FMO DATABASE

FMODB ID: VYV91

Calculation Name: 2G3Y-A-Xray547

Preferred Name:

Target Type:

Ligand Name: guanosine-5'-diphosphate

Ligand 3-letter code: GDP

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2G3Y

Chain ID: A

ChEMBL ID:

UniProt ID: P55040

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1824120.561147
FMO2-HF: Nuclear repulsion	1754477.851501
FMO2-HF: Total energy	-69642.709645
FMO2-MP2: Total energy	-69841.887845

3D Structure Molmil

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:73:ASN)

Summations of interaction energy for fragment #1(A:73:ASN)

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.
-163.808	-159.045	2.89	-3.183	-4.471	-0.026

Interaction energy analysis for fragmet #1(A:73:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / q_NPA : 0.916

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	75	TYR	0	0.054	0.029	2.291	-4.774	-0.040	2.891	-3.173	-4.452	-0.026
4	A	76	TYR	0	-0.008	-0.008	4.672	0.268	0.297	-0.001	-0.010	-0.019	0.000
5	A	77	ARG	1	0.867	0.911	6.537	40.461	40.461	0.000	0.000	0.000	0.000
6	A	78	VAL	0	-0.006	-0.007	9.629	1.151	1.151	0.000	0.000	0.000	0.000
7	A	79	VAL	0	0.025	0.021	13.452	0.519	0.519	0.000	0.000	0.000	0.000
8	A	80	LEU	0	-0.036	-0.010	16.042	0.739	0.739	0.000	0.000	0.000	0.000
9	A	81	ILE	0	0.017	0.002	19.515	0.338	0.338	0.000	0.000	0.000	0.000
10	A	82	GLY	0	0.023	0.004	22.470	0.147	0.147	0.000	0.000	0.000	0.000
11	A	83	GLU	-1	-0.841	-0.903	26.255	-10.146	-10.146	0.000	0.000	0.000	0.000
12	A	84	GLN	0	-0.002	-0.007	28.609	-0.186	-0.186	0.000	0.000	0.000	0.000
13	A	85	GLY	0	0.015	0.019	29.726	0.255	0.255	0.000	0.000	0.000	0.000
14	A	86	VAL	0	-0.044	-0.021	26.942	0.195	0.195	0.000	0.000	0.000	0.000
15	A	87	GLY	0	0.002	-0.001	27.638	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	88	LYS	1	0.774	0.882	22.505	12.211	12.211	0.000	0.000	0.000	0.000
17	A	89	SER	0	0.113	0.031	22.378	-0.207	-0.207	0.000	0.000	0.000	0.000
18	A	90	THR	0	-0.068	-0.026	23.195	-0.139	-0.139	0.000	0.000	0.000	0.000
19	A	91	LEU	0	-0.014	-0.015	20.966	-0.073	-0.073	0.000	0.000	0.000	0.000
20	A	92	ALA	0	0.024	0.011	18.842	-0.367	-0.367	0.000	0.000	0.000	0.000
21	A	93	ASN	0	0.045	0.020	19.481	-0.460	-0.460	0.000	0.000	0.000	0.000
22	A	94	ILE	0	-0.051	-0.015	21.801	0.024	0.024	0.000	0.000	0.000	0.000
23	A	95	PHE	0	-0.032	-0.011	14.227	0.098	0.098	0.000	0.000	0.000	0.000
24	A	96	ALA	0	-0.004	0.000	17.164	-0.449	-0.449	0.000	0.000	0.000	0.000
25	A	97	GLY	0	-0.018	0.003	18.176	-0.073	-0.073	0.000	0.000	0.000	0.000
26	A	98	VAL	0	-0.060	-0.040	21.149	0.029	0.029	0.000	0.000	0.000	0.000
27	A	99	HIS	1	0.766	0.844	13.990	19.093	19.093	0.000	0.000	0.000	0.000
