FMO DATABASE

FMODB ID: YNY32

Calculation Name: 3WKM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3WKM

Chain ID: A

ChEMBL ID:

UniProt ID: O67776

Base Structure: X-ray

Registration Date: 2023-09-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	176
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1708115.887854
FMO2-HF: Nuclear repulsion	1641467.788227
FMO2-HF: Total energy	-66648.099627
FMO2-MP2: Total energy	-66848.448353

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:116:VAL)

Summations of interaction energy for fragment #1(A:116: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.
-3.236	-0.593	0.342	-1.007	-1.977	-0.001

Interaction energy analysis for fragmet #1(A:116:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : -0.003

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	118	LYS	1	0.985	0.975	3.496	-1.223	0.361	0.024	-0.763	-0.845	0.001
4	A	119	TYR	0	0.079	0.045	5.059	0.005	0.178	-0.001	-0.008	-0.163	0.000
5	A	120	LEU	0	-0.034	-0.009	2.559	-0.432	0.211	0.317	-0.207	-0.753	-0.002
6	A	121	LYS	1	0.873	0.902	3.611	1.713	1.956	0.002	-0.029	-0.216	0.000
7	A	122	GLU	-1	-0.956	-0.970	7.538	-0.561	-0.561	0.000	0.000	0.000	0.000
8	A	123	PRO	0	0.051	0.016	10.344	0.019	0.019	0.000	0.000	0.000	0.000
9	A	124	VAL	0	-0.006	0.010	13.289	-0.003	-0.003	0.000	0.000	0.000	0.000
10	A	125	VAL	0	-0.004	0.006	15.153	0.047	0.047	0.000	0.000	0.000	0.000
11	A	126	VAL	0	-0.032	-0.013	16.357	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	127	GLY	0	-0.009	-0.019	17.136	0.011	0.011	0.000	0.000	0.000	0.000
13	A	128	TYR	0	-0.059	-0.043	17.624	0.028	0.028	0.000	0.000	0.000	0.000
14	A	129	VAL	0	0.023	0.015	18.793	-0.017	-0.017	0.000	0.000	0.000	0.000
15	A	130	GLN	0	0.022	0.006	18.859	0.003	0.003	0.000	0.000	0.000	0.000
16	A	131	ARG	1	0.861	0.918	21.721	-0.036	-0.036	0.000	0.000	0.000	0.000
17	A	132	ASP	-1	-0.825	-0.894	25.200	0.021	0.021	0.000	0.000	0.000	0.000
18	A	133	SER	0	-0.013	-0.008	22.185	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	134	ILE	0	0.010	-0.007	23.067	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	135	ALA	0	0.034	0.022	21.323	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	136	GLN	0	0.048	0.022	23.466	0.002	0.002	0.000	0.000	0.000	0.000
22	A	137	LYS	1	0.843	0.922	26.056	0.016	0.016	0.000	0.000	0.000	0.000
23	A	138	ILE	0	0.006	0.019	25.024	0.001	0.001	0.000	0.000	0.000	0.000
24	A	139	GLY	0	-0.012	0.005	28.120	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	140	ILE	0	-0.017	-0.013	21.641	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	141	LYS	1	0.885	0.939	24.784	0.066	0.066	0.000	0.000	0.000	0.000
27	A	142	PRO	0	-0.016	-0.027	21.661	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	143	GLY	0	-0.018	-0.005	21.271	0.008	0.008	0.000	0.000	0.000	0.000
