FMO DATABASE

FMODB ID: VKRM1

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	OptAll
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	-1708246.899857
FMO2-HF: Nuclear repulsion	1641598.428454
FMO2-HF: Total energy	-66648.471402
FMO2-MP2: Total energy	-66848.817322

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.
-2.584	0.066999999999999	0.407	-0.862	-2.196	-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 : 0.024 / 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	0.982	0.991	3.831	-0.624	0.768	0.007	-0.561	-0.837	0.001
4	A	119	TYR	0	0.060	0.030	4.735	-0.035	0.142	-0.001	-0.008	-0.168	0.000
5	A	120	LEU	0	-0.015	-0.001	2.508	-0.427	0.238	0.374	-0.221	-0.818	-0.002
6	A	121	LYS	1	0.853	0.897	3.143	1.580	1.997	0.027	-0.072	-0.373	0.000
7	A	122	GLU	-1	-0.934	-0.964	7.123	-0.647	-0.647	0.000	0.000	0.000	0.000
8	A	123	PRO	0	0.049	0.010	9.980	0.016	0.016	0.000	0.000	0.000	0.000
9	A	124	VAL	0	-0.001	0.016	13.272	0.005	0.005	0.000	0.000	0.000	0.000
10	A	125	VAL	0	0.002	0.003	15.047	0.046	0.046	0.000	0.000	0.000	0.000
11	A	126	VAL	0	-0.021	-0.010	16.441	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	127	GLY	0	-0.015	-0.023	17.371	0.011	0.011	0.000	0.000	0.000	0.000
13	A	128	TYR	0	-0.036	-0.026	17.647	0.028	0.028	0.000	0.000	0.000	0.000
14	A	129	VAL	0	0.031	0.011	18.789	-0.020	-0.020	0.000	0.000	0.000	0.000
15	A	130	GLN	0	0.002	0.010	18.436	0.002	0.002	0.000	0.000	0.000	0.000
16	A	131	ARG	1	0.890	0.916	21.821	-0.022	-0.022	0.000	0.000	0.000	0.000
17	A	132	ASP	-1	-0.827	-0.884	24.983	0.009	0.009	0.000	0.000	0.000	0.000
18	A	133	SER	0	-0.021	-0.005	22.291	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	134	ILE	0	0.011	0.006	22.658	0.001	0.001	0.000	0.000	0.000	0.000
20	A	135	ALA	0	0.043	0.022	21.307	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	136	GLN	0	0.010	0.006	23.448	0.004	0.004	0.000	0.000	0.000	0.000
22	A	137	LYS	1	0.858	0.918	26.114	0.023	0.023	0.000	0.000	0.000	0.000
23	A	138	ILE	0	0.005	0.018	24.780	0.001	0.001	0.000	0.000	0.000	0.000
24	A	139	GLY	0	0.031	0.029	27.818	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	140	ILE	0	-0.010	0.003	21.415	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	141	LYS	1	0.823	0.897	24.188	0.077	0.077	0.000	0.000	0.000	0.000
27	A	142	PRO	0	-0.033	-0.024	21.469	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	143	GLY	0	0.006	0.008	21.376	0.011	0.011	0.000	0.000	0.000	0.000
29	A	144	ASP	-1	-0.747	-0.820	22.073	-0.114	-0.114	0.000	0.000	0.000	0.000
30	A	145	LYS	1	0.792	0.875	18.416	0.191	0.191	0.000	0.000	0.000	0.000
31	A	146	ILE	0	-0.025	-0.017	17.786	0.013	0.013	0.000	0.000	0.000	0.000
