FMO DATABASE

FMODB ID: 5N3MZ

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	OptH
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	-1705371.219922
FMO2-HF: Nuclear repulsion	1638724.208053
FMO2-HF: Total energy	-66647.011869
FMO2-MP2: Total energy	-66847.340496

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.
-2.243	0.378	0.399	-1.027	-1.992	-0.003

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 : 0.029 / q_NPA : 0.002

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	0.993	0.975	3.391	-0.643	0.955	0.038	-0.774	-0.862	0.000
4	A	119	TYR	0	0.074	0.043	5.000	0.091	0.264	-0.001	-0.008	-0.164	0.000
5	A	120	LEU	0	-0.015	-0.004	2.548	-0.407	0.252	0.362	-0.227	-0.793	-0.003
6	A	121	LYS	1	0.931	0.957	3.845	1.822	2.013	0.000	-0.018	-0.173	0.000
7	A	122	GLU	-1	-0.979	-0.976	7.484	-0.711	-0.711	0.000	0.000	0.000	0.000
8	A	123	PRO	0	0.027	0.002	10.280	0.041	0.041	0.000	0.000	0.000	0.000
9	A	124	VAL	0	0.000	0.012	13.377	-0.015	-0.015	0.000	0.000	0.000	0.000
10	A	125	VAL	0	-0.012	0.004	15.138	0.056	0.056	0.000	0.000	0.000	0.000
11	A	126	VAL	0	-0.028	-0.011	16.334	-0.014	-0.014	0.000	0.000	0.000	0.000
12	A	127	GLY	0	-0.013	-0.021	17.108	0.010	0.010	0.000	0.000	0.000	0.000
13	A	128	TYR	0	-0.059	-0.038	17.647	0.030	0.030	0.000	0.000	0.000	0.000
14	A	129	VAL	0	0.025	0.014	18.750	-0.017	-0.017	0.000	0.000	0.000	0.000
15	A	130	GLN	0	0.005	-0.005	19.079	0.008	0.008	0.000	0.000	0.000	0.000
16	A	131	ARG	1	0.938	0.972	21.670	-0.030	-0.030	0.000	0.000	0.000	0.000
17	A	132	ASP	-1	-0.916	-0.966	25.146	0.015	0.015	0.000	0.000	0.000	0.000
18	A	133	SER	0	-0.045	-0.013	22.113	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	134	ILE	0	0.006	-0.012	22.656	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	135	ALA	0	0.040	0.016	21.297	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	136	GLN	0	0.041	0.024	23.421	0.003	0.003	0.000	0.000	0.000	0.000
22	A	137	LYS	1	0.902	0.955	26.011	0.024	0.024	0.000	0.000	0.000	0.000
23	A	138	ILE	0	-0.007	0.007	25.026	0.002	0.002	0.000	0.000	0.000	0.000
24	A	139	GLY	0	-0.011	0.007	28.099	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	140	ILE	0	-0.028	-0.013	21.663	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	141	LYS	1	0.906	0.945	24.778	0.090	0.090	0.000	0.000	0.000	0.000
27	A	142	PRO	0	-0.022	-0.025	21.620	-0.014	-0.014	0.000	0.000	0.000	0.000
28	A	143	GLY	0	-0.020	-0.005	21.246	0.011	0.011	0.000	0.000	0.000	0.000
29	A	144	ASP	-1	-0.726	-0.807	22.295	-0.139	-0.139	0.000	0.000	0.000	0.000
30	A	145	LYS	1	0.962	0.983	17.762	0.306	0.306	0.000	0.000	0.000	0.000
31	A	146	ILE	0	-0.012	-0.019	17.821	0.018	0.018	0.000	0.000	0.000	0.000
32	A	147	ILE	0	0.016	0.006	18.409	-0.037	-0.037	0.000	0.000	0.000	0.000