28	A	100	ASP	-1	-0.867	-0.931	19.089	-13.158	-13.158	0.000	0.000	0.000	0.000
29	A	101	SER	0	-0.020	-0.019	18.561	-0.489	-0.489	0.000	0.000	0.000	0.000
30	A	102	MET	0	-0.084	-0.048	19.626	0.133	0.133	0.000	0.000	0.000	0.000
31	A	103	ASP	-1	-0.753	-0.855	13.342	-20.508	-20.508	0.000	0.000	0.000	0.000
32	A	104	SER	0	-0.097	-0.073	13.832	1.040	1.040	0.000	0.000	0.000	0.000
33	A	105	ASP	-1	-1.060	-1.016	8.723	-24.749	-24.749	0.000	0.000	0.000	0.000
34	A	106	CYS	-1	-0.795	-0.828	8.562	-26.830	-26.830	0.000	0.000	0.000	0.000
35	A	107	GLU	-1	-0.822	-0.936	10.911	-17.406	-17.406	0.000	0.000	0.000	0.000
36	A	108	VAL	0	-0.025	0.008	9.981	1.488	1.488	0.000	0.000	0.000	0.000
37	A	109	LEU	0	-0.073	-0.036	10.591	-0.470	-0.470	0.000	0.000	0.000	0.000
38	A	110	GLY	0	-0.004	-0.013	14.377	1.271	1.271	0.000	0.000	0.000	0.000
39	A	111	GLU	-1	-0.915	-0.951	17.124	-14.404	-14.404	0.000	0.000	0.000	0.000
40	A	112	ASP	-1	-0.844	-0.925	18.120	-14.832	-14.832	0.000	0.000	0.000	0.000
41	A	113	THR	0	-0.068	-0.027	12.616	-0.978	-0.978	0.000	0.000	0.000	0.000
42	A	114	TYR	0	-0.033	-0.034	14.682	0.809	0.809	0.000	0.000	0.000	0.000
43	A	115	GLU	-1	-0.934	-0.988	8.036	-33.629	-33.629	0.000	0.000	0.000	0.000
44	A	116	ARG	1	0.901	0.934	11.303	20.376	20.376	0.000	0.000	0.000	0.000
45	A	117	THR	0	0.007	0.020	10.608	-1.657	-1.657	0.000	0.000	0.000	0.000
46	A	118	LEU	0	0.004	-0.008	11.539	2.524	2.524	0.000	0.000	0.000	0.000
47	A	119	MET	0	-0.017	0.012	12.723	-1.798	-1.798	0.000	0.000	0.000	0.000
48	A	120	VAL	0	0.018	0.007	14.031	1.222	1.222	0.000	0.000	0.000	0.000
49	A	121	ASP	-1	-0.817	-0.882	15.505	-18.009	-18.009	0.000	0.000	0.000	0.000
50	A	122	GLY	0	-0.008	0.004	17.605	0.249	0.249	0.000	0.000	0.000	0.000
51	A	123	GLU	-1	-0.874	-0.928	10.437	-28.776	-28.776	0.000	0.000	0.000	0.000
52	A	124	SER	0	-0.004	-0.012	10.352	0.362	0.362	0.000	0.000	0.000	0.000
53	A	125	ALA	0	-0.008	0.001	8.571	-2.669	-2.669	0.000	0.000	0.000	0.000
54	A	126	THR	0	0.015	0.007	5.601	1.943	1.943	0.000	0.000	0.000	0.000
55	A	127	ILE	0	-0.046	-0.035	7.229	-3.601	-3.601	0.000	0.000	0.000	0.000
56	A	128	ILE	0	0.029	0.020	7.141	0.222	0.222	0.000	0.000	0.000	0.000
57	A	129	LEU	0	-0.063	-0.024	10.405	0.653	0.653	0.000	0.000	0.000	0.000
58	A	130	LEU	0	0.031	0.014	11.436	-0.144	-0.144	0.000	0.000	0.000	0.000
59	A	131	ASP	-1	-0.826	-0.912	15.292	-13.840	-13.840	0.000	0.000	0.000	0.000
60	A	132	MET	0	0.038	0.045	15.014	0.686	0.686	0.000	0.000	0.000	0.000
61	A	133	TRP	0	-0.043	-0.018	20.049	0.154	0.154	0.000	0.000	0.000	0.000
62	A	134	GLU	-1	-0.785	-0.899	22.623	-11.161	-11.161	0.000	0.000	0.000	0.000
63	A	135	ASN	0	-0.089	-0.037	22.579	0.891	0.891	0.000	0.000	0.000	0.000
64	A	136	LYS	1	0.853	0.918	21.057	13.914	13.914	0.000	0.000	0.000	0.000
