FMO DATABASE

FMODB ID: KK563

Calculation Name: 1VHZ-B-Xray547

Preferred Name:

Target Type:

Ligand Name: adenosine-5-diphosphoribose

Ligand 3-letter code: APR

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VHZ

Chain ID: B

ChEMBL ID:

UniProt ID: P45799

Base Structure: X-ray

Registration Date: 2025-10-03

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	185
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1882526.984045
FMO2-HF: Nuclear repulsion	1808812.433937
FMO2-HF: Total energy	-73714.550108
FMO2-MP2: Total energy	-73929.449008

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-46.113	-44.727	-0.009	-0.597	-0.781	-0.002

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.875 / q_NPA : 0.924

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	4	SER	0	0.050	0.027	3.815	-0.250	1.136	-0.009	-0.597	-0.781	-0.002
4	A	5	LEU	0	0.013	0.006	6.354	0.132	0.132	0.000	0.000	0.000	0.000
5	A	6	GLN	0	0.006	-0.011	8.551	1.015	1.015	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.961	0.979	11.797	16.517	16.517	0.000	0.000	0.000	0.000
7	A	8	PRO	0	0.018	0.017	14.870	-0.291	-0.291	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.018	-0.005	16.865	0.801	0.801	0.000	0.000	0.000	0.000
9	A	10	ILE	0	0.016	-0.007	19.825	0.043	0.043	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.048	-0.021	22.745	0.227	0.227	0.000	0.000	0.000	0.000
11	A	12	ASN	0	0.013	0.008	25.336	0.542	0.542	0.000	0.000	0.000	0.000
12	A	13	VAL	0	-0.056	-0.033	27.616	-0.405	-0.405	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.905	-0.934	30.085	-8.817	-8.817	0.000	0.000	0.000	0.000
14	A	15	THR	0	-0.096	-0.061	33.115	-0.034	-0.034	0.000	0.000	0.000	0.000
15	A	16	VAL	0	0.047	0.033	33.270	0.223	0.223	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.022	0.017	36.026	0.232	0.232	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.919	0.952	37.599	7.692	7.692	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.012	0.010	40.191	0.187	0.187	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.979	0.977	42.349	6.616	6.616	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.016	0.019	40.931	0.043	0.043	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.032	0.029	36.111	-0.211	-0.211	0.000	0.000	0.000	0.000
22	A	23	THR	0	0.012	-0.020	35.577	0.211	0.211	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.028	0.027	31.937	-0.215	-0.215	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.824	-0.930	30.424	-9.857	-9.857	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.067	0.041	29.632	-0.425	-0.425	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.027	-0.024	24.637	0.055	0.055	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.816	-0.898	25.393	-11.466	-11.466	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.047	-0.035	20.018	-0.382	-0.382	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.820	-0.899	18.046	-15.202	-15.202	0.000	0.000	0.000	0.000
30	A	31	PHE	0	0.005	0.002	13.865	-0.729	-0.729	0.000	0.000	0.000	0.000
31	A	32	SER	0	-0.016	-0.006	10.385	-1.145	-1.145	0.000	0.000	0.000	0.000
32	A	33	ASN	0	-0.031	-0.032	10.867	-0.441	-0.441	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.063	0.043	12.617	0.456	0.456	0.000	0.000	0.000	0.000
34	A	35	VAL	0	-0.047	-0.012	15.214	1.128	1.128	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.883	0.920	17.266	13.710	13.710	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.876	0.934	18.864	15.216	15.216	0.000	0.000	0.000	0.000
37	A	38	VAL	0	0.081	0.058	22.307	-0.070	-0.070	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.070	-0.045	18.788	-0.252	-0.252	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.878	-0.932	25.356	-9.621	-9.621	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.813	0.898	25.450	10.941	10.941	0.000	0.000	0.000	0.000