29	A	144	ASP	-1	-0.730	-0.805	22.260	-0.110	-0.110	0.000	0.000	0.000	0.000
30	A	145	LYS	1	0.802	0.886	18.718	0.198	0.198	0.000	0.000	0.000	0.000
31	A	146	ILE	0	-0.010	-0.013	17.824	0.014	0.014	0.000	0.000	0.000	0.000
32	A	147	ILE	0	0.019	0.006	18.422	-0.031	-0.031	0.000	0.000	0.000	0.000
33	A	148	LYS	1	0.851	0.921	20.479	0.177	0.177	0.000	0.000	0.000	0.000
34	A	149	ILE	0	0.009	0.011	18.946	0.016	0.016	0.000	0.000	0.000	0.000
35	A	150	ASN	0	0.051	0.037	22.023	-0.017	-0.017	0.000	0.000	0.000	0.000
36	A	151	GLY	0	-0.011	-0.011	24.416	0.003	0.003	0.000	0.000	0.000	0.000
37	A	152	TYR	0	-0.029	-0.021	18.962	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	153	GLU	-1	-0.813	-0.893	19.105	-0.230	-0.230	0.000	0.000	0.000	0.000
39	A	154	VAL	0	-0.046	-0.017	15.238	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	155	ARG	1	0.886	0.929	14.560	0.370	0.370	0.000	0.000	0.000	0.000
41	A	156	THR	0	-0.044	-0.032	9.986	-0.050	-0.050	0.000	0.000	0.000	0.000
42	A	157	TRP	0	-0.007	-0.021	9.185	0.092	0.092	0.000	0.000	0.000	0.000
43	A	158	GLU	-1	-0.827	-0.890	5.767	-1.565	-1.565	0.000	0.000	0.000	0.000
44	A	159	ASP	-1	-0.753	-0.848	9.384	-0.463	-0.463	0.000	0.000	0.000	0.000
45	A	160	LEU	0	-0.033	-0.009	13.014	0.068	0.068	0.000	0.000	0.000	0.000
46	A	161	ARG	1	0.859	0.917	9.382	0.254	0.254	0.000	0.000	0.000	0.000
47	A	162	ASP	-1	-0.863	-0.941	11.286	-0.443	-0.443	0.000	0.000	0.000	0.000
48	A	163	ALA	0	-0.009	-0.008	13.832	0.048	0.048	0.000	0.000	0.000	0.000
49	A	164	LEU	0	-0.044	-0.024	15.713	0.040	0.040	0.000	0.000	0.000	0.000
50	A	165	ILE	0	-0.005	-0.009	13.276	0.036	0.036	0.000	0.000	0.000	0.000
51	A	166	ARG	1	0.850	0.924	17.215	0.196	0.196	0.000	0.000	0.000	0.000
52	A	167	LEU	0	0.020	0.010	19.216	0.022	0.022	0.000	0.000	0.000	0.000
53	A	168	SER	0	-0.041	-0.034	20.924	0.020	0.020	0.000	0.000	0.000	0.000
54	A	169	LEU	0	-0.081	-0.041	18.390	0.015	0.015	0.000	0.000	0.000	0.000
55	A	170	ASP	-1	-0.839	-0.896	22.459	-0.133	-0.133	0.000	0.000	0.000	0.000
56	A	171	GLY	0	-0.054	-0.022	24.987	0.007	0.007	0.000	0.000	0.000	0.000
57	A	172	VAL	0	-0.003	-0.001	25.490	0.007	0.007	0.000	0.000	0.000	0.000
58	A	173	LYS	1	0.906	0.953	26.332	0.061	0.061	0.000	0.000	0.000	0.000
59	A	174	GLU	-1	-0.908	-0.946	27.680	-0.057	-0.057	0.000	0.000	0.000	0.000
60	A	175	THR	0	-0.007	-0.015	23.997	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	176	THR	0	0.017	0.028	27.174	0.006	0.006	0.000	0.000	0.000	0.000
62	A	177	LEU	0	-0.037	-0.021	20.633	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	178	PHE	0	0.000	-0.007	23.483	0.012	0.012	0.000	0.000	0.000	0.000
64	A	179	LEU	0	-0.022	-0.016	22.305	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	180	GLU	-1	-0.788	-0.873	23.517	-0.176	-0.176	0.000	0.000	0.000	0.000
66	A	181	ARG	1	0.799	0.840	24.630	0.084	0.084	0.000	0.000	0.000	0.000
