	0.008	29.626	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.981	1.009	32.762	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	45	HIS	0	0.022	0.014	29.422	0.010	0.010	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.049	0.039	32.127	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.051	0.019	32.665	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	48	GLY	0	0.020	0.022	30.208	0.003	0.003	0.000	0.000	0.000	0.000
47	A	49	VAL	0	0.031	-0.001	23.506	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	50	ALA	0	0.019	0.026	26.322	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	51	GLY	0	-0.012	0.008	28.135	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	52	ALA	0	0.005	0.005	26.266	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.036	0.010	21.487	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	54	ASN	0	0.061	0.006	25.210	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.972	1.003	28.256	0.024	0.024	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.039	-0.010	24.048	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.052	-0.014	24.482	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.037	-0.026	26.743	0.001	0.001	0.000	0.000	0.000	0.000
57	A	59	ASN	0	0.001	0.004	30.180	0.004	0.004	0.000	0.000	0.000	0.000
58	A	60	ALA	0	0.035	0.028	28.420	0.004	0.004	0.000	0.000	0.000	0.000
59	A	61	MET	0	0.001	0.008	24.236	0.006	0.006	0.000	0.000	0.000	0.000
60	A	62	GLN	0	-0.056	-0.030	28.805	0.008	0.008	0.000	0.000	0.000	0.000
61	A	63	VAL	0	0.030	0.027	32.380	0.003	0.003	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.727	-0.842	27.276	-0.042	-0.042	0.000	0.000	0.000	0.000
63	A	65	SER	0	0.009	-0.007	30.320	0.006	0.006	0.000	0.000	0.000	0.000
64	A	66	ASP	-1	-0.816	-0.895	32.130	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.822	-0.861	34.154	-0.019	-0.019	0.000	0.000	0.000	0.000
66	A	68	TYR	0	0.004	-0.017	30.294	0.004	0.004	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.039	-0.025	33.551	0.005	0.005	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.026	0.001	36.084	0.003	0.003	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.036	-0.005	35.720	0.000	0.000	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.084	-0.048	33.371	0.003	0.003	0.000	0.000	0.000	0.000
71	A	73	GLY	0	0.023	0.024	36.350	0.004	0.004	0.000	0.000	0.000	0.000
72	A	74	PRO	0	-0.040	-0.022	35.660	0.000	0.000	0.000	0.000	0.000	0.000
73	A	75	LEU	0	-0.015	-0.001	29.440	0.003	0.003	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.974	0.981	32.708	-0.053	-0.053	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.031	0.007	32.126	0.002	0.002	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.015	0.019	29.415	0.002	0.002	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.028	-0.007	28.513	0.010	0.010	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.010	-0.038	24.786	0.000	0.000	0.000	0.000	0.000	0.000
79	A	81	CYS	0	-0.031	0.010	26.145	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	82	VAL	0	0.008	0.008	21.161	0.002	0.002	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.002	0.008	23.708	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	84	SER	0	0.029	0.012	22.810	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	85	GLY	0	-0.009	0.010	20.367	0.014	0.014	0.000	0.000	0.000	0.000