33	A	148	LYS	1	0.911	0.971	20.446	0.183	0.183	0.000	0.000	0.000	0.000
34	A	149	ILE	0	0.005	0.009	18.968	0.016	0.016	0.000	0.000	0.000	0.000
35	A	150	ASN	0	0.090	0.071	22.001	-0.016	-0.016	0.000	0.000	0.000	0.000
36	A	151	GLY	0	-0.065	-0.045	24.591	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	152	TYR	0	0.008	-0.022	18.905	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	153	GLU	-1	-0.894	-0.943	19.345	-0.262	-0.262	0.000	0.000	0.000	0.000
39	A	154	VAL	0	-0.029	-0.007	15.280	-0.026	-0.026	0.000	0.000	0.000	0.000
40	A	155	ARG	1	0.877	0.925	14.569	0.391	0.391	0.000	0.000	0.000	0.000
41	A	156	THR	0	-0.009	-0.002	9.919	-0.024	-0.024	0.000	0.000	0.000	0.000
42	A	157	TRP	0	0.010	-0.013	9.197	0.106	0.106	0.000	0.000	0.000	0.000
43	A	158	GLU	-1	-0.891	-0.945	5.826	-1.553	-1.553	0.000	0.000	0.000	0.000
44	A	159	ASP	-1	-0.762	-0.866	9.367	-0.489	-0.489	0.000	0.000	0.000	0.000
45	A	160	LEU	0	-0.045	-0.016	12.981	0.080	0.080	0.000	0.000	0.000	0.000
46	A	161	ARG	1	0.926	0.959	9.373	0.239	0.239	0.000	0.000	0.000	0.000
47	A	162	ASP	-1	-0.872	-0.940	11.233	-0.470	-0.470	0.000	0.000	0.000	0.000
48	A	163	ALA	0	0.001	-0.006	13.808	0.054	0.054	0.000	0.000	0.000	0.000
49	A	164	LEU	0	-0.040	-0.024	15.861	0.044	0.044	0.000	0.000	0.000	0.000
50	A	165	ILE	0	-0.005	-0.008	13.233	0.038	0.038	0.000	0.000	0.000	0.000
51	A	166	ARG	1	0.913	0.961	17.337	0.171	0.171	0.000	0.000	0.000	0.000
52	A	167	LEU	0	-0.001	0.012	19.189	0.024	0.024	0.000	0.000	0.000	0.000
53	A	168	SER	0	-0.020	0.001	20.787	0.020	0.020	0.000	0.000	0.000	0.000
54	A	169	LEU	0	-0.071	-0.045	18.388	0.015	0.015	0.000	0.000	0.000	0.000
55	A	170	ASP	-1	-0.896	-0.940	22.422	-0.114	-0.114	0.000	0.000	0.000	0.000
56	A	171	GLY	0	-0.062	-0.023	24.958	0.005	0.005	0.000	0.000	0.000	0.000
57	A	172	VAL	0	-0.020	-0.003	25.406	0.006	0.006	0.000	0.000	0.000	0.000
58	A	173	LYS	1	0.920	0.953	26.294	0.048	0.048	0.000	0.000	0.000	0.000
59	A	174	GLU	-1	-0.906	-0.948	27.640	-0.060	-0.060	0.000	0.000	0.000	0.000
60	A	175	THR	0	0.008	-0.004	23.850	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	176	THR	0	0.024	0.024	27.133	0.008	0.008	0.000	0.000	0.000	0.000
62	A	177	LEU	0	-0.034	-0.016	20.609	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	178	PHE	0	-0.003	-0.010	23.454	0.013	0.013	0.000	0.000	0.000	0.000
64	A	179	LEU	0	-0.028	-0.018	22.125	-0.022	-0.022	0.000	0.000	0.000	0.000
65	A	180	GLU	-1	-0.888	-0.943	23.493	-0.207	-0.207	0.000	0.000	0.000	0.000
66	A	181	ARG	1	0.779	0.835	24.576	0.107	0.107	0.000	0.000	0.000	0.000
67	A	182	ASN	0	-0.040	-0.028	27.255	0.003	0.003	0.000	0.000	0.000	0.000
68	A	183	GLY	0	0.020	0.014	27.743	0.006	0.006	0.000	0.000	0.000	0.000
69	A	184	GLU	-1	-0.917	-0.932	28.963	-0.097	-0.097	0.000	0.000	0.000	0.000
