FMO DATABASE

FMODB ID: 43QJN

Calculation Name: 7TX4-A-Xray89

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 7TX4

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2022-12-13

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	177
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 16 beta / 20190613

Total energy (hartree)

FMO2-HF: Electronic energy	-1659699.777522
FMO2-HF: Nuclear repulsion	1596412.217322
FMO2-HF: Total energy	-63287.560199
FMO2-MP2: Total energy	-63473.559998

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.
-7.354	-1.96	1.168	-2.578	-3.983	-0.007

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 : 0.034 / q_NPA : 0.015

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	0.045	0.034	2.355	-1.953	0.806	0.988	-1.456	-2.291	0.004
4	A	6	PHE	0	0.022	0.018	3.716	0.310	0.497	0.012	-0.007	-0.192	0.000
5	A	7	SER	0	0.002	-0.007	7.454	0.113	0.113	0.000	0.000	0.000	0.000
6	A	8	GLY	0	0.037	0.010	9.892	0.013	0.013	0.000	0.000	0.000	0.000
7	A	9	TYR	0	-0.091	-0.066	10.819	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	10	LEU	0	0.014	0.016	14.373	0.016	0.016	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.839	0.921	16.004	0.351	0.351	0.000	0.000	0.000	0.000
10	A	12	LEU	0	0.000	0.002	18.292	0.034	0.034	0.000	0.000	0.000	0.000
11	A	13	THR	0	0.042	0.013	19.896	0.018	0.018	0.000	0.000	0.000	0.000
12	A	14	ASP	-1	-0.875	-0.941	18.962	-0.333	-0.333	0.000	0.000	0.000	0.000
13	A	15	ASN	0	-0.044	-0.023	16.545	-0.019	-0.019	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.031	0.029	16.334	-0.059	-0.059	0.000	0.000	0.000	0.000
15	A	17	TYR	0	-0.003	-0.003	13.968	0.040	0.040	0.000	0.000	0.000	0.000
16	A	18	ILE	0	0.011	0.006	16.281	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	19	LYS	1	0.835	0.900	12.109	0.398	0.398	0.000	0.000	0.000	0.000
18	A	20	ASN	0	0.017	0.014	16.844	0.010	0.010	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.007	-0.018	15.305	0.011	0.011	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.772	-0.888	17.026	-0.203	-0.203	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.014	0.011	13.866	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.012	0.007	13.366	-0.050	-0.050	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.992	-1.006	13.109	-0.125	-0.125	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.788	-0.866	11.012	-0.512	-0.512	0.000	0.000	0.000	0.000
25	A	27	ALA	0	0.010	0.002	9.085	-0.126	-0.126	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.933	0.970	8.270	0.047	0.047	0.000	0.000	0.000	0.000
27	A	29	LYS	1	0.853	0.930	6.326	0.495	0.495	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.099	-0.049	5.247	0.204	0.204	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.903	0.967	3.522	-2.214	-1.340	0.028	-0.312	-0.590	-0.002
30	A	32	PRO	0	0.017	0.014	2.878	-3.867	-2.472	0.141	-0.787	-0.748	-0.009
31	A	33	THR	0	0.002	-0.013	3.794	0.575	0.754	-0.001	-0.016	-0.162	0.000
32	A	34	VAL	0	0.016	0.003	5.790	0.434	0.434	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.015	0.008	9.400	-0.140	-0.140	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.017	0.009	11.374	0.087	0.087	0.000	0.000	0.000	0.000
35	A	37	ASN	0	-0.004	-0.027	15.018	0.008	0.008	0.000	0.000	0.000	0.000
36	A	38	ALA	0	-0.013	0.013	17.930	0.001	0.001	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.025	0.022	21.371	0.020	0.020	0.000	0.000	0.000	0.000
38	A	40	ASN	0	0.006	-0.007	23.242	0.004	0.004	0.000	0.000	0.000	0.000
39	A	41	VAL	0	0.038	0.012	26.161	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	42	TYR	0	0.016	0.005	28.379	0.004	0.004	0.000	0.000	0.000	0.000
