FMO DATABASE

FMODB ID: ML48Z

Calculation Name: 3REF-A-Xray547

Preferred Name:

Target Type:

Ligand Name: guanosine-5'-diphosphate | sulfate ion | magnesium ion

Ligand 3-letter code: GDP | SO4 | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3REF

Chain ID: A

ChEMBL ID:

UniProt ID: C4M4W4

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	173
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1806439.800425
FMO2-HF: Nuclear repulsion	1738838.203896
FMO2-HF: Total energy	-67601.596529
FMO2-MP2: Total energy	-67798.454862

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:12:GLY)

Summations of interaction energy for fragment #1(A:12:GLY)

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.
-257.466	-252.555	11.279	-8.481	-7.712	-0.089

Interaction energy analysis for fragmet #1(A:12:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.855 / q_NPA : 0.931

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	14	ILE	0	0.036	0.004	3.831	3.976	4.966	-0.017	-0.438	-0.535	0.000
9	A	20	ALA	0	-0.031	-0.011	4.797	4.506	4.570	-0.001	-0.009	-0.054	0.000
10	A	21	LEU	0	0.016	0.003	3.536	-17.237	-16.706	0.020	-0.327	-0.225	-0.002
11	A	22	LYS	1	0.790	0.907	4.699	37.015	37.045	-0.001	-0.001	-0.029	0.000
82	A	93	ASP	-1	-0.827	-0.910	2.199	-117.928	-117.029	8.785	-5.453	-4.232	-0.064
83	A	94	VAL	0	-0.013	-0.014	5.119	3.530	3.577	-0.001	-0.002	-0.044	0.000
172	A	183	ILE	0	-0.069	-0.045	2.634	-6.608	-5.691	0.696	-0.654	-0.959	-0.006
173	A	184	PHE	-1	-0.880	-0.920	2.607	-42.930	-41.497	1.798	-1.597	-1.634	-0.017
4	A	15	GLU	-1	-0.808	-0.878	7.176	-33.462	-33.462	0.000	0.000	0.000	0.000
5	A	16	ASN	0	-0.022	-0.018	10.143	3.050	3.050	0.000	0.000	0.000	0.000
6	A	17	GLY	0	0.014	0.017	12.555	0.355	0.355	0.000	0.000	0.000	0.000
7	A	18	LYS	1	0.832	0.913	10.352	20.589	20.589	0.000	0.000	0.000	0.000
8	A	19	LYS	1	0.884	0.934	5.368	30.097	30.097	0.000	0.000	0.000	0.000
12	A	23	ILE	0	-0.008	-0.007	6.836	-1.806	-1.806	0.000	0.000	0.000	0.000
13	A	24	VAL	0	0.010	0.009	9.709	2.225	2.225	0.000	0.000	0.000	0.000
14	A	25	VAL	0	-0.008	0.004	12.768	0.089	0.089	0.000	0.000	0.000	0.000
15	A	26	VAL	0	0.013	0.023	16.211	0.931	0.931	0.000	0.000	0.000	0.000
16	A	27	GLY	0	0.103	0.040	18.713	0.075	0.075	0.000	0.000	0.000	0.000
17	A	28	ASP	-1	-0.803	-0.873	22.199	-11.814	-11.814	0.000	0.000	0.000	0.000
18	A	29	GLY	0	0.007	-0.007	25.393	-0.293	-0.293	0.000	0.000	0.000	0.000
19	A	30	ALA	0	0.004	-0.007	27.767	0.125	0.125	0.000	0.000	0.000	0.000
20	A	31	VAL	0	-0.001	0.009	23.780	0.249	0.249	0.000	0.000	0.000	0.000
21	A	32	GLY	0	0.028	0.007	25.371	0.055	0.055	0.000	0.000	0.000	0.000
22	A	33	LYS	1	0.838	0.940	19.999	14.079	14.079	0.000	0.000	0.000	0.000
