FMO DATABASE

FMODB ID: 64M3Z

Calculation Name: 4Z1O-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 1-o-pyrophosphono-5-o-phosphono-alpha-d-ribofuranose

Ligand 3-letter code: PRP

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4Z1O

Chain ID: A

ChEMBL ID:

UniProt ID: D0KMY9

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	176
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1871897.335319
FMO2-HF: Nuclear repulsion	1802409.395018
FMO2-HF: Total energy	-69487.940301
FMO2-MP2: Total energy	-69695.900057

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:4:TYR)

Summations of interaction energy for fragment #1(A:4:TYR)

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.
-26.009	-11.168	15.292	-10.362	-19.768	-0.062

Interaction energy analysis for fragmet #1(A:4:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.791 / q_NPA : 0.886

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	6	ILE	0	-0.008	-0.011	2.629	-4.021	-1.342	0.999	-1.147	-2.530	-0.006
4	A	7	PRO	0	0.002	0.043	4.869	2.651	2.705	-0.001	-0.009	-0.043	0.000
138	A	141	LYS	1	0.881	0.945	2.666	44.440	45.300	0.522	-0.267	-1.114	-0.004
139	A	142	TRP	0	0.012	0.006	2.172	0.753	3.117	3.458	-1.945	-3.877	-0.006
140	A	143	ILE	0	0.040	0.012	2.213	-28.698	-24.854	5.286	-4.941	-4.189	-0.058
141	A	144	ILE	0	-0.060	-0.022	2.701	0.468	2.047	2.265	-0.651	-3.193	0.002
142	A	145	PHE	0	0.093	0.041	5.179	-0.185	-0.160	-0.001	-0.002	-0.022	0.000
149	A	152	VAL	0	0.044	0.017	4.069	-0.022	0.238	0.002	-0.038	-0.224	0.000
153	A	156	ASN	0	0.036	0.013	3.526	0.633	1.008	0.004	-0.113	-0.266	0.000
156	A	159	VAL	0	-0.018	0.013	2.627	-4.391	-2.849	2.104	-0.814	-2.833	0.007
157	A	160	PRO	0	-0.018	0.002	2.744	2.969	4.228	0.654	-0.435	-1.477	0.003
5	A	8	SER	0	0.043	0.015	8.569	0.915	0.915	0.000	0.000	0.000	0.000
6	A	9	TRP	0	0.016	-0.033	11.351	0.040	0.040	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.875	-0.921	14.524	-17.228	-17.228	0.000	0.000	0.000	0.000
8	A	11	GLU	-1	-0.728	-0.835	10.148	-29.473	-29.473	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.081	-0.047	11.170	0.232	0.232	0.000	0.000	0.000	0.000
10	A	13	GLU	-1	-0.924	-0.958	14.554	-13.993	-13.993	0.000	0.000	0.000	0.000
11	A	14	ASP	-1	-0.837	-0.913	16.477	-16.073	-16.073	0.000	0.000	0.000	0.000
12	A	15	ALA	0	-0.097	-0.038	14.710	0.544	0.544	0.000	0.000	0.000	0.000
13	A	16	VAL	0	-0.009	-0.022	16.871	0.666	0.666	0.000	0.000	0.000	0.000
14	A	17	PHE	0	0.021	0.005	19.715	0.821	0.821	0.000	0.000	0.000	0.000
15	A	18	SER	0	-0.011	-0.010	19.354	0.496	0.496	0.000	0.000	0.000	0.000
16	A	19	ILE	0	-0.072	-0.024	18.892	0.468	0.468	0.000	0.000	0.000	0.000
17	A	20	GLY	0	0.046	0.015	22.087	0.580	0.580	0.000	0.000	0.000	0.000
18	A	21	GLU	-1	-0.915	-0.964	24.656	-12.300	-12.300	0.000	0.000	0.000	0.000
