FMO DATABASE

FMODB ID: 4NZ7N

Calculation Name: 7KR1-A-Xray89

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 7KR1

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	176
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1670020.487788
FMO2-HF: Nuclear repulsion	1606413.073796
FMO2-HF: Total energy	-63607.413992
FMO2-MP2: Total energy	-63794.449865

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.
-11.514	-3.81	1.704	-4.001	-5.408	-0.022

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 : 0.015 / 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

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	-0.013	0.002	2.501	-4.076	-0.593	0.802	-1.947	-2.338	-0.008
4	A	6	PHE	0	0.027	0.017	4.382	0.993	1.179	-0.001	-0.027	-0.159	0.000
5	A	7	SER	0	0.015	-0.002	8.049	0.133	0.133	0.000	0.000	0.000	0.000
6	A	8	GLY	0	0.013	-0.001	10.580	0.102	0.102	0.000	0.000	0.000	0.000
7	A	9	TYR	0	-0.078	-0.050	11.030	0.042	0.042	0.000	0.000	0.000	0.000
8	A	10	LEU	0	0.013	0.016	15.092	-0.013	-0.013	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.846	0.912	17.219	0.480	0.480	0.000	0.000	0.000	0.000
10	A	12	LEU	0	-0.022	0.005	19.338	0.039	0.039	0.000	0.000	0.000	0.000
11	A	13	THR	0	0.048	0.022	20.121	0.019	0.019	0.000	0.000	0.000	0.000
12	A	14	ASP	-1	-0.848	-0.935	19.356	-0.437	-0.437	0.000	0.000	0.000	0.000
13	A	15	ASN	0	-0.069	-0.041	15.888	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.018	0.021	15.586	-0.039	-0.039	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.012	0.003	14.095	0.011	0.011	0.000	0.000	0.000	0.000
16	A	18	ILE	0	0.020	0.013	16.587	0.010	0.010	0.000	0.000	0.000	0.000
17	A	19	LYS	1	0.815	0.892	12.219	0.503	0.503	0.000	0.000	0.000	0.000
18	A	20	ASN	0	0.013	0.017	17.335	0.032	0.032	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.026	-0.032	15.614	0.005	0.005	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.788	-0.904	17.119	-0.037	-0.037	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.023	0.017	13.875	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.008	0.004	13.013	-0.004	-0.004	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.830	-0.914	12.781	0.192	0.192	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.845	-0.888	10.970	-0.455	-0.455	0.000	0.000	0.000	0.000
25	A	27	ALA	0	0.034	0.019	8.712	-0.078	-0.078	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.844	0.908	7.732	-0.075	-0.075	0.000	0.000	0.000	0.000
27	A	29	LYS	1	0.844	0.927	8.143	0.463	0.463	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.043	-0.020	5.302	0.306	0.306	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.898	0.957	2.454	-5.767	-4.304	0.599	-0.756	-1.307	-0.002
30	A	32	PRO	0	0.017	0.009	3.031	-3.019	-0.838	0.300	-1.216	-1.265	-0.012
31	A	33	THR	0	0.026	0.005	3.632	-0.031	0.329	0.005	-0.054	-0.311	0.000
32	A	34	VAL	0	-0.004	-0.003	5.073	0.199	0.230	-0.001	-0.001	-0.028	0.000
33	A	35	VAL	0	0.007	0.014	8.688	-0.125	-0.125	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.006	0.004	11.016	0.057	0.057	0.000	0.000	0.000	0.000
35	A	37	ASN	0	-0.027	-0.042	14.620	0.000	0.000	0.000	0.000	0.000	0.000
36	A	38	ALA	0	-0.013	0.006	17.583	-0.008	-0.008	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.008	0.015	21.083	0.016	0.016	0.000	0.000	0.000	0.000
38	A	40	ASN	0	0.010	-0.007	22.824	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	41	VAL	0	0.043	0.014	25.727	0.004	0.004	0.000	0.000	0.000	0.000
40	A	42	TYR	0	0.000	-0.001	27.834	0.002	0.002	0.000	0.000	0.000	0.000
