FMO DATABASE

FMODB ID: LZNG9

Calculation Name: 1JQ6-A-Xray372

Preferred Name: Human herpes virus 5 capsid protein P40

Target Type: SINGLE PROTEIN

Ligand Name: s-(dimethylarsenic)cysteine

ligand 3-letter code: CAS

PDB ID: 1JQ6

Chain ID: A

ChEMBL ID: CHEMBL3771

UniProt ID: P16753

Base Structure: X-ray

Registration Date: 2023-06-22

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	179
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1864337.152054
FMO2-HF: Nuclear repulsion	1788880.912296
FMO2-HF: Total energy	-75456.239758
FMO2-MP2: Total energy	-75658.378255

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:11:VAL)

Summations of interaction energy for fragment #1(A:11: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.
-6.006	-1.069	3.53	-2.408	-6.058	-0.007

Interaction energy analysis for fragmet #1(A:11:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.026 / q_NPA : 0.010

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	13	PRO	0	0.041	0.019	2.700	-3.011	0.149	0.601	-1.702	-2.060	-0.008
4	A	14	VAL	0	-0.046	-0.014	4.747	0.536	0.634	-0.001	-0.005	-0.092	0.000
5	A	15	TYR	0	0.011	0.003	7.379	0.015	0.015	0.000	0.000	0.000	0.000
6	A	16	VAL	0	0.015	-0.002	10.853	0.086	0.086	0.000	0.000	0.000	0.000
7	A	17	GLY	0	0.031	0.012	13.783	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	18	GLY	0	0.034	0.014	17.539	0.021	0.021	0.000	0.000	0.000	0.000
9	A	19	PHE	0	-0.036	-0.017	20.974	-0.006	-0.006	0.000	0.000	0.000	0.000
10	A	20	LEU	0	-0.015	-0.006	21.139	0.007	0.007	0.000	0.000	0.000	0.000
11	A	21	ALA	0	0.005	0.003	24.732	0.016	0.016	0.000	0.000	0.000	0.000
12	A	22	ARG	1	0.817	0.887	28.431	0.154	0.154	0.000	0.000	0.000	0.000
13	A	23	TYR	0	-0.040	-0.033	30.880	0.003	0.003	0.000	0.000	0.000	0.000
14	A	24	ASP	-1	-0.960	-0.963	34.221	-0.114	-0.114	0.000	0.000	0.000	0.000
15	A	34	LEU	0	-0.015	-0.026	30.256	0.003	0.003	0.000	0.000	0.000	0.000
16	A	35	PRO	0	0.023	0.016	34.021	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	36	ARG	1	0.849	0.911	33.654	0.136	0.136	0.000	0.000	0.000	0.000
18	A	37	ASP	-1	-0.895	-0.955	35.146	-0.114	-0.114	0.000	0.000	0.000	0.000
19	A	38	VAL	0	-0.014	-0.008	34.724	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	39	VAL	0	-0.080	-0.038	29.914	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	40	GLU	-1	-0.858	-0.894	31.745	-0.154	-0.154	0.000	0.000	0.000	0.000
22	A	41	HIS	0	-0.009	-0.006	32.739	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	42	TRP	0	-0.070	-0.035	31.135	0.004	0.004	0.000	0.000	0.000	0.000
24	A	55	VAL	0	0.012	-0.013	20.715	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	56	ALA	0	-0.010	0.008	17.129	0.006	0.006	0.000	0.000	0.000	0.000