19	A	22	ALA	0	-0.027	-0.012	23.875	0.510	0.510	0.000	0.000	0.000	0.000
20	A	23	LEU	0	-0.007	0.003	25.227	0.447	0.447	0.000	0.000	0.000	0.000
21	A	24	VAL	0	0.007	0.006	27.912	0.491	0.491	0.000	0.000	0.000	0.000
22	A	25	LYS	1	0.900	0.957	28.784	10.353	10.353	0.000	0.000	0.000	0.000
23	A	26	SER	0	-0.050	-0.039	28.334	0.261	0.261	0.000	0.000	0.000	0.000
24	A	27	ASN	0	-0.078	-0.028	31.061	0.252	0.252	0.000	0.000	0.000	0.000
25	A	28	TYR	0	-0.023	-0.046	28.981	0.379	0.379	0.000	0.000	0.000	0.000
26	A	29	ILE	0	0.057	0.034	30.416	-0.330	-0.330	0.000	0.000	0.000	0.000
27	A	30	PRO	0	-0.024	-0.014	28.757	0.327	0.327	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.806	-0.899	32.075	-8.492	-8.492	0.000	0.000	0.000	0.000
29	A	32	VAL	0	-0.056	-0.040	30.526	0.152	0.152	0.000	0.000	0.000	0.000
30	A	33	LEU	0	0.005	0.021	25.256	-0.223	-0.223	0.000	0.000	0.000	0.000
31	A	34	ILE	0	-0.022	-0.021	25.536	0.194	0.194	0.000	0.000	0.000	0.000
32	A	35	ALA	0	0.026	0.011	22.922	-0.472	-0.472	0.000	0.000	0.000	0.000
33	A	36	VAL	0	-0.016	-0.018	19.406	0.547	0.547	0.000	0.000	0.000	0.000
34	A	37	LEU	0	-0.068	-0.017	20.062	-0.495	-0.495	0.000	0.000	0.000	0.000
35	A	38	THR	0	-0.016	-0.036	17.290	-0.114	-0.114	0.000	0.000	0.000	0.000
36	A	39	GLY	0	0.053	0.028	15.316	0.052	0.052	0.000	0.000	0.000	0.000
37	A	40	GLY	0	0.067	0.026	15.950	-0.270	-0.270	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.055	-0.017	18.697	0.627	0.627	0.000	0.000	0.000	0.000
39	A	42	ILE	0	-0.013	0.001	16.402	0.590	0.590	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.022	0.007	16.170	0.443	0.443	0.000	0.000	0.000	0.000
41	A	44	ALA	0	0.025	0.021	18.916	0.524	0.524	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.945	0.972	22.330	11.609	11.609	0.000	0.000	0.000	0.000
43	A	46	LEU	0	0.008	-0.001	18.435	0.432	0.432	0.000	0.000	0.000	0.000
44	A	47	LEU	0	0.025	0.013	22.403	0.352	0.352	0.000	0.000	0.000	0.000
45	A	48	SER	0	-0.085	-0.059	23.947	0.465	0.465	0.000	0.000	0.000	0.000
46	A	49	ASP	-1	-0.981	-0.987	25.789	-10.540	-10.540	0.000	0.000	0.000	0.000
47	A	50	LEU	0	0.004	0.015	23.609	0.348	0.348	0.000	0.000	0.000	0.000
48	A	51	LEU	0	-0.039	-0.022	26.872	0.240	0.240	0.000	0.000	0.000	0.000
49	A	52	ASP	-1	-0.794	-0.861	29.411	-8.604	-8.604	0.000	0.000	0.000	0.000
50	A	53	LEU	0	-0.011	0.009	28.018	0.301	0.301	0.000	0.000	0.000	0.000
51	A	54	LYS	1	0.778	0.861	30.519	8.470	8.470	0.000	0.000	0.000	0.000
52	A	55	VAL	0	-0.053	-0.012	32.570	0.115	0.115	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.026	0.025	26.447	-0.222	-0.222	0.000	0.000	0.000	0.000
54	A	57	ARG	1	0.764	0.850	28.913	9.393	9.393	0.000	0.000	0.000	0.000
55	A	58	TYR	0	0.029	0.011	25.221	-0.493	-0.493	0.000	0.000	0.000	0.000