41	A	43	LEU	0	-0.020	0.005	22.438	0.005	0.005	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.860	0.939	25.411	0.047	0.047	0.000	0.000	0.000	0.000
43	A	45	HIS	0	-0.002	-0.014	22.094	-0.018	-0.018	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.018	0.011	24.873	0.005	0.005	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.027	0.002	26.759	0.007	0.007	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.017	-0.005	25.067	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	49	VAL	0	0.052	0.018	18.695	0.005	0.005	0.000	0.000	0.000	0.000
48	A	50	ALA	0	0.027	0.024	20.186	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	51	GLY	0	-0.019	-0.003	21.273	0.008	0.008	0.000	0.000	0.000	0.000
50	A	52	ALA	0	-0.017	-0.013	20.364	0.013	0.013	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.020	0.003	14.741	0.008	0.008	0.000	0.000	0.000	0.000
52	A	54	ASN	0	0.059	0.018	17.793	0.022	0.022	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.953	0.985	20.208	0.053	0.053	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.022	-0.008	16.425	0.018	0.018	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.021	-0.007	15.480	0.020	0.020	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.056	-0.033	17.901	0.012	0.012	0.000	0.000	0.000	0.000
57	A	59	ASN	0	0.009	0.007	21.480	0.001	0.001	0.000	0.000	0.000	0.000
58	A	60	ALA	0	0.027	0.025	18.748	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	61	MET	0	0.007	0.018	16.156	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	62	GLN	0	-0.026	-0.023	19.859	-0.012	-0.012	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.008	0.004	23.525	0.000	0.000	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.721	-0.839	18.196	-0.038	-0.038	0.000	0.000	0.000	0.000
63	A	65	SER	0	-0.002	-0.015	21.682	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	66	ASP	-1	-0.831	-0.898	23.574	-0.036	-0.036	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.922	-0.947	25.296	0.002	0.002	0.000	0.000	0.000	0.000
66	A	68	TYR	0	0.017	-0.008	23.294	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.011	-0.008	25.563	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.054	-0.019	28.339	0.000	0.000	0.000	0.000	0.000	0.000
69	A	71	THR	0	-0.039	-0.009	28.077	0.004	0.004	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.081	-0.049	26.157	0.001	0.001	0.000	0.000	0.000	0.000
71	A	73	GLY	0	0.003	0.022	29.351	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	74	PRO	0	-0.035	-0.018	28.898	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	75	LEU	0	-0.007	0.005	23.463	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.892	0.939	28.045	0.122	0.122	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.070	0.021	27.911	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.004	0.003	26.666	0.005	0.005	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.034	-0.008	25.106	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.037	-0.041	20.014	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	81	CYS	0	0.000	0.019	20.506	0.015	0.015	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.004	-0.001	14.494	-0.029	-0.029	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.005	0.013	16.460	0.032	0.032	0.000	0.000	0.000	0.000
82	A	84	SER	0	0.024	0.013	14.057	-0.030	-0.030	0.000	0.000	0.000	0.000
83	A	85	GLY	0	-0.009	0.006	11.127	-0.038	-0.038	0.000	0.000	0.000	0.000
84	A	86	HIS	0	-0.034	-0.034	12.175	0.016	0.016	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.041	-0.037	11.291	0.031	0.031	0.000	0.000	0.000	0.000