32	A	147	ILE	0	0.023	0.009	18.354	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	148	LYS	1	0.819	0.915	20.273	0.178	0.178	0.000	0.000	0.000	0.000
34	A	149	ILE	0	0.005	0.007	19.153	0.013	0.013	0.000	0.000	0.000	0.000
35	A	150	ASN	0	0.042	0.018	22.073	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	151	GLY	0	0.017	0.003	24.144	0.004	0.004	0.000	0.000	0.000	0.000
37	A	152	TYR	0	-0.047	-0.023	18.645	-0.015	-0.015	0.000	0.000	0.000	0.000
38	A	153	GLU	-1	-0.786	-0.883	18.474	-0.229	-0.229	0.000	0.000	0.000	0.000
39	A	154	VAL	0	-0.050	-0.024	15.256	-0.026	-0.026	0.000	0.000	0.000	0.000
40	A	155	ARG	1	0.858	0.926	14.162	0.369	0.369	0.000	0.000	0.000	0.000
41	A	156	THR	0	-0.056	-0.041	9.669	-0.050	-0.050	0.000	0.000	0.000	0.000
42	A	157	TRP	0	-0.004	-0.024	9.098	0.102	0.102	0.000	0.000	0.000	0.000
43	A	158	GLU	-1	-0.834	-0.887	5.584	-1.492	-1.492	0.000	0.000	0.000	0.000
44	A	159	ASP	-1	-0.793	-0.877	9.340	-0.440	-0.440	0.000	0.000	0.000	0.000
45	A	160	LEU	0	0.006	0.001	12.851	0.063	0.063	0.000	0.000	0.000	0.000
46	A	161	ARG	1	0.818	0.886	9.315	0.244	0.244	0.000	0.000	0.000	0.000
47	A	162	ASP	-1	-0.841	-0.930	11.104	-0.399	-0.399	0.000	0.000	0.000	0.000
48	A	163	ALA	0	-0.004	0.005	13.685	0.046	0.046	0.000	0.000	0.000	0.000
49	A	164	LEU	0	-0.032	-0.020	15.798	0.039	0.039	0.000	0.000	0.000	0.000
50	A	165	ILE	0	-0.017	-0.010	13.085	0.034	0.034	0.000	0.000	0.000	0.000
51	A	166	ARG	1	0.814	0.886	16.787	0.191	0.191	0.000	0.000	0.000	0.000
52	A	167	LEU	0	0.033	0.009	19.024	0.021	0.021	0.000	0.000	0.000	0.000
53	A	168	SER	0	-0.059	-0.048	20.660	0.020	0.020	0.000	0.000	0.000	0.000
54	A	169	LEU	0	-0.069	-0.034	18.293	0.014	0.014	0.000	0.000	0.000	0.000
55	A	170	ASP	-1	-0.822	-0.874	22.383	-0.132	-0.132	0.000	0.000	0.000	0.000
56	A	171	GLY	0	0.017	0.014	24.660	0.006	0.006	0.000	0.000	0.000	0.000
57	A	172	VAL	0	0.018	0.029	25.384	0.008	0.008	0.000	0.000	0.000	0.000
58	A	173	LYS	1	0.817	0.886	26.508	0.068	0.068	0.000	0.000	0.000	0.000
59	A	174	GLU	-1	-0.897	-0.948	27.835	-0.058	-0.058	0.000	0.000	0.000	0.000
60	A	175	THR	0	-0.015	-0.015	24.269	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	176	THR	0	0.014	0.025	26.855	0.004	0.004	0.000	0.000	0.000	0.000
62	A	177	LEU	0	-0.017	-0.009	20.450	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	178	PHE	0	-0.008	-0.006	23.164	0.012	0.012	0.000	0.000	0.000	0.000
64	A	179	LEU	0	-0.003	-0.008	22.308	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	180	GLU	-1	-0.793	-0.872	23.214	-0.171	-0.171	0.000	0.000	0.000	0.000
66	A	181	ARG	1	0.813	0.846	24.212	0.088	0.088	0.000	0.000	0.000	0.000
67	A	182	ASN	0	-0.022	-0.020	26.961	0.002	0.002	0.000	0.000	0.000	0.000
68	A	183	GLY	0	0.028	0.024	27.648	0.005	0.005	0.000	0.000	0.000	0.000
69	A	184	GLU	-1	-0.932	-0.945	28.813	-0.082	-0.082	0.000	0.000	0.000	0.000