56	A	59	ILE	0	0.011	0.008	24.031	0.413	0.413	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.808	-0.865	23.480	-12.527	-12.527	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.020	0.004	21.280	0.430	0.430	0.000	0.000	0.000	0.000
59	A	62	LYS	1	0.898	0.961	16.698	14.379	14.379	0.000	0.000	0.000	0.000
60	A	63	PHE	0	0.035	0.027	16.529	0.450	0.450	0.000	0.000	0.000	0.000
61	A	64	TYR	0	-0.008	-0.013	16.281	-0.808	-0.808	0.000	0.000	0.000	0.000
62	A	65	ARG	0	0.024	0.072	8.256	-2.170	-2.170	0.000	0.000	0.000	0.000
63	A	66	SER	0	0.013	-0.002	12.907	0.780	0.780	0.000	0.000	0.000	0.000
64	A	67	VAL	0	0.036	0.014	14.586	-0.468	-0.468	0.000	0.000	0.000	0.000
65	A	68	GLY	0	0.080	0.045	16.038	0.631	0.631	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.889	0.924	18.321	12.395	12.395	0.000	0.000	0.000	0.000
67	A	70	THR	0	-0.052	-0.012	18.459	0.480	0.480	0.000	0.000	0.000	0.000
68	A	71	GLU	-1	-0.821	-0.914	20.084	-11.696	-11.696	0.000	0.000	0.000	0.000
69	A	72	SER	0	-0.103	-0.065	20.292	-0.387	-0.387	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.889	0.940	21.515	11.840	11.840	0.000	0.000	0.000	0.000
71	A	74	PRO	0	-0.028	0.009	20.582	-0.306	-0.306	0.000	0.000	0.000	0.000
72	A	75	VAL	0	0.014	-0.001	21.631	0.565	0.565	0.000	0.000	0.000	0.000
73	A	76	ILE	0	-0.003	-0.013	23.831	-0.297	-0.297	0.000	0.000	0.000	0.000
74	A	77	ARG	1	0.765	0.852	21.521	12.430	12.430	0.000	0.000	0.000	0.000
75	A	78	SER	0	0.009	0.004	27.606	0.454	0.454	0.000	0.000	0.000	0.000
76	A	79	VAL	0	0.024	0.005	28.151	-0.434	-0.434	0.000	0.000	0.000	0.000
77	A	80	TYR	0	-0.031	-0.002	27.400	0.439	0.439	0.000	0.000	0.000	0.000
78	A	81	THR	0	0.006	-0.027	31.225	-0.275	-0.275	0.000	0.000	0.000	0.000
79	A	82	ASP	-1	-0.799	-0.841	33.426	-8.292	-8.292	0.000	0.000	0.000	0.000
80	A	83	SER	0	0.020	0.002	36.025	-0.238	-0.238	0.000	0.000	0.000	0.000
81	A	84	LEU	0	-0.011	-0.016	32.124	-0.052	-0.052	0.000	0.000	0.000	0.000
82	A	85	GLU	-1	-0.851	-0.903	36.342	-7.415	-7.415	0.000	0.000	0.000	0.000
83	A	86	GLY	0	-0.018	-0.014	39.429	0.080	0.080	0.000	0.000	0.000	0.000
84	A	87	LYS	1	0.900	0.963	35.872	8.345	8.345	0.000	0.000	0.000	0.000
85	A	88	LYS	1	0.818	0.906	33.588	8.659	8.659	0.000	0.000	0.000	0.000
86	A	89	VAL	0	0.029	0.013	29.171	-0.108	-0.108	0.000	0.000	0.000	0.000
87	A	90	LEU	0	-0.016	0.011	24.798	-0.077	-0.077	0.000	0.000	0.000	0.000
88	A	91	VAL	0	-0.012	-0.006	22.725	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	92	VAL	0	0.004	-0.004	20.382	-0.316	-0.316	0.000	0.000	0.000	0.000
90	A	93	ASP	-1	-0.807	-0.932	17.099	-16.370	-16.370	0.000	0.000	0.000	0.000
91	A	94	ASP	-1	-0.846	-0.908	13.166	-20.757	-20.757	0.000	0.000	0.000	0.000
92	A	95	VAL	0	-0.049	-0.038	10.003	-1.263	-1.263	0.000	0.000	0.000	0.000
93	A	96	ALA	0	0.019	0.020	13.048	0.964	0.964	0.000	0.000	0.000	0.000