26	A	57	LEU	0	0.022	0.016	18.743	0.011	0.011	0.000	0.000	0.000	0.000
27	A	58	PRO	0	0.024	0.018	15.564	-0.056	-0.056	0.000	0.000	0.000	0.000
28	A	59	LEU	0	0.002	-0.007	12.656	0.044	0.044	0.000	0.000	0.000	0.000
29	A	60	ASN	0	-0.011	-0.010	13.993	-0.031	-0.031	0.000	0.000	0.000	0.000
30	A	61	ILE	0	-0.006	0.012	12.569	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	62	ASN	0	0.021	-0.019	16.545	0.018	0.018	0.000	0.000	0.000	0.000
32	A	63	HIS	0	0.007	0.004	19.875	0.023	0.023	0.000	0.000	0.000	0.000
33	A	64	ASP	-1	-0.766	-0.835	18.747	-0.072	-0.072	0.000	0.000	0.000	0.000
34	A	65	ASP	-1	-0.940	-0.976	18.248	-0.119	-0.119	0.000	0.000	0.000	0.000
35	A	66	THR	0	-0.007	-0.027	17.619	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	67	ALA	0	-0.011	-0.016	14.541	0.017	0.017	0.000	0.000	0.000	0.000
37	A	68	VAL	0	0.017	-0.002	12.925	-0.052	-0.052	0.000	0.000	0.000	0.000
38	A	69	VAL	0	-0.046	-0.030	9.704	0.025	0.025	0.000	0.000	0.000	0.000
39	A	70	GLY	0	0.045	0.025	8.816	-0.271	-0.271	0.000	0.000	0.000	0.000
40	A	71	HIS	0	-0.054	-0.023	10.609	0.215	0.215	0.000	0.000	0.000	0.000
41	A	72	VAL	0	-0.014	-0.011	13.613	-0.089	-0.089	0.000	0.000	0.000	0.000
42	A	73	ALA	0	-0.035	-0.027	14.721	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	74	ALA	0	-0.031	-0.012	16.808	0.033	0.033	0.000	0.000	0.000	0.000
44	A	75	MET	0	-0.014	-0.011	20.140	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	76	GLN	0	0.031	0.025	23.146	0.000	0.000	0.000	0.000	0.000	0.000
46	A	77	SER	0	0.014	0.020	26.142	0.003	0.003	0.000	0.000	0.000	0.000
47	A	78	VAL	0	-0.018	0.001	26.717	0.005	0.005	0.000	0.000	0.000	0.000
48	A	79	ARG	1	0.828	0.872	29.903	0.162	0.162	0.000	0.000	0.000	0.000
49	A	80	ASP	-1	-0.714	-0.825	30.469	-0.141	-0.141	0.000	0.000	0.000	0.000
50	A	81	GLY	0	0.026	-0.004	29.553	0.005	0.005	0.000	0.000	0.000	0.000
51	A	82	LEU	0	-0.009	0.030	25.611	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	83	PHE	0	0.016	-0.002	20.429	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	84	CYS	0	-0.072	-0.029	19.860	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	85	LEU	0	0.008	0.008	14.831	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	86	GLY	0	0.036	0.011	14.525	0.027	0.027	0.000	0.000	0.000	0.000
56	A	87	CAS	0	-0.060	-0.023	9.900	0.009	0.009	0.000	0.000	0.000	0.000
57	A	88	VAL	0	0.032	0.021	7.802	0.050	0.050	0.000	0.000	0.000	0.000
58	A	89	THR	0	-0.031	-0.061	5.356	-0.333	-0.333	0.000	0.000	0.000	0.000
59	A	90	SER	0	-0.024	-0.029	3.941	-0.900	-0.725	0.001	-0.063	-0.112	0.000
60	A	91	PRO	0	0.014	-0.002	2.379	-1.331	-0.255	1.557	-0.586	-2.046	0.002
61	A	92	ARG	1	0.855	0.935	3.361	-0.073	-0.158	-0.002	0.344	-0.257	0.000