23	A	34	THR	0	0.055	0.011	20.798	-0.351	-0.351	0.000	0.000	0.000	0.000
24	A	35	CYS	0	-0.009	-0.018	22.604	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	36	LEU	0	0.003	0.037	18.053	0.188	0.188	0.000	0.000	0.000	0.000
26	A	37	LEU	0	0.028	0.015	15.782	-0.263	-0.263	0.000	0.000	0.000	0.000
27	A	38	LEU	0	-0.027	0.006	19.454	-0.061	-0.061	0.000	0.000	0.000	0.000
28	A	39	ALA	0	-0.002	-0.001	22.672	0.058	0.058	0.000	0.000	0.000	0.000
29	A	40	PHE	0	-0.024	-0.014	14.593	0.069	0.069	0.000	0.000	0.000	0.000
30	A	41	SER	0	-0.046	-0.041	18.389	0.137	0.137	0.000	0.000	0.000	0.000
31	A	42	LYS	1	0.907	0.943	19.855	13.600	13.600	0.000	0.000	0.000	0.000
32	A	43	GLY	0	0.016	0.031	23.107	0.511	0.511	0.000	0.000	0.000	0.000
33	A	44	GLU	-1	-0.971	-0.995	24.863	-9.981	-9.981	0.000	0.000	0.000	0.000
34	A	45	ILE	0	-0.010	-0.014	26.262	-0.477	-0.477	0.000	0.000	0.000	0.000
35	A	46	PRO	0	-0.001	0.009	27.418	0.363	0.363	0.000	0.000	0.000	0.000
36	A	47	THR	0	-0.003	-0.009	30.441	0.117	0.117	0.000	0.000	0.000	0.000
37	A	48	ALA	0	-0.021	-0.018	31.449	0.238	0.238	0.000	0.000	0.000	0.000
38	A	49	TYR	0	-0.011	0.000	30.445	-0.061	-0.061	0.000	0.000	0.000	0.000
39	A	50	VAL	0	-0.001	0.005	27.006	-0.267	-0.267	0.000	0.000	0.000	0.000
40	A	51	PRO	0	-0.012	-0.007	25.179	0.262	0.262	0.000	0.000	0.000	0.000
41	A	52	THR	0	-0.055	-0.047	26.378	-0.198	-0.198	0.000	0.000	0.000	0.000
42	A	53	VAL	0	-0.013	-0.006	20.746	-0.317	-0.317	0.000	0.000	0.000	0.000
43	A	54	PHE	0	-0.065	-0.031	19.592	0.579	0.579	0.000	0.000	0.000	0.000
44	A	55	GLU	-1	-0.910	-0.954	19.740	-14.311	-14.311	0.000	0.000	0.000	0.000
45	A	56	ASN	0	-0.036	-0.014	14.497	0.031	0.031	0.000	0.000	0.000	0.000
46	A	57	PHE	0	-0.031	-0.018	15.264	0.348	0.348	0.000	0.000	0.000	0.000
47	A	58	SER	0	0.008	0.009	12.791	-1.005	-1.005	0.000	0.000	0.000	0.000
48	A	59	HIS	0	0.011	0.011	13.152	1.695	1.695	0.000	0.000	0.000	0.000
49	A	60	VAL	0	-0.037	-0.018	12.729	-2.006	-2.006	0.000	0.000	0.000	0.000
50	A	61	MET	0	0.008	0.018	12.077	0.902	0.902	0.000	0.000	0.000	0.000
51	A	62	LYS	1	0.930	0.963	12.867	14.133	14.133	0.000	0.000	0.000	0.000
52	A	63	TYR	0	-0.010	-0.039	11.441	0.877	0.877	0.000	0.000	0.000	0.000
53	A	64	LYS	1	0.804	0.903	9.559	28.281	28.281	0.000	0.000	0.000	0.000
54	A	65	ASN	0	-0.007	0.002	14.555	1.663	1.663	0.000	0.000	0.000	0.000
55	A	66	GLU	-1	-0.854	-0.905	10.326	-26.366	-26.366	0.000	0.000	0.000	0.000
56	A	67	GLU	-1	-0.885	-0.939	12.464	-18.132	-18.132	0.000	0.000	0.000	0.000
57	A	68	PHE	0	-0.006	-0.004	6.617	-1.528	-1.528	0.000	0.000	0.000	0.000
58	A	69	ILE	0	-0.028	-0.017	8.485	2.971	2.971	0.000	0.000	0.000	0.000
59	A	70	LEU	0	0.012	-0.003	8.091	-4.388	-4.388	0.000	0.000	0.000	0.000
60	A	71	HIS	0	-0.033	-0.043	7.933	4.807	4.807	0.000	0.000	0.000	0.000