70	A	185	VAL	0	-0.006	-0.019	27.098	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	186	LEU	0	-0.032	0.001	27.716	0.012	0.012	0.000	0.000	0.000	0.000
72	A	187	HIS	0	0.021	-0.001	27.464	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	188	LEU	0	-0.004	-0.005	26.266	0.010	0.010	0.000	0.000	0.000	0.000
74	A	189	THR	0	0.026	0.019	27.398	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	190	ILE	0	-0.048	-0.016	22.488	0.006	0.006	0.000	0.000	0.000	0.000
76	A	191	LYS	1	0.921	0.956	25.918	0.033	0.033	0.000	0.000	0.000	0.000
77	A	192	VAL	0	0.004	-0.012	21.998	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	193	PRO	0	-0.065	-0.024	19.748	0.013	0.013	0.000	0.000	0.000	0.000
79	A	194	ASN	0	-0.004	-0.020	21.866	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	195	VAL	0	0.081	0.029	18.092	0.015	0.015	0.000	0.000	0.000	0.000
81	A	196	GLN	0	0.012	0.012	19.654	0.028	0.028	0.000	0.000	0.000	0.000
82	A	197	LYS	1	0.862	0.932	22.231	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	198	GLY	0	0.009	0.010	18.322	0.014	0.014	0.000	0.000	0.000	0.000
84	A	199	GLU	-1	-0.870	-0.918	18.468	-0.020	-0.020	0.000	0.000	0.000	0.000
85	A	200	GLU	-1	-0.931	-0.974	14.167	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	201	LEU	0	0.016	-0.001	17.621	0.006	0.006	0.000	0.000	0.000	0.000
87	A	202	GLY	0	0.030	0.012	17.863	0.009	0.009	0.000	0.000	0.000	0.000
88	A	203	ILE	0	-0.012	0.005	16.095	0.009	0.009	0.000	0.000	0.000	0.000
89	A	204	ALA	0	0.012	0.007	13.861	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	205	PRO	0	0.084	0.058	10.645	0.022	0.022	0.000	0.000	0.000	0.000
91	A	206	LEU	0	0.025	0.011	13.955	0.064	0.064	0.000	0.000	0.000	0.000
92	A	207	VAL	0	0.005	0.017	12.340	-0.032	-0.032	0.000	0.000	0.000	0.000
93	A	208	LYS	1	0.988	0.984	15.421	0.169	0.169	0.000	0.000	0.000	0.000
94	A	209	PRO	0	0.039	0.038	17.720	0.020	0.020	0.000	0.000	0.000	0.000
95	A	210	VAL	0	-0.019	-0.029	18.687	0.007	0.007	0.000	0.000	0.000	0.000
96	A	211	VAL	0	0.006	0.007	17.922	0.022	0.022	0.000	0.000	0.000	0.000
97	A	212	GLY	0	-0.070	-0.054	15.848	-0.041	-0.041	0.000	0.000	0.000	0.000
98	A	213	GLY	0	0.017	0.014	16.717	0.006	0.006	0.000	0.000	0.000	0.000
99	A	214	VAL	0	0.021	0.005	17.581	0.001	0.001	0.000	0.000	0.000	0.000
100	A	215	LYS	1	0.933	0.982	18.940	-0.384	-0.384	0.000	0.000	0.000	0.000
101	A	216	LYS	1	1.027	1.012	20.537	-0.223	-0.223	0.000	0.000	0.000	0.000
102	A	217	GLY	0	-0.023	-0.018	23.902	0.018	0.018	0.000	0.000	0.000	0.000
103	A	218	SER	0	-0.070	-0.030	22.679	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	219	PRO	0	0.065	0.020	24.412	-0.012	-0.012	0.000	0.000	0.000	0.000
105	A	220	ALA	0	0.034	0.010	23.393	-0.018	-0.018	0.000	0.000	0.000	0.000