86	A	88	LEU	0	-0.054	-0.026	10.555	0.001	0.001	0.000	0.000	0.000	0.000
87	A	89	ALA	0	0.005	-0.002	7.029	-0.206	-0.206	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.869	0.949	6.612	0.229	0.229	0.000	0.000	0.000	0.000
89	A	91	HIS	0	0.039	0.017	8.394	0.120	0.120	0.000	0.000	0.000	0.000
90	A	92	CYS	0	-0.010	0.000	10.926	-0.129	-0.129	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.022	0.008	13.715	0.049	0.049	0.000	0.000	0.000	0.000
92	A	94	HIS	0	0.034	0.000	15.884	-0.023	-0.023	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.031	0.012	18.679	0.014	0.014	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.035	0.019	21.316	0.003	0.003	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.032	0.017	24.992	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	98	PRO	0	-0.010	0.007	26.392	0.010	0.010	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.027	-0.016	29.893	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.078	0.033	31.875	0.007	0.007	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.025	-0.007	33.608	0.008	0.008	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.856	0.930	35.297	0.074	0.074	0.000	0.000	0.000	0.000
101	A	103	GLY	0	0.024	0.023	37.152	0.003	0.003	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.848	-0.896	31.946	-0.097	-0.097	0.000	0.000	0.000	0.000
103	A	105	ASP	-1	-0.842	-0.928	35.182	-0.096	-0.096	0.000	0.000	0.000	0.000
104	A	106	ILE	0	0.043	0.011	31.108	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	107	GLN	0	0.010	-0.005	31.588	-0.014	-0.014	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.034	-0.019	30.115	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	109	LEU	0	-0.015	-0.008	25.747	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	110	LYS	1	0.885	0.941	25.979	0.139	0.139	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.009	-0.015	25.553	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	112	ALA	0	-0.002	0.004	24.059	-0.010	-0.010	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.062	0.014	20.458	-0.027	-0.027	0.000	0.000	0.000	0.000
112	A	114	GLU	-1	-0.844	-0.907	20.618	-0.195	-0.195	0.000	0.000	0.000	0.000
113	A	115	ASN	0	-0.064	-0.031	19.690	0.000	0.000	0.000	0.000	0.000	0.000
114	A	116	PHE	0	0.036	-0.008	16.519	-0.020	-0.020	0.000	0.000	0.000	0.000
115	A	117	ASN	0	-0.026	-0.008	15.786	-0.067	-0.067	0.000	0.000	0.000	0.000
116	A	118	GLN	0	-0.044	-0.002	16.788	0.012	0.012	0.000	0.000	0.000	0.000
117	A	119	HIS	0	-0.020	-0.018	11.541	-0.048	-0.048	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.878	-0.940	10.069	-0.620	-0.620	0.000	0.000	0.000	0.000
119	A	121	VAL	0	-0.021	-0.021	7.420	-0.047	-0.047	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.055	-0.008	9.181	-0.034	-0.034	0.000	0.000	0.000	0.000
121	A	123	LEU	0	-0.024	0.005	9.627	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	124	ALA	0	0.007	-0.010	11.357	0.071	0.071	0.000	0.000	0.000	0.000
123	A	125	PRO	0	-0.017	-0.003	14.997	0.003	0.003	0.000	0.000	0.000	0.000
124	A	126	LEU	0	0.017	0.003	18.368	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.026	-0.005	20.211	0.019	0.019	0.000	0.000	0.000	0.000
126	A	128	SER	0	0.022	-0.018	23.292	0.004	0.004	0.000	0.000	0.000	0.000
127	A	129	ALA	0	0.033	0.034	25.078	0.013	0.013	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.007	-0.006	26.986	0.002	0.002	0.000	0.000	0.000	0.000
129	A	131	ILE	0	0.004	-0.013	28.097	0.007	0.007	0.000	0.000	0.000	0.000
130	A	132	PHE	0	-0.076	-0.026	25.666	0.007	0.007	0.000	0.000	0.000	0.000
131	A	133	GLY	0	0.030	0.007	30.130	0.003	0.003	0.000	0.000	0.000	0.000