70	A	185	VAL	0	-0.018	-0.020	26.804	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	186	LEU	0	-0.027	-0.010	27.582	0.009	0.009	0.000	0.000	0.000	0.000
72	A	187	HIS	0	0.022	0.003	27.237	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	188	LEU	0	0.001	-0.006	26.617	0.009	0.009	0.000	0.000	0.000	0.000
74	A	189	THR	0	0.020	0.014	27.265	-0.010	-0.010	0.000	0.000	0.000	0.000
75	A	190	ILE	0	-0.035	-0.013	22.296	0.005	0.005	0.000	0.000	0.000	0.000
76	A	191	LYS	1	0.842	0.903	25.367	0.047	0.047	0.000	0.000	0.000	0.000
77	A	192	VAL	0	0.018	0.007	22.291	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	193	PRO	0	-0.027	0.002	19.546	0.014	0.014	0.000	0.000	0.000	0.000
79	A	194	ASN	0	0.044	0.027	21.813	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	195	VAL	0	0.077	0.020	17.918	0.012	0.012	0.000	0.000	0.000	0.000
81	A	196	GLN	0	-0.001	0.010	19.905	0.022	0.022	0.000	0.000	0.000	0.000
82	A	197	LYS	1	0.860	0.924	22.253	0.004	0.004	0.000	0.000	0.000	0.000
83	A	198	GLY	0	0.017	0.019	18.471	0.012	0.012	0.000	0.000	0.000	0.000
84	A	199	GLU	-1	-0.821	-0.879	18.852	-0.036	-0.036	0.000	0.000	0.000	0.000
85	A	200	GLU	-1	-0.831	-0.905	14.060	-0.099	-0.099	0.000	0.000	0.000	0.000
86	A	201	LEU	0	0.017	0.006	17.766	0.011	0.011	0.000	0.000	0.000	0.000
87	A	202	GLY	0	0.025	0.014	17.954	0.010	0.010	0.000	0.000	0.000	0.000
88	A	203	ILE	0	-0.006	-0.010	16.065	0.011	0.011	0.000	0.000	0.000	0.000
89	A	204	ALA	0	0.010	0.012	13.803	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	205	PRO	0	0.104	0.064	10.891	0.026	0.026	0.000	0.000	0.000	0.000
91	A	206	LEU	0	0.028	0.015	14.229	0.053	0.053	0.000	0.000	0.000	0.000
92	A	207	VAL	0	-0.025	0.004	12.294	0.000	0.000	0.000	0.000	0.000	0.000
93	A	208	LYS	1	1.001	0.996	15.372	0.098	0.098	0.000	0.000	0.000	0.000
94	A	209	PRO	0	0.019	0.028	17.950	0.027	0.027	0.000	0.000	0.000	0.000
95	A	210	VAL	0	-0.006	-0.014	19.014	0.001	0.001	0.000	0.000	0.000	0.000
96	A	211	VAL	0	0.000	0.001	18.281	0.025	0.025	0.000	0.000	0.000	0.000
97	A	212	GLY	0	-0.021	-0.017	16.292	-0.034	-0.034	0.000	0.000	0.000	0.000
98	A	213	GLY	0	0.020	0.010	17.095	0.011	0.011	0.000	0.000	0.000	0.000
99	A	214	VAL	0	-0.012	-0.016	17.968	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	215	LYS	1	0.899	0.972	19.415	-0.333	-0.333	0.000	0.000	0.000	0.000
101	A	216	LYS	1	1.030	1.010	20.805	-0.220	-0.220	0.000	0.000	0.000	0.000
102	A	217	GLY	0	0.013	0.004	24.235	0.009	0.009	0.000	0.000	0.000	0.000
103	A	218	SER	0	-0.062	-0.014	23.214	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	219	PRO	0	0.055	0.017	25.146	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	220	ALA	0	0.034	0.007	23.911	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	221	ASP	-1	-0.846	-0.914	24.913	0.176	0.176	0.000	0.000	0.000	0.000