106	A	221	ASP	-1	-0.866	-0.933	24.670	0.173	0.173	0.000	0.000	0.000	0.000
107	A	222	GLN	0	-0.059	-0.021	26.248	-0.024	-0.024	0.000	0.000	0.000	0.000
108	A	223	VAL	0	0.006	0.026	28.513	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	224	GLY	0	0.000	-0.003	29.295	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	225	ILE	0	-0.044	-0.023	23.798	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	226	LYS	1	0.921	0.960	24.515	-0.110	-0.110	0.000	0.000	0.000	0.000
112	A	227	PRO	0	0.002	-0.011	19.807	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	228	GLY	0	-0.039	-0.021	21.030	-0.016	-0.016	0.000	0.000	0.000	0.000
114	A	229	ASP	-1	-0.741	-0.840	22.440	0.071	0.071	0.000	0.000	0.000	0.000
115	A	230	LEU	0	-0.014	-0.009	22.707	0.004	0.004	0.000	0.000	0.000	0.000
116	A	231	ILE	0	0.006	0.003	21.679	0.000	0.000	0.000	0.000	0.000	0.000
117	A	232	LEU	0	-0.010	-0.006	24.681	-0.009	-0.009	0.000	0.000	0.000	0.000
118	A	233	GLU	-1	-0.865	-0.947	27.427	0.024	0.024	0.000	0.000	0.000	0.000
119	A	234	VAL	0	0.020	0.010	24.911	0.010	0.010	0.000	0.000	0.000	0.000
120	A	235	ASN	0	0.004	-0.009	28.332	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	236	GLY	0	0.028	0.025	31.679	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	237	LYS	1	0.947	0.984	28.830	-0.037	-0.037	0.000	0.000	0.000	0.000
123	A	238	LYS	1	0.956	0.967	28.831	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	239	ILE	0	-0.058	-0.007	22.250	0.002	0.002	0.000	0.000	0.000	0.000
125	A	240	ASN	0	0.014	-0.006	23.531	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	241	THR	0	-0.072	-0.047	18.376	-0.011	-0.011	0.000	0.000	0.000	0.000
127	A	242	TRP	0	0.025	0.006	15.138	0.003	0.003	0.000	0.000	0.000	0.000
128	A	243	TYR	0	0.009	-0.020	13.241	0.052	0.052	0.000	0.000	0.000	0.000
129	A	244	GLU	-1	-0.753	-0.865	17.780	0.026	0.026	0.000	0.000	0.000	0.000
130	A	245	LEU	0	0.003	0.013	19.278	0.008	0.008	0.000	0.000	0.000	0.000
131	A	246	VAL	0	-0.026	-0.018	16.013	0.014	0.014	0.000	0.000	0.000	0.000
132	A	247	GLU	-1	-0.891	-0.957	19.453	0.077	0.077	0.000	0.000	0.000	0.000
133	A	248	GLU	-1	-0.909	-0.968	21.955	0.076	0.076	0.000	0.000	0.000	0.000
134	A	249	VAL	0	-0.014	0.001	21.663	0.001	0.001	0.000	0.000	0.000	0.000
135	A	250	ARG	1	0.897	0.946	19.222	-0.204	-0.204	0.000	0.000	0.000	0.000
136	A	251	LYS	1	0.824	0.912	23.287	-0.090	-0.090	0.000	0.000	0.000	0.000
137	A	252	SER	0	0.007	0.018	26.422	-0.009	-0.009	0.000	0.000	0.000	0.000
138	A	253	GLN	0	-0.029	-0.023	28.250	-0.011	-0.011	0.000	0.000	0.000	0.000
139	A	254	GLY	0	-0.029	-0.008	28.702	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	255	LYS	1	0.948	0.987	29.808	-0.090	-0.090	0.000	0.000	0.000	0.000