132	A	134	ALA	0	-0.008	0.010	29.244	0.005	0.005	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.815	-0.912	30.340	-0.135	-0.135	0.000	0.000	0.000	0.000
134	A	136	PRO	0	0.000	-0.004	26.940	-0.009	-0.009	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.012	-0.009	26.890	-0.016	-0.016	0.000	0.000	0.000	0.000
136	A	138	HIS	0	0.009	0.009	28.486	-0.009	-0.009	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.031	-0.032	25.264	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.017	-0.003	22.203	-0.015	-0.015	0.000	0.000	0.000	0.000
139	A	141	ARG	1	0.897	0.958	24.750	0.148	0.148	0.000	0.000	0.000	0.000
140	A	142	VAL	0	0.053	0.028	25.992	-0.004	-0.004	0.000	0.000	0.000	0.000
141	A	143	CYS	0	-0.051	-0.010	20.515	-0.020	-0.020	0.000	0.000	0.000	0.000
142	A	144	VAL	0	-0.008	-0.012	22.340	-0.018	-0.018	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.923	-0.947	23.546	-0.180	-0.180	0.000	0.000	0.000	0.000
144	A	146	THR	0	-0.114	-0.058	23.345	0.012	0.012	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.077	-0.044	17.505	0.000	0.000	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.948	0.971	19.450	0.241	0.241	0.000	0.000	0.000	0.000
147	A	149	THR	0	-0.028	0.008	14.025	0.007	0.007	0.000	0.000	0.000	0.000
148	A	150	ASN	0	-0.032	-0.008	11.609	0.077	0.077	0.000	0.000	0.000	0.000
149	A	151	VAL	0	0.016	0.000	12.326	-0.114	-0.114	0.000	0.000	0.000	0.000
150	A	152	TYR	0	-0.023	-0.011	10.565	-0.008	-0.008	0.000	0.000	0.000	0.000
151	A	153	LEU	0	0.037	0.009	13.523	-0.007	-0.007	0.000	0.000	0.000	0.000
152	A	154	ALA	0	-0.005	-0.001	14.711	0.010	0.010	0.000	0.000	0.000	0.000
153	A	155	VAL	0	-0.009	0.004	16.739	0.026	0.026	0.000	0.000	0.000	0.000
154	A	156	PHE	0	0.010	0.002	20.223	0.006	0.006	0.000	0.000	0.000	0.000
155	A	157	ASP	-1	-0.804	-0.895	21.381	-0.113	-0.113	0.000	0.000	0.000	0.000
156	A	158	LYS	1	0.898	0.928	24.300	0.131	0.131	0.000	0.000	0.000	0.000
157	A	159	ASN	0	-0.070	-0.049	25.588	0.002	0.002	0.000	0.000	0.000	0.000
158	A	160	LEU	0	-0.003	-0.001	25.509	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	161	TYR	0	-0.011	-0.007	19.445	0.002	0.002	0.000	0.000	0.000	0.000
160	A	162	ASP	-1	-0.777	-0.873	24.545	-0.147	-0.147	0.000	0.000	0.000	0.000
161	A	163	LYS	1	0.912	0.979	27.012	0.123	0.123	0.000	0.000	0.000	0.000
162	A	164	LEU	0	-0.007	0.005	23.875	0.002	0.002	0.000	0.000	0.000	0.000
163	A	165	VAL	0	0.028	0.008	22.728	-0.003	-0.003	0.000	0.000	0.000	0.000
164	A	166	SER	0	-0.028	-0.024	25.444	0.003	0.003	0.000	0.000	0.000	0.000
165	A	167	SER	0	-0.067	-0.045	28.783	0.011	0.011	0.000	0.000	0.000	0.000
166	A	168	PHE	0	-0.078	-0.053	25.655	0.002	0.002	0.000	0.000	0.000	0.000
167	A	169	LEU	-1	-0.924	-0.934	23.135	-0.148	-0.148	0.000	0.000	0.000	0.000
168	A	227	HOH	0	-0.016	-0.019	23.469	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	228	HOH	0	0.009	-0.011	24.468	-0.005	-0.005	0.000	0.000	0.000	0.000
170	A	229	HOH	0	-0.008	-0.032	16.289	-0.011	-0.011	0.000	0.000	0.000	0.000
171	A	232	HOH	0	0.034	0.021	17.747	-0.015	-0.015	0.000	0.000	0.000	0.000
172	A	238	HOH	0	-0.042	-0.041	29.205	0.002	0.002	0.000	0.000	0.000	0.000
173	A	248	HOH	0	-0.002	-0.006	27.406	-0.004	-0.004	0.000	0.000	0.000	0.000
174	A	249	HOH	0	-0.008	-0.016	19.699	0.003	0.003	0.000	0.000	0.000	0.000
175	A	250	HOH	0	-0.017	-0.026	23.933	-0.003	-0.003	0.000	0.000	0.000	0.000
176	A	259	HOH	0	-0.004	-0.008	23.311	-0.003	-0.003	0.000	0.000	0.000	0.000
177	A	286	HOH	0	-0.005	-0.018	29.783	0.000	0.000	0.000	0.000	0.000	0.000

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