61	A	72	LEU	0	-0.014	-0.002	10.167	-1.627	-1.627	0.000	0.000	0.000	0.000
62	A	73	TRP	0	0.051	0.007	11.232	1.543	1.543	0.000	0.000	0.000	0.000
63	A	74	ASP	-1	-0.731	-0.855	14.635	-15.211	-15.211	0.000	0.000	0.000	0.000
64	A	75	THR	0	-0.042	-0.039	17.231	0.097	0.097	0.000	0.000	0.000	0.000
65	A	76	ALA	0	0.016	-0.001	20.002	0.535	0.535	0.000	0.000	0.000	0.000
66	A	77	GLY	0	0.018	0.001	23.441	-0.386	-0.386	0.000	0.000	0.000	0.000
67	A	78	GLN	0	-0.044	-0.016	26.097	0.425	0.425	0.000	0.000	0.000	0.000
68	A	79	GLU	-1	-0.837	-0.919	27.704	-10.893	-10.893	0.000	0.000	0.000	0.000
69	A	80	GLU	-1	-0.868	-0.936	26.682	-11.107	-11.107	0.000	0.000	0.000	0.000
70	A	81	TYR	0	0.043	0.007	23.228	-0.660	-0.660	0.000	0.000	0.000	0.000
71	A	82	ASP	-1	-0.864	-0.918	23.353	-12.654	-12.654	0.000	0.000	0.000	0.000
72	A	83	ARG	1	0.853	0.925	24.542	10.977	10.977	0.000	0.000	0.000	0.000
73	A	84	LEU	0	0.018	0.011	21.495	-0.344	-0.344	0.000	0.000	0.000	0.000
74	A	85	ARG	1	0.712	0.831	19.175	13.424	13.424	0.000	0.000	0.000	0.000
75	A	86	PRO	0	0.008	-0.007	17.899	-1.066	-1.066	0.000	0.000	0.000	0.000
76	A	87	LEU	0	-0.007	-0.002	16.745	-1.045	-1.045	0.000	0.000	0.000	0.000
77	A	88	SER	0	-0.027	-0.010	14.952	-0.958	-0.958	0.000	0.000	0.000	0.000
78	A	89	TYR	0	-0.022	-0.038	12.687	-1.862	-1.862	0.000	0.000	0.000	0.000
79	A	90	ALA	0	0.024	0.041	11.244	-2.080	-2.080	0.000	0.000	0.000	0.000
80	A	91	ASP	-1	-0.908	-0.957	7.064	-33.064	-33.064	0.000	0.000	0.000	0.000
81	A	92	SER	0	-0.024	-0.030	6.356	-4.342	-4.342	0.000	0.000	0.000	0.000
84	A	95	VAL	0	0.006	-0.003	8.368	1.167	1.167	0.000	0.000	0.000	0.000
85	A	96	LEU	0	-0.015	-0.002	12.106	0.940	0.940	0.000	0.000	0.000	0.000
86	A	97	LEU	0	0.019	0.006	15.062	0.848	0.848	0.000	0.000	0.000	0.000
87	A	98	CYS	0	-0.048	-0.020	18.032	0.439	0.439	0.000	0.000	0.000	0.000
88	A	99	PHE	0	0.032	0.007	20.780	0.402	0.402	0.000	0.000	0.000	0.000
89	A	100	ALA	0	-0.026	-0.011	24.502	-0.156	-0.156	0.000	0.000	0.000	0.000
90	A	101	VAL	0	0.033	0.016	27.115	0.275	0.275	0.000	0.000	0.000	0.000
91	A	102	ASN	0	-0.017	0.001	29.254	-0.044	-0.044	0.000	0.000	0.000	0.000
92	A	103	ASN	0	-0.021	-0.016	30.238	0.114	0.114	0.000	0.000	0.000	0.000
93	A	104	ARG	1	0.886	0.944	30.185	9.182	9.182	0.000	0.000	0.000	0.000
94	A	105	THR	0	0.027	0.016	30.441	-0.187	-0.187	0.000	0.000	0.000	0.000
95	A	106	SER	0	-0.008	-0.013	26.775	-0.393	-0.393	0.000	0.000	0.000	0.000
96	A	107	PHE	0	-0.021	-0.010	25.850	-0.593	-0.593	0.000	0.000	0.000	0.000
97	A	108	ASP	-1	-0.847	-0.929	26.239	-10.553	-10.553	0.000	0.000	0.000	0.000
98	A	109	ASN	0	-0.045	-0.045	26.330	-0.081	-0.081	0.000	0.000	0.000	0.000
99	A	110	ILE	0	-0.054	-0.020	20.856	-0.523	-0.523	0.000	0.000	0.000	0.000