141	A	256	ALA	0	0.009	-0.008	30.608	0.007	0.007	0.000	0.000	0.000	0.000
142	A	257	ILE	0	-0.014	0.006	25.980	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	258	LYS	1	0.990	0.990	30.487	-0.058	-0.058	0.000	0.000	0.000	0.000
144	A	259	LEU	0	-0.027	-0.016	25.555	0.001	0.001	0.000	0.000	0.000	0.000
145	A	260	LYS	1	0.913	0.963	29.339	-0.033	-0.033	0.000	0.000	0.000	0.000
146	A	261	ILE	0	-0.023	-0.021	26.374	0.002	0.002	0.000	0.000	0.000	0.000
147	A	262	LEU	0	-0.015	0.000	27.760	-0.006	-0.006	0.000	0.000	0.000	0.000
148	A	263	ARG	1	0.841	0.899	27.548	-0.073	-0.073	0.000	0.000	0.000	0.000
149	A	264	ASN	0	-0.007	-0.017	28.470	0.003	0.003	0.000	0.000	0.000	0.000
150	A	265	GLY	0	0.037	0.019	30.387	-0.002	-0.002	0.000	0.000	0.000	0.000
151	A	266	LYS	1	0.949	0.975	32.383	-0.016	-0.016	0.000	0.000	0.000	0.000
152	A	267	MET	0	0.001	0.018	32.381	0.005	0.005	0.000	0.000	0.000	0.000
153	A	268	ILE	0	0.000	-0.004	31.779	0.002	0.002	0.000	0.000	0.000	0.000
154	A	269	GLU	-1	-0.902	-0.950	32.071	0.046	0.046	0.000	0.000	0.000	0.000
155	A	270	LYS	1	0.826	0.916	29.384	-0.084	-0.084	0.000	0.000	0.000	0.000
156	A	271	GLU	-1	-0.900	-0.958	31.693	0.076	0.076	0.000	0.000	0.000	0.000
157	A	272	LEU	0	-0.010	0.003	25.625	0.005	0.005	0.000	0.000	0.000	0.000
158	A	273	ILE	0	0.060	0.024	29.885	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	274	PRO	0	-0.057	-0.020	25.082	0.014	0.014	0.000	0.000	0.000	0.000
160	A	275	ALA	0	0.055	0.037	25.102	-0.010	-0.010	0.000	0.000	0.000	0.000
161	A	276	LYS	1	0.964	0.971	24.161	-0.163	-0.163	0.000	0.000	0.000	0.000
162	A	277	ASP	-1	-0.854	-0.930	18.915	0.430	0.430	0.000	0.000	0.000	0.000
163	A	278	PRO	0	-0.002	-0.009	21.189	0.012	0.012	0.000	0.000	0.000	0.000
164	A	279	LYS	1	0.933	0.974	16.770	-0.544	-0.544	0.000	0.000	0.000	0.000
165	A	280	THR	0	-0.026	-0.019	15.387	0.018	0.018	0.000	0.000	0.000	0.000
166	A	281	GLY	0	0.017	0.026	17.603	-0.016	-0.016	0.000	0.000	0.000	0.000
167	A	282	THR	0	-0.050	-0.037	19.143	-0.046	-0.046	0.000	0.000	0.000	0.000
168	A	283	TYR	0	-0.034	-0.002	21.699	0.015	0.015	0.000	0.000	0.000	0.000
169	A	284	PHE	0	0.027	0.015	17.088	0.019	0.019	0.000	0.000	0.000	0.000
170	A	285	ILE	0	0.061	0.015	21.068	-0.015	-0.015	0.000	0.000	0.000	0.000
171	A	286	GLY	0	-0.008	-0.008	19.941	-0.013	-0.013	0.000	0.000	0.000	0.000
172	A	287	LEU	0	-0.010	0.003	18.838	-0.005	-0.005	0.000	0.000	0.000	0.000
173	A	288	PHE	0	0.002	-0.003	13.365	0.042	0.042	0.000	0.000	0.000	0.000
174	A	289	PRO	0	0.071	0.049	12.221	-0.047	-0.047	0.000	0.000	0.000	0.000
175	A	290	LYS	1	0.933	0.963	13.649	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	291	THR	0	-0.004	0.008	8.378	-0.028	-0.028	0.000	0.000	0.000	0.000

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