62	A	93	PHE	0	0.049	0.026	6.585	0.033	0.033	0.000	0.000	0.000	0.000
63	A	94	LEU	0	0.014	0.003	2.338	-0.524	-0.191	1.376	-0.384	-1.325	-0.001
64	A	95	GLU	-1	-0.776	-0.858	4.705	1.036	1.164	-0.001	-0.007	-0.120	0.000
65	A	96	ILE	0	-0.048	-0.025	5.807	-0.029	-0.029	0.000	0.000	0.000	0.000
66	A	97	VAL	0	0.013	0.008	7.832	0.004	0.004	0.000	0.000	0.000	0.000
67	A	98	ARG	1	0.776	0.864	6.427	-0.651	-0.651	0.000	0.000	0.000	0.000
68	A	99	ARG	1	0.861	0.930	8.518	-0.621	-0.621	0.000	0.000	0.000	0.000
69	A	100	ALA	0	0.048	0.029	11.235	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	101	SER	0	-0.037	-0.022	11.207	-0.015	-0.015	0.000	0.000	0.000	0.000
71	A	102	GLU	-1	-0.808	-0.901	11.648	0.332	0.332	0.000	0.000	0.000	0.000
72	A	103	LYS	1	0.768	0.894	14.193	-0.234	-0.234	0.000	0.000	0.000	0.000
73	A	104	SER	0	0.000	0.001	16.572	-0.019	-0.019	0.000	0.000	0.000	0.000
74	A	105	GLU	-1	-0.769	-0.860	18.797	0.026	0.026	0.000	0.000	0.000	0.000
75	A	106	LEU	0	-0.062	-0.018	18.233	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	107	VAL	0	-0.021	0.002	14.986	-0.025	-0.025	0.000	0.000	0.000	0.000
77	A	108	SER	0	-0.021	-0.046	18.140	0.022	0.022	0.000	0.000	0.000	0.000
78	A	109	ARG	1	0.780	0.853	18.278	-0.044	-0.044	0.000	0.000	0.000	0.000
79	A	110	GLY	0	0.025	0.016	18.653	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	111	PRO	0	-0.041	-0.017	17.491	0.002	0.002	0.000	0.000	0.000	0.000
81	A	112	VAL	0	0.028	0.015	14.374	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	113	SER	0	0.015	0.006	16.868	0.002	0.002	0.000	0.000	0.000	0.000
83	A	114	PRO	0	0.023	-0.019	16.168	-0.015	-0.015	0.000	0.000	0.000	0.000
84	A	115	LEU	0	-0.030	-0.002	17.252	-0.032	-0.032	0.000	0.000	0.000	0.000
85	A	116	GLN	0	-0.038	-0.014	17.183	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	117	PRO	0	-0.014	-0.008	14.116	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	118	ASP	-1	-0.743	-0.853	9.011	-0.448	-0.448	0.000	0.000	0.000	0.000
88	A	119	LYS	1	0.861	0.896	11.680	0.041	0.041	0.000	0.000	0.000	0.000
89	A	120	VAL	0	0.004	0.015	6.546	0.019	0.019	0.000	0.000	0.000	0.000
90	A	121	VAL	0	0.014	0.016	9.430	-0.034	-0.034	0.000	0.000	0.000	0.000
91	A	122	GLU	-1	-0.752	-0.811	11.410	-0.088	-0.088	0.000	0.000	0.000	0.000
92	A	123	PHE	0	0.063	0.024	12.257	0.012	0.012	0.000	0.000	0.000	0.000
93	A	124	LEU	0	-0.021	0.013	8.921	0.016	0.016	0.000	0.000	0.000	0.000
94	A	125	SER	0	-0.014	-0.024	13.399	0.006	0.006	0.000	0.000	0.000	0.000
95	A	126	GLY	0	0.003	0.013	16.302	0.021	0.021	0.000	0.000	0.000	0.000
96	A	127	SER	0	-0.094	-0.057	14.947	0.017	0.017	0.000	0.000	0.000	0.000
97	A	128	TYR	0	0.074	0.017	13.476	0.023	0.023	0.000	0.000	0.000	0.000