84	A	86	HIS	0	-0.027	-0.031	21.437	-0.013	-0.013	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.028	-0.028	21.379	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	88	LEU	0	-0.020	-0.020	19.051	-0.018	-0.018	0.000	0.000	0.000	0.000
87	A	89	ALA	0	-0.001	-0.002	16.262	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.848	0.945	15.614	0.169	0.169	0.000	0.000	0.000	0.000
89	A	91	HIS	0	0.029	0.012	16.955	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	92	CYS	0	-0.019	-0.006	18.870	0.003	0.003	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.028	0.008	19.566	0.002	0.002	0.000	0.000	0.000	0.000
92	A	94	HIS	0	0.057	0.006	21.851	0.016	0.016	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.012	0.002	22.611	0.004	0.004	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.038	0.009	25.731	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.051	0.031	28.547	0.007	0.007	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.008	0.002	29.107	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.021	-0.008	32.100	0.003	0.003	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.061	0.021	33.861	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.050	-0.023	35.973	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.809	0.904	35.832	-0.039	-0.039	0.000	0.000	0.000	0.000
101	A	103	GLY	0	0.002	0.010	39.434	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.789	-0.846	35.091	0.051	0.051	0.000	0.000	0.000	0.000
103	A	105	ASP	-1	-0.813	-0.910	36.655	0.079	0.079	0.000	0.000	0.000	0.000
104	A	106	ILE	0	0.050	0.012	31.332	0.003	0.003	0.000	0.000	0.000	0.000
105	A	107	GLN	0	0.004	0.004	31.845	0.015	0.015	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.045	-0.028	31.463	0.008	0.008	0.000	0.000	0.000	0.000
107	A	109	LEU	0	-0.030	-0.022	26.543	0.003	0.003	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.898	0.942	25.219	-0.184	-0.184	0.000	0.000	0.000	0.000
109	A	111	SER	0	0.026	0.005	26.006	0.009	0.009	0.000	0.000	0.000	0.000
110	A	112	ALA	0	0.023	0.011	26.490	0.002	0.002	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.024	-0.005	20.702	0.005	0.005	0.000	0.000	0.000	0.000
112	A	114	GLU	-1	-0.814	-0.863	21.572	0.182	0.182	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.066	-0.024	22.038	0.001	0.001	0.000	0.000	0.000	0.000
114	A	116	PHE	0	0.038	-0.008	17.583	-0.012	-0.012	0.000	0.000	0.000	0.000
115	A	117	ASN	0	-0.014	0.002	17.225	0.065	0.065	0.000	0.000	0.000	0.000
116	A	118	GLN	0	-0.042	0.004	17.732	0.009	0.009	0.000	0.000	0.000	0.000
117	A	119	HIS	0	-0.036	-0.025	15.078	-0.042	-0.042	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.872	-0.930	9.944	0.402	0.402	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.007	-0.011	7.553	0.206	0.206	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.037	0.024	10.999	-0.170	-0.170	0.000	0.000	0.000	0.000
121	A	123	LEU	0	-0.016	0.015	12.994	0.058	0.058	0.000	0.000	0.000	0.000
122	A	124	ALA	0	0.026	-0.004	14.633	-0.025	-0.025	0.000	0.000	0.000	0.000
123	A	125	PRO	0	-0.039	0.000	17.920	0.009	0.009	0.000	0.000	0.000	0.000
124	A	126	LEU	0	0.040	0.015	20.911	0.014	0.014	0.000	0.000	0.000	0.000