67	A	182	ASN	0	-0.023	-0.019	27.341	0.002	0.002	0.000	0.000	0.000	0.000
68	A	183	GLY	0	0.014	0.008	27.824	0.005	0.005	0.000	0.000	0.000	0.000
69	A	184	GLU	-1	-0.915	-0.929	29.038	-0.079	-0.079	0.000	0.000	0.000	0.000
70	A	185	VAL	0	-0.013	-0.025	27.121	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	186	LEU	0	-0.036	-0.004	27.735	0.010	0.010	0.000	0.000	0.000	0.000
72	A	187	HIS	0	0.028	0.002	27.486	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	188	LEU	0	-0.006	-0.003	26.612	0.009	0.009	0.000	0.000	0.000	0.000
74	A	189	THR	0	0.041	0.022	27.429	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	190	ILE	0	-0.044	-0.014	22.459	0.006	0.006	0.000	0.000	0.000	0.000
76	A	191	LYS	1	0.867	0.918	25.512	0.040	0.040	0.000	0.000	0.000	0.000
77	A	192	VAL	0	0.004	-0.009	22.135	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	193	PRO	0	-0.051	-0.016	19.753	0.012	0.012	0.000	0.000	0.000	0.000
79	A	194	ASN	0	0.026	0.007	21.911	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	195	VAL	0	0.077	0.026	18.121	0.013	0.013	0.000	0.000	0.000	0.000
81	A	196	GLN	0	0.008	0.011	19.687	0.021	0.021	0.000	0.000	0.000	0.000
82	A	197	LYS	1	0.866	0.938	22.262	0.002	0.002	0.000	0.000	0.000	0.000
83	A	198	GLY	0	0.013	0.010	18.365	0.014	0.014	0.000	0.000	0.000	0.000
84	A	199	GLU	-1	-0.831	-0.887	18.517	-0.028	-0.028	0.000	0.000	0.000	0.000
85	A	200	GLU	-1	-0.863	-0.933	13.980	-0.065	-0.065	0.000	0.000	0.000	0.000
86	A	201	LEU	0	0.023	0.006	17.662	0.008	0.008	0.000	0.000	0.000	0.000
87	A	202	GLY	0	0.022	0.009	17.898	0.009	0.009	0.000	0.000	0.000	0.000
88	A	203	ILE	0	-0.004	0.007	16.099	0.012	0.012	0.000	0.000	0.000	0.000
89	A	204	ALA	0	0.002	0.001	13.942	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	205	PRO	0	0.090	0.065	10.651	0.018	0.018	0.000	0.000	0.000	0.000
91	A	206	LEU	0	0.027	0.011	13.986	0.061	0.061	0.000	0.000	0.000	0.000
92	A	207	VAL	0	0.004	0.018	12.388	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	208	LYS	1	0.994	0.987	15.444	0.071	0.071	0.000	0.000	0.000	0.000
94	A	209	PRO	0	0.033	0.040	17.742	0.029	0.029	0.000	0.000	0.000	0.000
95	A	210	VAL	0	-0.024	-0.032	18.723	0.002	0.002	0.000	0.000	0.000	0.000
96	A	211	VAL	0	0.007	0.006	17.942	0.033	0.033	0.000	0.000	0.000	0.000
97	A	212	GLY	0	-0.035	-0.030	16.179	-0.038	-0.038	0.000	0.000	0.000	0.000
98	A	213	GLY	0	0.021	0.010	16.953	0.009	0.009	0.000	0.000	0.000	0.000
99	A	214	VAL	0	0.002	-0.006	17.831	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	215	LYS	1	0.934	0.989	19.034	-0.374	-0.374	0.000	0.000	0.000	0.000
101	A	216	LYS	1	1.038	1.019	20.545	-0.238	-0.238	0.000	0.000	0.000	0.000
102	A	217	GLY	0	-0.005	0.001	23.923	0.013	0.013	0.000	0.000	0.000	0.000
103	A	218	SER	0	-0.071	-0.026	22.693	-0.014	-0.014	0.000	0.000	0.000	0.000