41	A	42	MET	0	0.024	0.021	28.571	0.457	0.457	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.861	0.934	30.001	8.817	8.817	0.000	0.000	0.000	0.000
43	A	44	PRO	0	-0.060	-0.022	27.916	0.055	0.055	0.000	0.000	0.000	0.000
44	A	45	THR	0	0.003	-0.005	30.214	0.318	0.318	0.000	0.000	0.000	0.000
45	A	46	ASN	0	0.006	-0.007	31.059	-0.508	-0.508	0.000	0.000	0.000	0.000
46	A	47	ARG	1	0.854	0.924	32.883	7.716	7.716	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.799	-0.878	31.123	-9.982	-9.982	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.050	0.030	34.364	0.247	0.247	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.008	-0.011	35.546	-0.279	-0.279	0.000	0.000	0.000	0.000
50	A	51	MET	0	-0.004	0.002	35.744	-0.062	-0.062	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.018	0.017	38.644	-0.159	-0.159	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.026	-0.008	38.930	0.058	0.058	0.000	0.000	0.000	0.000
53	A	54	PRO	0	0.028	0.018	42.025	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.033	-0.023	42.646	0.012	0.012	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.007	-0.004	47.015	0.059	0.059	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.901	-0.947	50.818	-5.752	-5.752	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.890	-0.927	48.939	-6.241	-6.241	0.000	0.000	0.000	0.000
58	A	59	HIS	0	-0.092	-0.065	48.404	-0.036	-0.036	0.000	0.000	0.000	0.000
59	A	60	LEU	0	0.000	0.006	42.585	-0.044	-0.044	0.000	0.000	0.000	0.000
60	A	61	ILE	0	-0.014	-0.014	46.247	0.149	0.149	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.056	-0.025	43.287	-0.169	-0.169	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.059	0.028	44.867	0.195	0.195	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.918	0.952	46.217	6.279	6.279	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.876	-0.943	44.401	-6.870	-6.870	0.000	0.000	0.000	0.000
65	A	66	TYR	0	0.001	0.014	46.004	-0.135	-0.135	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.033	0.019	41.940	-0.079	-0.079	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.025	-0.005	43.940	-0.030	-0.030	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.070	-0.033	40.767	0.004	0.004	0.000	0.000	0.000	0.000
69	A	70	THR	0	-0.051	-0.035	39.926	-0.171	-0.171	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.989	-0.971	42.595	-6.562	-6.562	0.000	0.000	0.000	0.000
71	A	72	SER	0	-0.037	-0.022	44.465	0.100	0.100	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.095	-0.077	46.171	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.857	-0.916	40.257	-7.842	-7.842	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.043	-0.029	43.442	0.230	0.230	0.000	0.000	0.000	0.000
75	A	76	GLY	0	-0.008	-0.020	41.649	-0.202	-0.202	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.058	-0.027	38.314	0.132	0.132	0.000	0.000	0.000	0.000
77	A	78	SER	0	0.011	-0.008	41.741	-0.089	-0.089	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.756	0.851	37.913	7.506	7.506	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.179	0.116	40.538	0.103	0.103	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.141	-0.085	38.179	-0.348	-0.348	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.002	0.009	36.214	0.115	0.115	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.825	-0.894	39.888	-7.208	-7.208	0.000	0.000	0.000	0.000
83	A	84	PRO	0	-0.106	-0.079	40.805	-0.119	-0.119	0.000	0.000	0.000	0.000
84	A	85	GLY	0	-0.011	-0.003	41.016	0.171	0.171	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.775	-0.839	41.893	-7.032	-7.032	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.084	-0.079	39.493	-0.275	-0.275	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.014	-0.031	35.486	0.076	0.076	0.000	0.000	0.000	0.000