65	A	137	GLY	0	0.050	0.032	21.965	0.065	0.065	0.000	0.000	0.000	0.000
66	A	138	GLU	-1	-0.902	-0.961	22.640	-11.069	-11.069	0.000	0.000	0.000	0.000
67	A	139	ASN	0	-0.009	-0.018	25.887	0.467	0.467	0.000	0.000	0.000	0.000
68	A	140	GLU	-1	-0.830	-0.908	21.362	-14.344	-14.344	0.000	0.000	0.000	0.000
69	A	141	TRP	0	-0.039	-0.019	22.261	-0.233	-0.233	0.000	0.000	0.000	0.000
70	A	142	LEU	0	-0.029	-0.033	25.265	0.342	0.342	0.000	0.000	0.000	0.000
71	A	143	HIS	0	-0.112	-0.058	28.320	0.767	0.767	0.000	0.000	0.000	0.000
72	A	144	ASP	-1	-0.840	-0.928	24.634	-11.735	-11.735	0.000	0.000	0.000	0.000
73	A	145	HIS	1	0.779	0.909	25.121	10.952	10.952	0.000	0.000	0.000	0.000
74	A	146	CYS	0	-0.023	-0.002	20.116	-0.386	-0.386	0.000	0.000	0.000	0.000
75	A	147	MET	0	-0.019	0.003	18.048	0.139	0.139	0.000	0.000	0.000	0.000
76	A	148	GLN	0	0.022	-0.009	14.686	-0.730	-0.730	0.000	0.000	0.000	0.000
77	A	149	VAL	0	0.014	0.010	10.605	-0.042	-0.042	0.000	0.000	0.000	0.000
78	A	150	GLY	0	0.031	0.014	10.910	-1.153	-1.153	0.000	0.000	0.000	0.000
79	A	151	ASP	-1	-0.832	-0.885	7.642	-40.841	-40.841	0.000	0.000	0.000	0.000
80	A	152	ALA	0	0.014	0.000	10.612	1.313	1.313	0.000	0.000	0.000	0.000
81	A	153	TYR	0	-0.023	-0.031	14.259	-0.267	-0.267	0.000	0.000	0.000	0.000
82	A	154	LEU	0	-0.029	-0.015	17.547	0.698	0.698	0.000	0.000	0.000	0.000
83	A	155	ILE	0	0.009	0.015	20.194	0.209	0.209	0.000	0.000	0.000	0.000
84	A	156	VAL	0	-0.026	-0.016	22.936	0.380	0.380	0.000	0.000	0.000	0.000
85	A	157	TYR	0	0.013	0.010	25.589	0.213	0.213	0.000	0.000	0.000	0.000
86	A	158	SER	0	0.008	-0.015	29.384	-0.249	-0.249	0.000	0.000	0.000	0.000
87	A	159	ILE	0	-0.012	-0.006	32.036	0.243	0.243	0.000	0.000	0.000	0.000
88	A	160	THR	0	-0.046	-0.024	34.454	0.191	0.191	0.000	0.000	0.000	0.000
89	A	161	ASP	-1	-0.828	-0.896	34.571	-8.932	-8.932	0.000	0.000	0.000	0.000
90	A	162	ARG	1	0.874	0.928	35.012	7.930	7.930	0.000	0.000	0.000	0.000
91	A	163	ALA	0	0.031	0.029	36.216	-0.100	-0.100	0.000	0.000	0.000	0.000
92	A	164	SER	0	-0.009	-0.025	31.391	-0.365	-0.365	0.000	0.000	0.000	0.000
93	A	165	PHE	0	-0.020	-0.021	31.220	-0.368	-0.368	0.000	0.000	0.000	0.000
94	A	166	GLU	-1	-0.906	-0.954	32.108	-8.713	-8.713	0.000	0.000	0.000	0.000
95	A	167	LYS	1	0.889	0.938	29.967	10.070	10.070	0.000	0.000	0.000	0.000
96	A	168	ALA	0	0.025	0.002	27.943	-0.357	-0.357	0.000	0.000	0.000	0.000
97	A	169	SER	0	-0.029	-0.023	27.913	-0.376	-0.376	0.000	0.000	0.000	0.000
98	A	170	GLU	-1	-0.875	-0.923	29.675	-10.203	-10.203	0.000	0.000	0.000	0.000
99	A	171	LEU	0	0.022	0.010	25.428	-0.186	-0.186	0.000	0.000	0.000	0.000
100	A	172	ARG	1	0.879	0.936	22.113	13.087	13.087	0.000	0.000	0.000	0.000