41	A	43	LEU	0	0.002	0.015	21.928	0.008	0.008	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.837	0.927	24.890	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	45	HIS	0	0.025	-0.005	21.486	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.006	0.006	24.316	0.010	0.010	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.023	-0.003	26.239	0.004	0.004	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.003	0.007	24.815	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	49	VAL	0	0.049	0.012	18.565	0.012	0.012	0.000	0.000	0.000	0.000
48	A	50	ALA	0	0.054	0.046	19.960	0.013	0.013	0.000	0.000	0.000	0.000
49	A	51	GLY	0	-0.027	-0.007	20.938	0.019	0.019	0.000	0.000	0.000	0.000
50	A	52	ALA	0	-0.006	-0.011	19.848	0.020	0.020	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.026	0.006	14.466	0.027	0.027	0.000	0.000	0.000	0.000
52	A	54	ASN	0	0.053	0.015	17.474	0.050	0.050	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.932	0.961	19.832	-0.061	-0.061	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.000	0.020	15.851	0.020	0.020	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.016	0.009	15.195	0.045	0.045	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.061	-0.042	17.572	0.026	0.026	0.000	0.000	0.000	0.000
57	A	59	ASN	0	-0.011	-0.007	21.089	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	60	ALA	0	0.024	0.024	18.242	-0.014	-0.014	0.000	0.000	0.000	0.000
59	A	61	MET	0	0.017	0.021	15.610	-0.020	-0.020	0.000	0.000	0.000	0.000
60	A	62	GLN	0	-0.029	-0.026	19.231	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.004	0.002	22.918	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.726	-0.841	17.433	0.128	0.128	0.000	0.000	0.000	0.000
63	A	65	SER	0	-0.007	-0.015	21.000	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	66	ASP	-1	-0.833	-0.901	22.834	0.043	0.043	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.926	-0.951	24.254	0.073	0.073	0.000	0.000	0.000	0.000
66	A	68	TYR	0	0.033	0.010	22.430	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.057	-0.030	24.845	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.032	-0.010	27.652	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.066	-0.024	26.757	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.047	-0.027	26.829	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	73	GLY	0	0.015	0.017	28.893	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	74	PRO	0	-0.062	-0.029	28.755	0.000	0.000	0.000	0.000	0.000	0.000
73	A	75	LEU	0	0.044	0.017	22.853	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.943	0.961	27.569	0.041	0.041	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.026	0.010	27.421	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	78	GLY	0	-0.001	0.005	26.295	0.000	0.000	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.027	-0.007	24.760	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.050	-0.054	19.567	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	81	CYS	0	-0.011	0.015	19.829	0.009	0.009	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.006	0.000	13.821	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.001	0.012	15.690	0.015	0.015	0.000	0.000	0.000	0.000
82	A	84	SER	0	0.035	0.016	13.243	0.006	0.006	0.000	0.000	0.000	0.000
83	A	85	GLY	0	-0.014	0.005	10.568	-0.046	-0.046	0.000	0.000	0.000	0.000
84	A	86	HIS	0	-0.042	-0.042	11.609	0.060	0.060	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.030	-0.029	10.746	0.043	0.043	0.000	0.000	0.000	0.000
86	A	88	LEU	0	-0.043	-0.021	10.066	0.111	0.111	0.000	0.000	0.000	0.000