88	A	89	TYR	0	0.001	-0.004	37.954	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.822	-0.872	42.064	-6.923	-6.923	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.042	0.035	40.932	0.103	0.103	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.002	-0.010	41.178	0.082	0.082	0.000	0.000	0.000	0.000
92	A	93	ASN	0	0.002	-0.013	43.025	0.143	0.143	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.723	0.833	43.768	7.032	7.032	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.763	-0.899	43.028	-6.950	-6.950	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.053	-0.022	46.247	0.063	0.063	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.815	0.902	47.892	6.160	6.160	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.878	-0.922	48.799	-6.343	-6.343	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.752	-0.850	45.153	-6.871	-6.871	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.075	-0.053	48.692	0.047	0.047	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.016	0.011	51.295	0.112	0.112	0.000	0.000	0.000	0.000
101	A	102	PHE	0	-0.062	-0.044	51.191	0.125	0.125	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.080	0.030	50.417	-0.099	-0.099	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.039	-0.029	47.387	0.037	0.037	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.090	-0.053	49.389	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.917	-0.941	44.931	-7.023	-7.023	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.017	0.007	42.950	-0.064	-0.064	0.000	0.000	0.000	0.000
107	A	108	THR	0	-0.001	-0.001	38.655	-0.137	-0.137	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.032	-0.017	31.549	-0.139	-0.139	0.000	0.000	0.000	0.000
109	A	110	LEU	0	-0.021	0.006	33.900	-0.132	-0.132	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.913	0.942	26.493	10.524	10.524	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.842	0.927	28.431	10.155	10.155	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.006	0.004	27.080	-0.486	-0.486	0.000	0.000	0.000	0.000
113	A	114	SER	0	-0.026	-0.022	24.596	0.092	0.092	0.000	0.000	0.000	0.000
114	A	115	MET	0	0.055	0.025	26.730	-0.243	-0.243	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.033	0.018	25.452	-0.068	-0.068	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.024	0.003	21.646	0.036	0.036	0.000	0.000	0.000	0.000
117	A	118	SER	0	-0.064	-0.026	21.852	-0.305	-0.305	0.000	0.000	0.000	0.000
118	A	119	TYR	0	-0.006	0.006	23.105	-0.038	-0.038	0.000	0.000	0.000	0.000
119	A	120	PHE	0	0.039	0.022	26.635	0.416	0.416	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.012	-0.013	26.529	-0.316	-0.316	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.035	-0.009	27.604	-0.089	-0.089	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.875	0.933	24.894	11.244	11.244	0.000	0.000	0.000	0.000
123	A	124	MET	0	0.032	0.037	30.413	0.258	0.258	0.000	0.000	0.000	0.000
124	A	125	ASN	0	-0.077	-0.054	31.679	-0.493	-0.493	0.000	0.000	0.000	0.000
125	A	126	ILE	0	0.035	0.016	32.006	0.207	0.207	0.000	0.000	0.000	0.000
126	A	127	VAL	0	-0.004	-0.008	35.402	-0.151	-0.151	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.000	0.010	38.558	0.080	0.080	0.000	0.000	0.000	0.000
128	A	129	ALA	0	0.001	0.005	40.930	0.018	0.018	0.000	0.000	0.000	0.000
129	A	130	GLN	0	-0.032	-0.032	44.640	0.053	0.053	0.000	0.000	0.000	0.000
130	A	131	ASP	-1	-0.852	-0.924	47.430	-5.923	-5.923	0.000	0.000	0.000	0.000
131	A	132	LEU	0	0.007	0.011	48.196	-0.019	-0.019	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.024	0.003	51.478	0.128	0.128	0.000	0.000	0.000	0.000
133	A	134	PRO	0	-0.038	-0.029	54.626	-0.067	-0.067	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.857	-0.918	54.677	-5.720	-5.720	0.000	0.000	0.000	0.000