125	A	127	LEU	0	0.002	0.019	22.679	-0.022	-0.022	0.000	0.000	0.000	0.000
126	A	128	SER	0	0.029	-0.015	25.068	0.008	0.008	0.000	0.000	0.000	0.000
127	A	129	ALA	0	-0.004	0.020	26.281	-0.004	-0.004	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.030	0.023	28.273	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	131	ILE	0	0.016	-0.014	30.039	0.001	0.001	0.000	0.000	0.000	0.000
130	A	132	PHE	0	-0.070	-0.022	30.420	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	133	GLY	0	0.025	0.020	32.525	0.002	0.002	0.000	0.000	0.000	0.000
132	A	134	ALA	0	0.000	0.003	30.148	0.001	0.001	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.796	-0.899	30.741	0.100	0.100	0.000	0.000	0.000	0.000
134	A	136	PRO	0	-0.012	-0.017	26.305	0.009	0.009	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.025	0.009	25.752	0.013	0.013	0.000	0.000	0.000	0.000
136	A	138	HIS	0	0.036	0.023	26.331	0.018	0.018	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.011	-0.024	25.032	0.017	0.017	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.016	-0.004	19.465	0.013	0.013	0.000	0.000	0.000	0.000
139	A	141	ARG	1	0.851	0.922	22.012	-0.201	-0.201	0.000	0.000	0.000	0.000
140	A	142	VAL	0	0.011	0.012	23.663	0.016	0.016	0.000	0.000	0.000	0.000
141	A	143	CYS	0	-0.031	0.002	18.963	0.024	0.024	0.000	0.000	0.000	0.000
142	A	144	VAL	0	0.015	0.016	18.169	0.030	0.030	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.802	-0.893	19.915	0.263	0.263	0.000	0.000	0.000	0.000
144	A	146	THR	0	-0.121	-0.066	21.536	-0.019	-0.019	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.054	-0.013	16.110	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.918	0.965	16.643	-0.275	-0.275	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.044	0.000	13.253	0.099	0.099	0.000	0.000	0.000	0.000
148	A	150	ASN	0	-0.006	0.007	9.033	0.100	0.100	0.000	0.000	0.000	0.000
149	A	151	VAL	0	0.012	0.001	11.094	-0.123	-0.123	0.000	0.000	0.000	0.000
150	A	152	TYR	0	0.023	0.025	6.373	0.137	0.137	0.000	0.000	0.000	0.000
151	A	153	LEU	0	0.020	-0.007	12.709	-0.079	-0.079	0.000	0.000	0.000	0.000
152	A	154	ALA	0	0.006	0.003	16.363	-0.003	-0.003	0.000	0.000	0.000	0.000
153	A	155	VAL	0	0.002	0.005	18.197	-0.005	-0.005	0.000	0.000	0.000	0.000
154	A	156	PHE	0	0.009	-0.003	21.483	-0.006	-0.006	0.000	0.000	0.000	0.000
155	A	157	ASP	-1	-0.811	-0.912	23.723	0.044	0.044	0.000	0.000	0.000	0.000
156	A	158	LYS	1	0.864	0.918	22.339	-0.058	-0.058	0.000	0.000	0.000	0.000
157	A	159	ASN	0	-0.027	-0.016	25.223	0.012	0.012	0.000	0.000	0.000	0.000
158	A	160	LEU	0	0.008	-0.002	25.561	0.007	0.007	0.000	0.000	0.000	0.000
159	A	161	TYR	0	-0.015	-0.004	17.025	0.004	0.004	0.000	0.000	0.000	0.000
160	A	162	ASP	-1	-0.766	-0.860	23.237	0.097	0.097	0.000	0.000	0.000	0.000
161	A	163	LYS	1	0.947	0.990	24.848	-0.076	-0.076	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.042	-0.016	22.598	0.005	0.005	0.000	0.000	0.000	0.000
163	A	165	VAL	0	0.009	0.010	19.924	0.015	0.015	0.000	0.000	0.000	0.000
164	A	166	SER	0	-0.046	-0.032	22.493	0.006	0.006	0.000	0.000	0.000	0.000
165	A	167	SER	0	-0.105	-0.072	25.775	0.001	0.001	0.000	0.000	0.000	0.000
166	A	168	PHE	0	-0.012	-0.003	20.063	0.000	0.000	0.000	0.000	0.000	0.000
167	A	169	LEU	-1	-0.880	-0.925	23.298	0.243	0.243	0.000	0.000	0.000	0.000