87	A	89	ALA	0	0.018	0.006	6.694	-0.081	-0.081	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.871	0.957	5.860	-0.061	-0.061	0.000	0.000	0.000	0.000
89	A	91	HIS	0	0.018	0.004	7.637	0.063	0.063	0.000	0.000	0.000	0.000
90	A	92	CYS	0	0.000	-0.001	10.254	-0.051	-0.051	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.025	0.004	13.008	0.015	0.015	0.000	0.000	0.000	0.000
92	A	94	HIS	0	0.024	0.000	15.200	-0.031	-0.031	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.045	0.017	18.154	0.001	0.001	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.040	0.009	20.784	0.004	0.004	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.044	0.027	24.495	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.003	0.008	26.050	0.011	0.011	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.017	-0.006	29.631	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.040	0.014	31.689	0.004	0.004	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.031	-0.012	33.690	0.003	0.003	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.804	0.908	32.428	0.033	0.033	0.000	0.000	0.000	0.000
101	A	103	GLY	0	0.014	0.016	36.984	0.002	0.002	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.778	-0.845	31.711	-0.048	-0.048	0.000	0.000	0.000	0.000
103	A	105	ASP	-1	-0.812	-0.921	34.675	-0.072	-0.072	0.000	0.000	0.000	0.000
104	A	106	ILE	0	0.052	0.020	30.871	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	107	GLN	0	0.009	0.004	31.135	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.053	-0.029	29.726	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	109	LEU	0	-0.033	-0.021	25.430	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.917	0.946	25.523	0.122	0.122	0.000	0.000	0.000	0.000
109	A	111	SER	0	0.000	-0.012	25.043	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	112	ALA	0	0.003	0.005	23.581	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.032	-0.006	19.925	-0.013	-0.013	0.000	0.000	0.000	0.000
112	A	114	GLU	-1	-0.743	-0.835	20.254	-0.190	-0.190	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.066	-0.020	19.241	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	116	PHE	0	0.019	-0.010	16.014	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	117	ASN	0	-0.008	-0.002	15.268	-0.064	-0.064	0.000	0.000	0.000	0.000
116	A	118	GLN	0	-0.068	-0.023	16.309	0.009	0.009	0.000	0.000	0.000	0.000
117	A	119	HIS	0	-0.007	-0.006	11.155	0.001	0.001	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.904	-0.944	9.308	-0.639	-0.639	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.001	-0.017	6.887	-0.073	-0.073	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.051	-0.007	8.721	0.067	0.067	0.000	0.000	0.000	0.000
121	A	123	LEU	0	-0.030	0.007	9.577	-0.056	-0.056	0.000	0.000	0.000	0.000
122	A	124	ALA	0	0.013	-0.006	11.302	0.102	0.102	0.000	0.000	0.000	0.000
123	A	125	PRO	0	-0.023	-0.006	14.928	-0.014	-0.014	0.000	0.000	0.000	0.000
124	A	126	LEU	0	0.021	0.003	18.398	-0.008	-0.008	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.033	-0.007	19.892	0.024	0.024	0.000	0.000	0.000	0.000
126	A	128	SER	0	0.023	-0.015	23.126	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	129	ALA	0	0.044	0.039	25.396	0.007	0.007	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.009	-0.005	27.219	0.008	0.008	0.000	0.000	0.000	0.000
129	A	131	ILE	0	-0.001	-0.016	28.480	0.002	0.002	0.000	0.000	0.000	0.000
130	A	132	PHE	0	-0.073	-0.030	25.824	0.005	0.005	0.000	0.000	0.000	0.000
131	A	133	GLY	0	0.024	0.012	30.160	0.000	0.000	0.000	0.000	0.000	0.000