104	A	219	PRO	0	0.072	0.023	24.425	-0.010	-0.010	0.000	0.000	0.000	0.000
105	A	220	ALA	0	0.034	0.011	23.388	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	221	ASP	-1	-0.869	-0.953	24.651	0.194	0.194	0.000	0.000	0.000	0.000
107	A	222	GLN	0	-0.058	-0.030	26.259	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	223	VAL	0	0.010	0.025	28.436	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	224	GLY	0	-0.003	0.005	29.308	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	225	ILE	0	-0.018	-0.004	23.817	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	226	LYS	1	0.846	0.922	24.662	-0.162	-0.162	0.000	0.000	0.000	0.000
112	A	227	PRO	0	0.014	-0.003	20.062	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	228	GLY	0	-0.040	-0.025	21.347	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	229	ASP	-1	-0.737	-0.811	22.761	0.109	0.109	0.000	0.000	0.000	0.000
115	A	230	LEU	0	-0.018	-0.009	22.726	0.011	0.011	0.000	0.000	0.000	0.000
116	A	231	ILE	0	0.015	0.005	21.909	-0.006	-0.006	0.000	0.000	0.000	0.000
117	A	232	LEU	0	-0.009	0.000	24.702	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	233	GLU	-1	-0.805	-0.900	27.448	0.041	0.041	0.000	0.000	0.000	0.000
119	A	234	VAL	0	0.010	0.003	24.884	0.010	0.010	0.000	0.000	0.000	0.000
120	A	235	ASN	0	0.021	0.002	28.351	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	236	GLY	0	0.028	0.029	31.697	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	237	LYS	1	0.897	0.959	26.634	-0.059	-0.059	0.000	0.000	0.000	0.000
123	A	238	LYS	1	0.911	0.937	28.852	-0.028	-0.028	0.000	0.000	0.000	0.000
124	A	239	ILE	0	-0.078	-0.016	22.440	0.000	0.000	0.000	0.000	0.000	0.000
125	A	240	ASN	0	-0.002	-0.015	23.426	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	241	THR	0	-0.042	-0.027	18.443	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	242	TRP	0	0.024	0.008	15.431	0.007	0.007	0.000	0.000	0.000	0.000
128	A	243	TYR	0	0.008	-0.023	13.065	0.045	0.045	0.000	0.000	0.000	0.000
129	A	244	GLU	-1	-0.748	-0.871	17.799	0.051	0.051	0.000	0.000	0.000	0.000
130	A	245	LEU	0	0.009	0.016	19.456	0.003	0.003	0.000	0.000	0.000	0.000
131	A	246	VAL	0	-0.023	-0.017	16.028	0.008	0.008	0.000	0.000	0.000	0.000
132	A	247	GLU	-1	-0.866	-0.920	19.470	0.082	0.082	0.000	0.000	0.000	0.000
133	A	248	GLU	-1	-0.846	-0.926	21.972	0.086	0.086	0.000	0.000	0.000	0.000
134	A	249	VAL	0	-0.021	-0.002	21.680	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	250	ARG	1	0.894	0.955	19.049	-0.200	-0.200	0.000	0.000	0.000	0.000
136	A	251	LYS	1	0.783	0.863	23.300	-0.097	-0.097	0.000	0.000	0.000	0.000
137	A	252	SER	0	-0.015	-0.007	26.203	-0.010	-0.010	0.000	0.000	0.000	0.000
138	A	253	GLN	0	0.011	0.000	28.260	-0.010	-0.010	0.000	0.000	0.000	0.000