107	A	222	GLN	0	-0.035	-0.024	26.546	-0.021	-0.021	0.000	0.000	0.000	0.000
108	A	223	VAL	0	0.018	0.027	28.909	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	224	GLY	0	0.007	0.010	29.601	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	225	ILE	0	-0.015	0.000	24.197	-0.006	-0.006	0.000	0.000	0.000	0.000
111	A	226	LYS	1	0.786	0.876	24.520	-0.142	-0.142	0.000	0.000	0.000	0.000
112	A	227	PRO	0	-0.004	-0.011	20.138	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	228	GLY	0	-0.015	-0.005	21.933	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	229	ASP	-1	-0.751	-0.825	23.276	0.094	0.094	0.000	0.000	0.000	0.000
115	A	230	LEU	0	0.001	0.008	23.006	0.010	0.010	0.000	0.000	0.000	0.000
116	A	231	ILE	0	-0.012	-0.015	22.554	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	232	LEU	0	0.020	0.011	24.994	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	233	GLU	-1	-0.815	-0.889	27.824	0.031	0.031	0.000	0.000	0.000	0.000
119	A	234	VAL	0	0.011	0.002	25.455	0.010	0.010	0.000	0.000	0.000	0.000
120	A	235	ASN	0	0.008	-0.006	28.933	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	236	GLY	0	0.059	0.047	32.265	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	237	LYS	1	0.828	0.915	26.325	-0.043	-0.043	0.000	0.000	0.000	0.000
123	A	238	LYS	1	0.929	0.941	29.266	-0.019	-0.019	0.000	0.000	0.000	0.000
124	A	239	ILE	0	-0.091	-0.025	22.832	0.001	0.001	0.000	0.000	0.000	0.000
125	A	240	ASN	0	0.010	-0.006	23.555	-0.007	-0.007	0.000	0.000	0.000	0.000
126	A	241	THR	0	-0.055	-0.048	18.648	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	242	TRP	0	0.017	-0.001	15.719	0.011	0.011	0.000	0.000	0.000	0.000
128	A	243	TYR	0	-0.001	-0.025	13.336	0.039	0.039	0.000	0.000	0.000	0.000
129	A	244	GLU	-1	-0.702	-0.836	18.078	0.035	0.035	0.000	0.000	0.000	0.000
130	A	245	LEU	0	0.002	0.015	19.559	0.004	0.004	0.000	0.000	0.000	0.000
131	A	246	VAL	0	-0.009	-0.011	16.413	0.009	0.009	0.000	0.000	0.000	0.000
132	A	247	GLU	-1	-0.858	-0.917	19.850	0.060	0.060	0.000	0.000	0.000	0.000
133	A	248	GLU	-1	-0.845	-0.921	22.367	0.065	0.065	0.000	0.000	0.000	0.000
134	A	249	VAL	0	-0.017	-0.006	22.100	0.001	0.001	0.000	0.000	0.000	0.000
135	A	250	ARG	1	0.885	0.958	19.506	-0.170	-0.170	0.000	0.000	0.000	0.000
136	A	251	LYS	1	0.797	0.867	23.889	-0.075	-0.075	0.000	0.000	0.000	0.000
137	A	252	SER	0	-0.020	-0.008	26.596	-0.007	-0.007	0.000	0.000	0.000	0.000
138	A	253	GLN	0	0.015	0.008	28.547	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	254	GLY	0	0.014	0.010	28.942	0.000	0.000	0.000	0.000	0.000	0.000
140	A	255	LYS	1	0.898	0.955	29.847	-0.076	-0.076	0.000	0.000	0.000	0.000