94	A	97	ASP	-1	-0.825	-0.916	10.151	-26.675	-26.675	0.000	0.000	0.000	0.000
95	A	98	THR	0	0.081	0.020	13.155	0.426	0.426	0.000	0.000	0.000	0.000
96	A	99	GLY	0	0.049	0.032	16.297	0.805	0.805	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.846	-0.920	18.747	-12.189	-12.189	0.000	0.000	0.000	0.000
98	A	101	THR	0	0.012	0.005	17.549	0.777	0.777	0.000	0.000	0.000	0.000
99	A	102	LEU	0	0.098	0.044	19.175	0.681	0.681	0.000	0.000	0.000	0.000
100	A	103	GLU	-1	-0.885	-0.915	21.662	-11.411	-11.411	0.000	0.000	0.000	0.000
101	A	104	ALA	0	0.008	0.003	23.805	0.547	0.547	0.000	0.000	0.000	0.000
102	A	105	VAL	0	0.015	0.006	22.945	0.497	0.497	0.000	0.000	0.000	0.000
103	A	106	SER	0	0.034	0.003	25.323	0.371	0.371	0.000	0.000	0.000	0.000
104	A	107	ASN	0	-0.031	-0.003	27.509	0.456	0.456	0.000	0.000	0.000	0.000
105	A	108	VAL	0	0.012	0.003	28.377	0.353	0.353	0.000	0.000	0.000	0.000
106	A	109	ILE	0	-0.004	-0.005	28.311	0.301	0.301	0.000	0.000	0.000	0.000
107	A	110	THR	0	-0.002	-0.018	31.161	0.283	0.283	0.000	0.000	0.000	0.000
108	A	111	MET	0	-0.060	-0.029	33.523	0.215	0.215	0.000	0.000	0.000	0.000
109	A	112	PHE	0	-0.055	-0.023	32.964	0.218	0.218	0.000	0.000	0.000	0.000
110	A	113	ASN	0	-0.042	-0.027	36.625	0.008	0.008	0.000	0.000	0.000	0.000
111	A	114	PRO	0	0.002	0.017	33.508	0.151	0.151	0.000	0.000	0.000	0.000
112	A	115	ALA	0	-0.005	0.001	36.515	0.044	0.044	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.888	0.936	31.449	9.637	9.637	0.000	0.000	0.000	0.000
114	A	117	VAL	0	0.023	0.027	28.358	-0.078	-0.078	0.000	0.000	0.000	0.000
115	A	118	MET	0	-0.060	-0.007	27.245	0.184	0.184	0.000	0.000	0.000	0.000
116	A	119	THR	0	-0.064	-0.060	22.630	-0.232	-0.232	0.000	0.000	0.000	0.000
117	A	120	ALA	0	0.047	0.017	21.036	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	121	ALA	0	-0.027	-0.005	15.845	0.035	0.035	0.000	0.000	0.000	0.000
119	A	122	LEU	0	0.032	0.027	13.794	0.009	0.009	0.000	0.000	0.000	0.000
120	A	123	TYR	0	-0.057	-0.068	10.662	-0.499	-0.499	0.000	0.000	0.000	0.000
121	A	124	LEU	0	-0.006	0.011	12.668	1.028	1.028	0.000	0.000	0.000	0.000
122	A	125	LYS	1	0.846	0.938	7.231	31.262	31.262	0.000	0.000	0.000	0.000
123	A	126	PRO	0	-0.012	-0.014	10.972	1.703	1.703	0.000	0.000	0.000	0.000
124	A	127	TRP	0	-0.061	-0.034	8.478	0.496	0.496	0.000	0.000	0.000	0.000
125	A	128	SER	0	-0.038	-0.004	15.500	1.012	1.012	0.000	0.000	0.000	0.000
126	A	129	LYS	1	0.842	0.908	16.890	13.096	13.096	0.000	0.000	0.000	0.000
127	A	130	ARG	1	0.841	0.911	19.704	13.170	13.170	0.000	0.000	0.000	0.000
128	A	131	ILE	0	0.020	0.018	19.113	-0.779	-0.779	0.000	0.000	0.000	0.000
129	A	132	PRO	0	-0.019	-0.008	17.673	0.589	0.589	0.000	0.000	0.000	0.000
130	A	133	ASP	-1	-0.836	-0.892	20.868	-12.209	-12.209	0.000	0.000	0.000	0.000