135	A	136	SER	0	-0.001	0.000	54.730	-0.054	-0.054	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.078	-0.033	51.329	0.076	0.076	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.949	-0.974	54.333	-5.558	-5.558	0.000	0.000	0.000	0.000
138	A	139	GLY	0	0.048	0.039	51.282	-0.084	-0.084	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-1.019	-1.019	49.703	-6.084	-6.084	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.909	-0.946	49.949	-6.133	-6.133	0.000	0.000	0.000	0.000
141	A	142	PRO	0	-0.080	-0.043	50.547	0.124	0.124	0.000	0.000	0.000	0.000
142	A	143	GLU	-1	-0.892	-0.935	51.948	-5.850	-5.850	0.000	0.000	0.000	0.000
143	A	144	PRO	0	0.001	-0.006	52.934	-0.084	-0.084	0.000	0.000	0.000	0.000
144	A	145	LEU	0	0.086	0.055	47.966	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	146	PRO	0	-0.070	-0.030	51.101	0.051	0.051	0.000	0.000	0.000	0.000
146	A	147	GLN	0	0.025	0.011	50.653	-0.114	-0.114	0.000	0.000	0.000	0.000
147	A	148	VAL	0	-0.048	-0.025	48.873	0.111	0.111	0.000	0.000	0.000	0.000
148	A	149	ARG	1	0.916	0.977	49.264	5.809	5.809	0.000	0.000	0.000	0.000
149	A	150	TRP	0	0.015	-0.007	45.368	0.104	0.104	0.000	0.000	0.000	0.000
150	A	151	PRO	0	0.007	0.014	47.292	-0.104	-0.104	0.000	0.000	0.000	0.000
151	A	152	LEU	0	0.049	0.010	43.701	-0.133	-0.133	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.001	-0.003	44.126	-0.142	-0.142	0.000	0.000	0.000	0.000
153	A	154	HIS	1	0.790	0.877	45.015	6.573	6.573	0.000	0.000	0.000	0.000
154	A	155	MET	0	0.031	0.037	39.204	-0.036	-0.036	0.000	0.000	0.000	0.000
155	A	156	MET	0	0.001	-0.001	36.056	-0.107	-0.107	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.820	-0.896	40.425	-7.007	-7.007	0.000	0.000	0.000	0.000
157	A	158	LEU	0	-0.012	0.001	41.213	0.052	0.052	0.000	0.000	0.000	0.000
158	A	159	LEU	0	-0.024	-0.018	35.453	-0.097	-0.097	0.000	0.000	0.000	0.000
159	A	160	GLU	-1	-0.967	-0.965	39.471	-7.614	-7.614	0.000	0.000	0.000	0.000
160	A	161	ASP	-1	-0.892	-0.943	42.352	-6.734	-6.734	0.000	0.000	0.000	0.000
161	A	162	PRO	0	-0.076	-0.057	40.994	-0.196	-0.196	0.000	0.000	0.000	0.000
162	A	163	ASP	-1	-0.871	-0.918	41.029	-6.969	-6.969	0.000	0.000	0.000	0.000
163	A	164	PHE	0	0.011	0.005	37.936	-0.102	-0.102	0.000	0.000	0.000	0.000
164	A	165	ASN	0	-0.069	-0.033	36.946	-0.364	-0.364	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.752	-0.854	35.035	-9.019	-9.019	0.000	0.000	0.000	0.000
166	A	167	ALA	0	-0.016	-0.021	30.151	-0.063	-0.063	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.806	0.884	31.811	8.446	8.446	0.000	0.000	0.000	0.000
168	A	169	ASN	0	0.062	0.039	33.516	0.018	0.018	0.000	0.000	0.000	0.000
169	A	170	VAL	0	0.060	0.025	32.647	0.016	0.016	0.000	0.000	0.000	0.000
170	A	171	SER	0	-0.053	-0.048	30.204	-0.195	-0.195	0.000	0.000	0.000	0.000
171	A	172	ALA	0	-0.002	-0.009	32.060	-0.060	-0.060	0.000	0.000	0.000	0.000
172	A	173	LEU	0	0.026	0.028	34.939	0.078	0.078	0.000	0.000	0.000	0.000
173	A	174	PHE	0	-0.021	-0.017	32.067	0.072	0.072	0.000	0.000	0.000	0.000
174	A	175	LEU	0	-0.045	-0.027	29.434	-0.046	-0.046	0.000	0.000	0.000	0.000
175	A	176	VAL	0	0.059	0.024	33.359	0.048	0.048	0.000	0.000	0.000	0.000
176	A	177	ARG	1	0.867	0.936	33.594	8.864	8.864	0.000	0.000	0.000	0.000
177	A	178	GLU	-1	-0.912	-0.960	31.499	-9.120	-9.120	0.000	0.000	0.000	0.000
178	A	179	TRP	0	-0.008	-0.009	34.903	0.075	0.075	0.000	0.000	0.000	0.000
179	A	180	LEU	0	0.037	0.010	36.844	0.129	0.129	0.000	0.000	0.000	0.000
180	A	181	LYS	1	0.788	0.873	36.874	7.942	7.942	0.000	0.000	0.000	0.000
181	A	182	GLY	0	-0.028	-0.007	37.369	0.093	0.093	0.000	0.000	0.000	0.000
182	A	183	GLN	0	-0.049	-0.021	37.997	0.214	0.214	0.000	0.000	0.000	0.000
183	A	184	GLY	0	-0.035	-0.019	41.360	0.191	0.191	0.000	0.000	0.000	0.000
184	A	185	ARG	1	0.849	0.927	42.930	6.859	6.859	0.000	0.000	0.000	0.000
185	A	186	VAL	-1	-0.852	-0.886	41.663	-7.250	-7.250	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)