101	A	173	ILE	0	-0.033	-0.017	25.691	-0.257	-0.257	0.000	0.000	0.000	0.000
102	A	174	GLN	0	-0.078	-0.041	26.994	-0.294	-0.294	0.000	0.000	0.000	0.000
103	A	175	LEU	0	0.041	0.028	19.562	-0.035	-0.035	0.000	0.000	0.000	0.000
104	A	176	ARG	1	0.865	0.934	22.539	12.145	12.145	0.000	0.000	0.000	0.000
105	A	177	ARG	1	0.914	0.947	24.422	10.845	10.845	0.000	0.000	0.000	0.000
106	A	178	ALA	0	0.029	0.031	20.476	0.126	0.126	0.000	0.000	0.000	0.000
107	A	179	ARG	1	0.932	0.961	20.329	11.531	11.531	0.000	0.000	0.000	0.000
108	A	180	GLN	0	0.010	0.008	15.924	-0.786	-0.786	0.000	0.000	0.000	0.000
109	A	181	THR	0	-0.011	-0.028	15.908	-0.884	-0.884	0.000	0.000	0.000	0.000
110	A	182	GLU	-1	-1.026	-0.995	17.670	-13.906	-13.906	0.000	0.000	0.000	0.000
111	A	183	ASP	-1	-0.817	-0.907	16.706	-17.303	-17.303	0.000	0.000	0.000	0.000
112	A	184	ILE	0	-0.016	0.010	13.092	-0.956	-0.956	0.000	0.000	0.000	0.000
113	A	185	PRO	0	-0.042	-0.023	14.102	1.358	1.358	0.000	0.000	0.000	0.000
114	A	186	ILE	0	0.025	0.021	17.018	-0.315	-0.315	0.000	0.000	0.000	0.000
115	A	187	ILE	0	-0.042	-0.028	18.997	0.660	0.660	0.000	0.000	0.000	0.000
116	A	188	LEU	0	0.002	0.012	21.911	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	189	VAL	0	0.009	-0.017	22.647	0.179	0.179	0.000	0.000	0.000	0.000
118	A	190	GLY	0	0.052	0.021	25.916	0.230	0.230	0.000	0.000	0.000	0.000
119	A	191	ASN	0	0.007	-0.002	27.342	0.095	0.095	0.000	0.000	0.000	0.000
120	A	192	LYS	1	0.881	0.933	29.195	10.269	10.269	0.000	0.000	0.000	0.000
121	A	193	SER	0	-0.010	-0.026	31.181	0.386	0.386	0.000	0.000	0.000	0.000
122	A	194	ASP	-1	-0.814	-0.878	33.121	-9.385	-9.385	0.000	0.000	0.000	0.000
123	A	195	LEU	0	-0.010	0.005	35.191	0.353	0.353	0.000	0.000	0.000	0.000
124	A	196	VAL	0	0.019	-0.003	37.872	0.131	0.131	0.000	0.000	0.000	0.000
125	A	197	ARG	1	0.912	0.939	39.807	7.361	7.361	0.000	0.000	0.000	0.000
126	A	198	CYS	0	-0.096	-0.049	39.685	0.285	0.285	0.000	0.000	0.000	0.000
127	A	199	ARG	1	0.778	0.854	34.801	8.956	8.956	0.000	0.000	0.000	0.000
128	A	200	GLU	-1	-0.855	-0.914	38.685	-7.874	-7.874	0.000	0.000	0.000	0.000
129	A	201	VAL	0	-0.004	0.010	34.762	0.073	0.073	0.000	0.000	0.000	0.000
130	A	202	SER	0	-0.032	-0.024	37.134	-0.134	-0.134	0.000	0.000	0.000	0.000
131	A	203	VAL	0	0.048	0.003	33.638	-0.160	-0.160	0.000	0.000	0.000	0.000
132	A	204	SER	0	-0.094	-0.043	34.616	-0.171	-0.171	0.000	0.000	0.000	0.000
133	A	205	GLU	-1	-0.732	-0.830	35.954	-8.436	-8.436	0.000	0.000	0.000	0.000
134	A	206	GLY	0	0.081	0.046	32.690	-0.140	-0.140	0.000	0.000	0.000	0.000
135	A	207	ARG	1	0.946	0.975	31.094	9.784	9.784	0.000	0.000	0.000	0.000
136	A	208	ALA	0	0.004	-0.001	31.688	-0.189	-0.189	0.000	0.000	0.000	0.000