100	A	111	SER	0	0.011	0.006	22.574	-0.564	-0.564	0.000	0.000	0.000	0.000
101	A	112	THR	0	-0.069	-0.038	24.800	0.031	0.031	0.000	0.000	0.000	0.000
102	A	113	LYS	1	0.896	0.961	23.615	12.772	12.772	0.000	0.000	0.000	0.000
103	A	114	TRP	0	-0.025	-0.039	20.061	-0.510	-0.510	0.000	0.000	0.000	0.000
104	A	115	GLU	-1	-0.817	-0.896	18.036	-16.562	-16.562	0.000	0.000	0.000	0.000
105	A	116	PRO	0	0.035	0.010	18.734	-0.715	-0.715	0.000	0.000	0.000	0.000
106	A	117	GLU	-1	-0.798	-0.846	19.696	-15.269	-15.269	0.000	0.000	0.000	0.000
107	A	118	ILE	0	-0.011	-0.013	13.643	-0.573	-0.573	0.000	0.000	0.000	0.000
108	A	119	LYS	1	0.867	0.936	15.332	15.048	15.048	0.000	0.000	0.000	0.000
109	A	120	HIS	0	-0.072	-0.023	17.073	0.393	0.393	0.000	0.000	0.000	0.000
110	A	121	TYR	0	-0.048	-0.032	15.985	0.198	0.198	0.000	0.000	0.000	0.000
111	A	122	ILE	0	-0.052	-0.030	9.227	-0.907	-0.907	0.000	0.000	0.000	0.000
112	A	123	ASP	-1	-0.867	-0.932	11.510	-21.987	-21.987	0.000	0.000	0.000	0.000
113	A	124	THR	0	-0.038	-0.012	8.037	0.671	0.671	0.000	0.000	0.000	0.000
114	A	125	ALA	0	-0.056	-0.008	7.462	-4.496	-4.496	0.000	0.000	0.000	0.000
115	A	126	LYS	1	0.890	0.937	7.009	40.332	40.332	0.000	0.000	0.000	0.000
116	A	127	THR	0	0.085	0.042	9.607	-0.061	-0.061	0.000	0.000	0.000	0.000
117	A	128	VAL	0	0.004	0.006	12.038	0.402	0.402	0.000	0.000	0.000	0.000
118	A	129	LEU	0	-0.011	0.010	14.680	0.390	0.390	0.000	0.000	0.000	0.000
119	A	130	VAL	0	-0.003	-0.024	17.480	0.122	0.122	0.000	0.000	0.000	0.000
120	A	131	GLY	0	0.059	0.039	20.204	0.390	0.390	0.000	0.000	0.000	0.000
121	A	132	LEU	0	-0.029	-0.026	21.593	0.138	0.138	0.000	0.000	0.000	0.000
122	A	133	LYS	1	0.857	0.927	24.987	11.194	11.194	0.000	0.000	0.000	0.000
123	A	134	VAL	0	0.028	0.018	27.115	0.418	0.418	0.000	0.000	0.000	0.000
124	A	135	ASP	-1	-0.867	-0.914	29.092	-10.272	-10.272	0.000	0.000	0.000	0.000
125	A	136	LEU	0	-0.052	-0.032	31.905	0.365	0.365	0.000	0.000	0.000	0.000
126	A	137	ARG	1	0.747	0.854	28.652	10.879	10.879	0.000	0.000	0.000	0.000
127	A	138	LYS	1	0.889	0.934	34.034	8.130	8.130	0.000	0.000	0.000	0.000
128	A	139	ASP	-1	-0.873	-0.927	37.609	-8.298	-8.298	0.000	0.000	0.000	0.000
129	A	140	GLY	0	-0.072	-0.047	39.727	0.145	0.145	0.000	0.000	0.000	0.000
130	A	141	SER	0	-0.051	-0.022	37.258	0.227	0.227	0.000	0.000	0.000	0.000
131	A	142	ASP	-1	-0.912	-0.964	36.492	-8.753	-8.753	0.000	0.000	0.000	0.000
132	A	143	ASP	-1	-0.794	-0.896	33.360	-9.313	-9.313	0.000	0.000	0.000	0.000
133	A	144	VAL	0	-0.042	-0.006	28.007	0.056	0.056	0.000	0.000	0.000	0.000
134	A	145	THR	0	-0.003	-0.031	30.489	-0.208	-0.208	0.000	0.000	0.000	0.000
135	A	146	LYS	1	0.871	0.917	24.236	12.425	12.425	0.000	0.000	0.000	0.000