139	A	254	GLY	0	-0.025	-0.009	28.700	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	255	LYS	1	0.906	0.964	29.818	-0.090	-0.090	0.000	0.000	0.000	0.000
141	A	256	ALA	0	0.004	-0.013	30.621	0.007	0.007	0.000	0.000	0.000	0.000
142	A	257	ILE	0	-0.019	-0.001	25.834	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	258	LYS	1	0.904	0.932	30.503	-0.073	-0.073	0.000	0.000	0.000	0.000
144	A	259	LEU	0	-0.031	-0.016	25.681	0.002	0.002	0.000	0.000	0.000	0.000
145	A	260	LYS	1	0.879	0.945	29.357	-0.055	-0.055	0.000	0.000	0.000	0.000
146	A	261	ILE	0	-0.031	-0.027	25.995	0.005	0.005	0.000	0.000	0.000	0.000
147	A	262	LEU	0	-0.004	0.003	27.782	-0.008	-0.008	0.000	0.000	0.000	0.000
148	A	263	ARG	1	0.827	0.867	27.568	-0.104	-0.104	0.000	0.000	0.000	0.000
149	A	264	ASN	0	-0.006	-0.017	28.809	0.000	0.000	0.000	0.000	0.000	0.000
150	A	265	GLY	0	0.034	0.018	30.625	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	266	LYS	1	0.952	0.979	32.584	-0.044	-0.044	0.000	0.000	0.000	0.000
152	A	267	MET	0	0.001	0.012	32.401	0.007	0.007	0.000	0.000	0.000	0.000
153	A	268	ILE	0	-0.003	-0.001	31.505	0.000	0.000	0.000	0.000	0.000	0.000
154	A	269	GLU	-1	-0.863	-0.940	32.090	0.064	0.064	0.000	0.000	0.000	0.000
155	A	270	LYS	1	0.831	0.913	29.293	-0.103	-0.103	0.000	0.000	0.000	0.000
156	A	271	GLU	-1	-0.824	-0.900	31.716	0.082	0.082	0.000	0.000	0.000	0.000
157	A	272	LEU	0	-0.010	0.001	25.642	0.004	0.004	0.000	0.000	0.000	0.000
158	A	273	ILE	0	0.056	0.026	29.899	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	274	PRO	0	-0.046	-0.016	25.003	0.013	0.013	0.000	0.000	0.000	0.000
160	A	275	ALA	0	0.049	0.033	25.134	-0.012	-0.012	0.000	0.000	0.000	0.000
161	A	276	LYS	1	0.951	0.971	24.169	-0.145	-0.145	0.000	0.000	0.000	0.000
162	A	277	ASP	-1	-0.879	-0.945	19.418	0.387	0.387	0.000	0.000	0.000	0.000
163	A	278	PRO	0	0.011	-0.008	21.193	0.010	0.010	0.000	0.000	0.000	0.000
164	A	279	LYS	1	0.944	0.981	16.842	-0.496	-0.496	0.000	0.000	0.000	0.000
165	A	280	THR	0	-0.027	-0.012	15.584	0.015	0.015	0.000	0.000	0.000	0.000
166	A	281	GLY	0	0.029	0.029	17.607	-0.016	-0.016	0.000	0.000	0.000	0.000
167	A	282	THR	0	-0.054	-0.040	19.095	-0.040	-0.040	0.000	0.000	0.000	0.000
168	A	283	TYR	0	-0.022	0.002	21.707	0.015	0.015	0.000	0.000	0.000	0.000
169	A	284	PHE	0	0.025	0.017	16.665	0.018	0.018	0.000	0.000	0.000	0.000
170	A	285	ILE	0	0.063	0.018	21.079	-0.016	-0.016	0.000	0.000	0.000	0.000
171	A	286	GLY	0	0.003	-0.011	19.932	-0.012	-0.012	0.000	0.000	0.000	0.000
172	A	287	LEU	0	-0.019	0.000	18.853	-0.001	-0.001	0.000	0.000	0.000	0.000
173	A	288	PHE	0	0.016	0.004	13.704	0.039	0.039	0.000	0.000	0.000	0.000
174	A	289	PRO	0	0.070	0.047	12.167	-0.048	-0.048	0.000	0.000	0.000	0.000
175	A	290	LYS	1	0.900	0.944	13.667	-0.086	-0.086	0.000	0.000	0.000	0.000
176	A	291	THR	0	0.003	0.014	8.603	-0.002	-0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:116:VAL)