137	A	209	CYS	0	-0.002	-0.001	31.630	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	210	ALA	0	-0.007	-0.002	27.510	-0.216	-0.216	0.000	0.000	0.000	0.000
139	A	211	VAL	0	-0.032	-0.009	28.241	-0.277	-0.277	0.000	0.000	0.000	0.000
140	A	212	VAL	0	-0.043	-0.018	30.702	-0.025	-0.025	0.000	0.000	0.000	0.000
141	A	213	PHE	0	-0.020	-0.022	28.544	0.060	0.060	0.000	0.000	0.000	0.000
142	A	214	ASP	-1	-0.874	-0.909	24.545	-13.393	-13.393	0.000	0.000	0.000	0.000
143	A	215	CYS	0	-0.014	0.013	23.518	-0.612	-0.612	0.000	0.000	0.000	0.000
144	A	216	LYS	1	0.918	0.957	21.679	14.699	14.699	0.000	0.000	0.000	0.000
145	A	217	PHE	0	-0.008	-0.013	24.167	0.090	0.090	0.000	0.000	0.000	0.000
146	A	218	ILE	0	-0.033	-0.008	23.758	0.059	0.059	0.000	0.000	0.000	0.000
147	A	219	GLU	-1	-0.754	-0.844	27.082	-9.669	-9.669	0.000	0.000	0.000	0.000
148	A	220	THR	0	0.050	0.012	24.548	-0.195	-0.195	0.000	0.000	0.000	0.000
149	A	221	SER	0	-0.088	-0.053	27.967	0.399	0.399	0.000	0.000	0.000	0.000
150	A	222	ALA	0	0.042	0.015	26.513	-0.172	-0.172	0.000	0.000	0.000	0.000
151	A	223	ALA	0	-0.019	0.000	27.569	-0.045	-0.045	0.000	0.000	0.000	0.000
152	A	224	VAL	0	-0.016	-0.022	30.927	0.166	0.166	0.000	0.000	0.000	0.000
153	A	225	GLN	0	-0.013	-0.001	25.562	0.220	0.220	0.000	0.000	0.000	0.000
154	A	226	HIS	0	0.029	0.027	27.000	-0.305	-0.305	0.000	0.000	0.000	0.000
155	A	227	ASN	0	-0.029	-0.038	25.891	-0.157	-0.157	0.000	0.000	0.000	0.000
156	A	228	VAL	0	0.025	0.016	21.389	-0.508	-0.508	0.000	0.000	0.000	0.000
157	A	229	LYS	1	0.838	0.920	19.096	14.278	14.278	0.000	0.000	0.000	0.000
158	A	230	GLU	-1	-0.843	-0.932	19.688	-13.743	-13.743	0.000	0.000	0.000	0.000
159	A	231	LEU	0	-0.029	-0.006	19.515	-0.383	-0.383	0.000	0.000	0.000	0.000
160	A	232	PHE	0	0.049	0.012	15.359	-0.584	-0.584	0.000	0.000	0.000	0.000
161	A	233	GLU	-1	-0.817	-0.905	15.646	-16.659	-16.659	0.000	0.000	0.000	0.000
162	A	234	GLY	0	-0.028	-0.011	17.197	-0.473	-0.473	0.000	0.000	0.000	0.000
163	A	235	ILE	0	-0.024	-0.010	13.890	-0.193	-0.193	0.000	0.000	0.000	0.000
164	A	236	VAL	0	0.025	0.016	11.620	-0.819	-0.819	0.000	0.000	0.000	0.000
165	A	237	ARG	1	0.837	0.887	13.642	15.467	15.467	0.000	0.000	0.000	0.000
166	A	238	GLN	0	-0.021	-0.010	16.123	0.456	0.456	0.000	0.000	0.000	0.000
167	A	239	VAL	0	0.018	0.005	9.934	0.035	0.035	0.000	0.000	0.000	0.000
168	A	240	ARG	1	0.769	0.863	11.596	23.170	23.170	0.000	0.000	0.000	0.000
169	A	241	LEU	0	-0.053	-0.026	12.716	-0.036	-0.036	0.000	0.000	0.000	0.000
170	A	242	ARG	1	0.829	0.918	12.695	19.241	19.241	0.000	0.000	0.000	0.000
171	A	243	ARG	1	0.752	0.893	6.484	39.515	39.515	0.000	0.000	0.000	0.000
172	A	244	ASP	-2	-1.867	-1.919	11.066	-40.623	-40.623	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:73:ASN)