136	A	147	GLN	0	0.006	-0.002	27.040	-0.331	-0.331	0.000	0.000	0.000	0.000
137	A	148	GLU	-1	-0.727	-0.817	28.038	-10.161	-10.161	0.000	0.000	0.000	0.000
138	A	149	GLY	0	0.040	0.020	24.795	-0.279	-0.279	0.000	0.000	0.000	0.000
139	A	150	ASP	-1	-0.822	-0.916	23.378	-13.406	-13.406	0.000	0.000	0.000	0.000
140	A	151	ASP	-1	-0.920	-0.962	23.809	-11.300	-11.300	0.000	0.000	0.000	0.000
141	A	152	LEU	0	-0.082	-0.041	22.736	-0.168	-0.168	0.000	0.000	0.000	0.000
142	A	153	CYS	0	-0.023	-0.001	19.163	-0.720	-0.720	0.000	0.000	0.000	0.000
143	A	154	GLN	0	-0.014	0.000	20.048	-0.879	-0.879	0.000	0.000	0.000	0.000
144	A	155	LYS	1	0.879	0.931	22.262	11.089	11.089	0.000	0.000	0.000	0.000
145	A	156	LEU	0	-0.010	-0.007	19.293	0.083	0.083	0.000	0.000	0.000	0.000
146	A	157	GLY	0	-0.009	0.017	17.655	-0.754	-0.754	0.000	0.000	0.000	0.000
147	A	158	CYS	0	-0.079	-0.034	15.274	-0.939	-0.939	0.000	0.000	0.000	0.000
148	A	159	VAL	0	-0.002	-0.024	11.135	0.393	0.393	0.000	0.000	0.000	0.000
149	A	160	ALA	0	-0.033	-0.022	14.499	0.537	0.537	0.000	0.000	0.000	0.000
150	A	161	TYR	0	-0.056	-0.035	17.216	-0.272	-0.272	0.000	0.000	0.000	0.000
151	A	162	ILE	0	-0.047	-0.011	16.354	0.238	0.238	0.000	0.000	0.000	0.000
152	A	163	GLU	-1	-0.737	-0.815	20.668	-11.426	-11.426	0.000	0.000	0.000	0.000
153	A	164	ALA	0	0.006	-0.008	21.911	-0.073	-0.073	0.000	0.000	0.000	0.000
154	A	165	SER	0	-0.046	-0.063	24.040	0.419	0.419	0.000	0.000	0.000	0.000
155	A	166	SER	0	0.022	-0.007	24.029	-0.089	-0.089	0.000	0.000	0.000	0.000
156	A	167	VAL	0	-0.001	0.009	26.070	0.137	0.137	0.000	0.000	0.000	0.000
157	A	168	ALA	0	-0.004	-0.016	29.808	0.105	0.105	0.000	0.000	0.000	0.000
158	A	169	LYS	1	0.845	0.926	25.999	11.343	11.343	0.000	0.000	0.000	0.000
159	A	170	ILE	0	0.039	0.032	25.761	-0.146	-0.146	0.000	0.000	0.000	0.000
160	A	171	GLY	0	0.065	0.026	22.275	-0.236	-0.236	0.000	0.000	0.000	0.000
161	A	172	LEU	0	-0.043	-0.018	20.211	-0.760	-0.760	0.000	0.000	0.000	0.000
162	A	173	ASN	0	0.018	0.006	17.745	-0.987	-0.987	0.000	0.000	0.000	0.000
163	A	174	GLU	-1	-0.808	-0.890	16.361	-16.483	-16.483	0.000	0.000	0.000	0.000
164	A	175	VAL	0	0.004	0.000	15.716	-1.054	-1.054	0.000	0.000	0.000	0.000
165	A	176	PHE	0	0.014	0.010	12.745	-1.586	-1.586	0.000	0.000	0.000	0.000
166	A	177	GLU	-1	-0.907	-0.961	11.597	-19.743	-19.743	0.000	0.000	0.000	0.000
167	A	178	LYS	1	0.879	0.922	11.787	15.685	15.685	0.000	0.000	0.000	0.000
168	A	179	SER	0	0.006	-0.014	9.811	-1.220	-1.220	0.000	0.000	0.000	0.000
169	A	180	VAL	0	-0.015	-0.003	7.351	-4.440	-4.440	0.000	0.000	0.000	0.000
170	A	181	ASP	-1	-0.789	-0.886	7.287	-27.196	-27.196	0.000	0.000	0.000	0.000
171	A	182	CYS	0	-0.120	-0.023	8.604	-0.589	-0.589	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:GLY)