132	A	134	ALA	0	0.001	0.013	29.326	0.001	0.001	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.803	-0.914	30.463	-0.113	-0.113	0.000	0.000	0.000	0.000
134	A	136	PRO	0	-0.015	-0.009	26.938	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.023	0.003	26.734	-0.016	-0.016	0.000	0.000	0.000	0.000
136	A	138	HIS	0	0.022	0.010	28.129	-0.012	-0.012	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.021	-0.029	25.084	-0.012	-0.012	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.002	-0.001	22.007	-0.012	-0.012	0.000	0.000	0.000	0.000
139	A	141	ARG	1	0.903	0.943	24.232	0.143	0.143	0.000	0.000	0.000	0.000
140	A	142	VAL	0	0.016	0.013	25.438	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	143	CYS	0	-0.066	-0.019	19.929	-0.018	-0.018	0.000	0.000	0.000	0.000
142	A	144	VAL	0	-0.020	-0.026	21.516	-0.015	-0.015	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.965	-0.960	22.778	-0.167	-0.167	0.000	0.000	0.000	0.000
144	A	146	THR	0	-0.049	-0.014	22.436	0.010	0.010	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.082	-0.045	16.842	0.001	0.001	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.887	0.934	18.884	0.204	0.204	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.030	0.005	13.338	-0.014	-0.014	0.000	0.000	0.000	0.000
148	A	150	ASN	0	-0.025	-0.005	10.850	0.035	0.035	0.000	0.000	0.000	0.000
149	A	151	VAL	0	0.027	0.008	11.724	-0.052	-0.052	0.000	0.000	0.000	0.000
150	A	152	TYR	0	-0.013	-0.008	10.120	-0.051	-0.051	0.000	0.000	0.000	0.000
151	A	153	LEU	0	0.012	-0.002	13.229	0.036	0.036	0.000	0.000	0.000	0.000
152	A	154	ALA	0	0.001	0.004	14.578	-0.016	-0.016	0.000	0.000	0.000	0.000
153	A	155	VAL	0	-0.005	0.002	16.605	0.041	0.041	0.000	0.000	0.000	0.000
154	A	156	PHE	0	-0.004	-0.001	20.299	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	157	ASP	-1	-0.810	-0.902	21.547	-0.090	-0.090	0.000	0.000	0.000	0.000
156	A	158	LYS	1	0.907	0.931	24.701	0.136	0.136	0.000	0.000	0.000	0.000
157	A	159	ASN	0	-0.066	-0.045	25.840	-0.006	-0.006	0.000	0.000	0.000	0.000
158	A	160	LEU	0	-0.029	-0.015	25.460	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	161	TYR	0	0.000	0.002	19.945	-0.004	-0.004	0.000	0.000	0.000	0.000
160	A	162	ASP	-1	-0.779	-0.874	24.904	-0.161	-0.161	0.000	0.000	0.000	0.000
161	A	163	LYS	1	0.951	0.984	27.565	0.099	0.099	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.028	-0.007	23.804	0.000	0.000	0.000	0.000	0.000	0.000
163	A	165	VAL	0	0.002	-0.010	23.498	-0.008	-0.008	0.000	0.000	0.000	0.000
164	A	166	SER	0	-0.040	-0.033	26.209	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	167	SER	0	-0.007	-0.016	29.454	0.005	0.005	0.000	0.000	0.000	0.000
166	A	168	PHE	0	-0.090	-0.057	24.772	0.002	0.002	0.000	0.000	0.000	0.000
167	A	169	LEU	0	-0.054	-0.037	24.250	-0.009	-0.009	0.000	0.000	0.000	0.000
168	A	170	GLU	-2	-1.853	-1.854	28.717	-0.278	-0.278	0.000	0.000	0.000	0.000
169	A	223	HOH	0	-0.007	-0.031	15.664	-0.014	-0.014	0.000	0.000	0.000	0.000
170	A	228	HOH	0	-0.014	-0.019	23.062	-0.004	-0.004	0.000	0.000	0.000	0.000
171	A	231	HOH	0	-0.064	-0.057	28.878	0.003	0.003	0.000	0.000	0.000	0.000
172	A	233	HOH	0	0.005	-0.011	24.248	-0.006	-0.006	0.000	0.000	0.000	0.000
173	A	241	HOH	0	0.024	0.012	18.483	0.004	0.004	0.000	0.000	0.000	0.000
174	A	244	HOH	0	-0.022	-0.026	23.390	-0.004	-0.004	0.000	0.000	0.000	0.000
175	A	247	HOH	0	-0.009	-0.017	19.653	0.000	0.000	0.000	0.000	0.000	0.000
176	A	268	HOH	0	-0.054	-0.050	30.563	0.003	0.003	0.000	0.000	0.000	0.000

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