141	A	256	ALA	0	0.008	-0.005	31.014	0.007	0.007	0.000	0.000	0.000	0.000
142	A	257	ILE	0	-0.023	-0.006	26.459	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	258	LYS	1	0.883	0.921	31.142	-0.060	-0.060	0.000	0.000	0.000	0.000
144	A	259	LEU	0	-0.031	-0.021	26.158	0.002	0.002	0.000	0.000	0.000	0.000
145	A	260	LYS	1	0.863	0.936	29.601	-0.045	-0.045	0.000	0.000	0.000	0.000
146	A	261	ILE	0	-0.022	-0.013	26.459	0.003	0.003	0.000	0.000	0.000	0.000
147	A	262	LEU	0	0.002	0.011	28.046	-0.006	-0.006	0.000	0.000	0.000	0.000
148	A	263	ARG	1	0.835	0.863	27.850	-0.090	-0.090	0.000	0.000	0.000	0.000
149	A	264	ASN	0	-0.016	-0.023	29.176	0.001	0.001	0.000	0.000	0.000	0.000
150	A	265	GLY	0	0.045	0.028	30.888	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	266	LYS	1	0.950	0.981	32.791	-0.036	-0.036	0.000	0.000	0.000	0.000
152	A	267	MET	0	0.014	0.011	32.683	0.006	0.006	0.000	0.000	0.000	0.000
153	A	268	ILE	0	-0.017	-0.007	31.631	0.000	0.000	0.000	0.000	0.000	0.000
154	A	269	GLU	-1	-0.850	-0.937	32.068	0.053	0.053	0.000	0.000	0.000	0.000
155	A	270	LYS	1	0.819	0.901	29.643	-0.086	-0.086	0.000	0.000	0.000	0.000
156	A	271	GLU	-1	-0.797	-0.883	32.037	0.069	0.069	0.000	0.000	0.000	0.000
157	A	272	LEU	0	-0.018	0.001	26.179	0.004	0.004	0.000	0.000	0.000	0.000
158	A	273	ILE	0	0.060	0.023	30.195	-0.005	-0.005	0.000	0.000	0.000	0.000
159	A	274	PRO	0	-0.063	-0.026	25.192	0.012	0.012	0.000	0.000	0.000	0.000
160	A	275	ALA	0	0.073	0.049	25.248	-0.008	-0.008	0.000	0.000	0.000	0.000
161	A	276	LYS	1	0.936	0.960	24.437	-0.137	-0.137	0.000	0.000	0.000	0.000
162	A	277	ASP	-1	-0.865	-0.929	20.100	0.346	0.346	0.000	0.000	0.000	0.000
163	A	278	PRO	0	0.062	0.008	21.149	0.013	0.013	0.000	0.000	0.000	0.000
164	A	279	LYS	1	0.939	0.976	16.810	-0.454	-0.454	0.000	0.000	0.000	0.000
165	A	280	THR	0	-0.048	-0.024	16.226	0.030	0.030	0.000	0.000	0.000	0.000
166	A	281	GLY	0	0.031	0.028	18.128	-0.020	-0.020	0.000	0.000	0.000	0.000
167	A	282	THR	0	-0.053	-0.034	19.425	-0.034	-0.034	0.000	0.000	0.000	0.000
168	A	283	TYR	0	-0.046	-0.011	22.236	0.012	0.012	0.000	0.000	0.000	0.000
169	A	284	PHE	0	0.017	0.007	17.183	0.011	0.011	0.000	0.000	0.000	0.000
170	A	285	ILE	0	0.056	0.021	21.522	-0.010	-0.010	0.000	0.000	0.000	0.000
171	A	286	GLY	0	0.027	-0.012	20.977	-0.013	-0.013	0.000	0.000	0.000	0.000
172	A	287	LEU	0	-0.037	0.008	19.328	0.017	0.017	0.000	0.000	0.000	0.000
173	A	288	PHE	0	0.031	0.007	14.022	0.035	0.035	0.000	0.000	0.000	0.000
174	A	289	PRO	0	0.062	0.038	12.313	-0.040	-0.040	0.000	0.000	0.000	0.000
175	A	290	LYS	1	0.889	0.930	13.902	-0.059	-0.059	0.000	0.000	0.000	0.000
176	A	291	THR	0	-0.017	0.010	8.810	-0.043	-0.043	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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