131	A	134	PHE	0	0.003	-0.004	21.859	0.195	0.195	0.000	0.000	0.000	0.000
132	A	135	TYR	0	0.010	-0.017	15.699	-0.770	-0.770	0.000	0.000	0.000	0.000
133	A	136	TYR	0	0.042	0.039	13.427	-0.085	-0.085	0.000	0.000	0.000	0.000
134	A	137	LYS	1	0.893	0.940	12.238	20.522	20.522	0.000	0.000	0.000	0.000
135	A	138	GLN	0	0.015	0.010	12.595	-0.636	-0.636	0.000	0.000	0.000	0.000
136	A	139	ILE	0	-0.050	-0.028	6.178	-1.596	-1.596	0.000	0.000	0.000	0.000
137	A	140	ASP	-1	-0.834	-0.928	7.006	-37.270	-37.270	0.000	0.000	0.000	0.000
143	A	146	PRO	0	-0.018	-0.017	8.604	0.464	0.464	0.000	0.000	0.000	0.000
144	A	147	TRP	0	-0.030	-0.036	11.127	1.119	1.119	0.000	0.000	0.000	0.000
145	A	148	ASP	-1	-0.834	-0.905	8.353	-28.025	-28.025	0.000	0.000	0.000	0.000
146	A	149	LYS	1	0.927	0.954	8.157	23.630	23.630	0.000	0.000	0.000	0.000
147	A	150	TRP	0	-0.026	-0.025	9.219	-0.544	-0.544	0.000	0.000	0.000	0.000
148	A	151	ASP	-1	-0.830	-0.890	10.343	-18.425	-18.425	0.000	0.000	0.000	0.000
150	A	153	VAL	0	-0.035	-0.022	7.076	0.146	0.146	0.000	0.000	0.000	0.000
151	A	154	ARG	1	0.824	0.909	8.880	18.751	18.751	0.000	0.000	0.000	0.000
152	A	155	GLU	0	-0.052	-0.066	8.026	1.743	1.743	0.000	0.000	0.000	0.000
154	A	157	SER	0	0.023	0.003	5.897	-1.805	-1.805	0.000	0.000	0.000	0.000
155	A	158	ASN	0	-0.033	-0.019	5.107	1.490	1.490	0.000	0.000	0.000	0.000
158	A	161	VAL	0	0.020	0.007	5.589	-1.695	-1.695	0.000	0.000	0.000	0.000
159	A	162	ASP	-1	-0.836	-0.913	8.125	-22.388	-22.388	0.000	0.000	0.000	0.000
160	A	163	LYS	1	0.941	0.956	11.614	17.324	17.324	0.000	0.000	0.000	0.000
161	A	164	LYS	1	0.876	0.936	7.741	27.481	27.481	0.000	0.000	0.000	0.000
162	A	165	GLU	-1	-0.844	-0.928	13.304	-18.324	-18.324	0.000	0.000	0.000	0.000
163	A	166	ARG	1	0.972	0.982	16.102	14.219	14.219	0.000	0.000	0.000	0.000
164	A	167	PHE	0	-0.004	0.006	13.507	0.710	0.710	0.000	0.000	0.000	0.000
165	A	168	LEU	0	0.041	0.006	12.296	0.632	0.632	0.000	0.000	0.000	0.000
166	A	169	ASN	0	-0.046	-0.006	16.359	1.037	1.037	0.000	0.000	0.000	0.000
167	A	170	LEU	0	0.056	0.025	20.136	0.454	0.454	0.000	0.000	0.000	0.000
168	A	171	TYR	0	0.005	-0.006	14.694	0.304	0.304	0.000	0.000	0.000	0.000
169	A	172	ASN	0	-0.007	-0.020	18.226	0.755	0.755	0.000	0.000	0.000	0.000
170	A	173	GLN	0	-0.017	-0.010	20.460	0.225	0.225	0.000	0.000	0.000	0.000
171	A	174	LEU	0	0.006	-0.001	20.324	0.366	0.366	0.000	0.000	0.000	0.000
172	A	175	LEU	0	0.011	0.003	17.821	0.364	0.364	0.000	0.000	0.000	0.000
173	A	176	LYS	1	0.848	0.941	22.227	12.057	12.057	0.000	0.000	0.000	0.000
174	A	177	ILE	0	-0.025	-0.013	25.915	0.345	0.345	0.000	0.000	0.000	0.000
175	A	178	ARG	1	0.900	0.949	25.346	10.383	10.383	0.000	0.000	0.000	0.000
176	A	179	LYS	0	0.053	0.055	24.779	-0.806	-0.806	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:TYR)