168	A	204	HOH	0	-0.065	-0.051	37.676	0.000	0.000	0.000	0.000	0.000	0.000
169	A	215	HOH	0	-0.009	-0.022	24.598	0.011	0.011	0.000	0.000	0.000	0.000
170	A	223	HOH	0	-0.074	-0.061	31.754	0.000	0.000	0.000	0.000	0.000	0.000
171	A	232	HOH	0	0.007	-0.005	27.347	0.005	0.005	0.000	0.000	0.000	0.000
172	A	234	HOH	0	-0.008	-0.012	25.170	-0.005	-0.005	0.000	0.000	0.000	0.000
173	A	237	HOH	0	-0.040	-0.035	27.423	-0.005	-0.005	0.000	0.000	0.000	0.000
174	A	240	HOH	0	-0.048	-0.035	33.928	0.001	0.001	0.000	0.000	0.000	0.000
175	A	241	HOH	0	-0.030	-0.010	33.198	-0.002	-0.002	0.000	0.000	0.000	0.000
176	A	243	HOH	0	-0.021	-0.023	21.097	-0.007	-0.007	0.000	0.000	0.000	0.000
177	A	244	HOH	0	-0.028	-0.024	26.466	0.000	0.000	0.000	0.000	0.000	0.000
178	A	246	HOH	0	-0.015	-0.036	25.180	0.005	0.005	0.000	0.000	0.000	0.000
179	A	250	HOH	0	-0.063	-0.048	30.165	0.000	0.000	0.000	0.000	0.000	0.000
180	A	256	HOH	0	-0.028	-0.035	32.627	-0.003	-0.003	0.000	0.000	0.000	0.000
181	A	258	HOH	0	-0.060	-0.038	36.740	0.000	0.000	0.000	0.000	0.000	0.000
182	A	259	HOH	0	-0.009	-0.013	27.513	0.003	0.003	0.000	0.000	0.000	0.000
183	A	262	HOH	0	0.015	0.002	24.527	-0.002	-0.002	0.000	0.000	0.000	0.000
184	A	269	HOH	0	-0.017	-0.010	33.847	-0.001	-0.001	0.000	0.000	0.000	0.000
185	A	275	HOH	0	-0.029	-0.019	16.698	-0.001	-0.001	0.000	0.000	0.000	0.000
186	A	276	HOH	0	-0.028	-0.022	30.991	0.000	0.000	0.000	0.000	0.000	0.000
187	A	277	HOH	0	-0.007	-0.015	12.798	0.006	0.006	0.000	0.000	0.000	0.000
188	A	285	HOH	0	-0.019	-0.020	21.541	0.004	0.004	0.000	0.000	0.000	0.000
189	A	288	HOH	0	-0.010	-0.011	31.086	-0.002	-0.002	0.000	0.000	0.000	0.000
190	A	292	HOH	0	0.007	-0.005	27.024	-0.003	-0.003	0.000	0.000	0.000	0.000
191	A	293	HOH	0	-0.017	-0.026	12.408	-0.042	-0.042	0.000	0.000	0.000	0.000
192	A	296	HOH	0	-0.019	-0.020	18.980	-0.010	-0.010	0.000	0.000	0.000	0.000
193	A	300	HOH	0	0.004	-0.001	22.002	0.004	0.004	0.000	0.000	0.000	0.000
194	A	301	HOH	0	-0.003	-0.005	33.690	0.001	0.001	0.000	0.000	0.000	0.000
195	A	304	HOH	0	0.027	0.019	28.839	0.001	0.001	0.000	0.000	0.000	0.000
196	A	305	HOH	0	-0.023	-0.040	9.745	-0.035	-0.035	0.000	0.000	0.000	0.000
197	A	316	HOH	0	-0.029	-0.019	23.532	-0.007	-0.007	0.000	0.000	0.000	0.000
198	A	317	HOH	0	0.013	-0.010	30.712	0.003	0.003	0.000	0.000	0.000	0.000
199	A	318	HOH	0	0.025	0.011	30.422	0.001	0.001	0.000	0.000	0.000	0.000
200	A	319	HOH	0	-0.060	-0.056	34.822	-0.002	-0.002	0.000	0.000	0.000	0.000
201	A	322	HOH	0	-0.034	-0.023	28.627	0.002	0.002	0.000	0.000	0.000	0.000
202	A	329	HOH	0	0.033	0.019	16.715	0.014	0.014	0.000	0.000	0.000	0.000
203	A	330	HOH	0	-0.019	-0.019	24.846	0.007	0.007	0.000	0.000	0.000	0.000
204	A	331	HOH	0	0.023	0.012	16.360	-0.007	-0.007	0.000	0.000	0.000	0.000
205	A	347	HOH	0	-0.002	-0.009	29.032	0.000	0.000	0.000	0.000	0.000	0.000
206	A	353	HOH	0	-0.013	-0.017	28.289	-0.002	-0.002	0.000	0.000	0.000	0.000
207	A	360	HOH	0	-0.035	-0.026	36.715	-0.001	-0.001	0.000	0.000	0.000	0.000
208	A	362	HOH	0	-0.003	-0.004	21.088	-0.006	-0.006	0.000	0.000	0.000	0.000
209	A	366	HOH	0	0.007	0.010	22.226	0.002	0.002	0.000	0.000	0.000	0.000
210	A	394	HOH	0	-0.034	-0.028	32.430	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:VAL )