98	A	129	ALA	0	0.049	0.043	17.287	-0.034	-0.034	0.000	0.000	0.000	0.000
99	A	130	GLY	0	0.013	0.005	19.517	0.010	0.010	0.000	0.000	0.000	0.000
100	A	131	LEU	0	-0.002	-0.001	17.231	-0.023	-0.023	0.000	0.000	0.000	0.000
101	A	132	SER	0	-0.014	-0.010	20.605	0.024	0.024	0.000	0.000	0.000	0.000
102	A	133	LEU	0	0.067	0.041	22.212	-0.015	-0.015	0.000	0.000	0.000	0.000
103	A	134	SER	0	-0.004	0.003	24.300	0.016	0.016	0.000	0.000	0.000	0.000
104	A	155	PHE	0	0.006	-0.015	24.708	0.003	0.003	0.000	0.000	0.000	0.000
105	A	156	LYS	1	0.936	0.981	23.738	0.143	0.143	0.000	0.000	0.000	0.000
106	A	157	HIS	0	-0.001	-0.013	19.630	0.003	0.003	0.000	0.000	0.000	0.000
107	A	158	VAL	0	-0.004	-0.001	18.544	0.019	0.019	0.000	0.000	0.000	0.000
108	A	159	ALA	0	-0.002	0.023	18.103	-0.027	-0.027	0.000	0.000	0.000	0.000
109	A	160	LEU	0	0.012	-0.001	12.404	0.000	0.000	0.000	0.000	0.000	0.000
110	A	161	CAS	0	-0.047	-0.016	17.076	0.039	0.039	0.000	0.000	0.000	0.000
111	A	162	SER	0	0.054	0.028	18.915	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	163	VAL	0	-0.034	-0.023	20.478	0.014	0.014	0.000	0.000	0.000	0.000
113	A	164	GLY	0	0.040	0.052	24.353	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	165	ARG	1	0.888	0.944	24.569	0.161	0.161	0.000	0.000	0.000	0.000
115	A	166	ARG	1	0.921	0.937	27.414	0.088	0.088	0.000	0.000	0.000	0.000
116	A	167	ARG	1	0.903	0.941	20.910	0.101	0.101	0.000	0.000	0.000	0.000
117	A	168	GLY	0	0.044	0.026	22.805	-0.012	-0.012	0.000	0.000	0.000	0.000
118	A	169	THR	0	-0.015	-0.020	23.279	0.013	0.013	0.000	0.000	0.000	0.000
119	A	170	LEU	0	-0.058	0.006	21.850	0.000	0.000	0.000	0.000	0.000	0.000
120	A	171	ALA	0	0.000	0.019	17.401	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	172	VAL	0	-0.008	-0.005	16.813	0.022	0.022	0.000	0.000	0.000	0.000
122	A	173	TYR	0	0.011	-0.015	11.413	-0.064	-0.064	0.000	0.000	0.000	0.000
123	A	174	GLY	0	0.019	-0.010	11.636	0.087	0.087	0.000	0.000	0.000	0.000
124	A	175	ARG	1	0.784	0.855	4.219	1.068	1.120	-0.001	-0.005	-0.046	0.000
125	A	176	ASP	-1	-0.768	-0.883	10.144	-0.692	-0.692	0.000	0.000	0.000	0.000
126	A	177	PRO	0	0.029	0.024	12.594	0.070	0.070	0.000	0.000	0.000	0.000
127	A	178	GLU	-1	-0.820	-0.865	15.250	-0.307	-0.307	0.000	0.000	0.000	0.000
128	A	179	TRP	0	-0.035	-0.021	15.671	0.039	0.039	0.000	0.000	0.000	0.000
129	A	180	VAL	0	0.008	-0.001	13.809	0.047	0.047	0.000	0.000	0.000	0.000
130	A	181	THR	0	0.002	-0.021	16.996	0.048	0.048	0.000	0.000	0.000	0.000
131	A	182	GLN	0	-0.032	-0.029	20.184	0.049	0.049	0.000	0.000	0.000	0.000
132	A	183	ARG	1	0.814	0.925	19.137	0.329	0.329	0.000	0.000	0.000	0.000
133	A	184	PHE	0	0.001	0.009	19.344	0.022	0.022	0.000	0.000	0.000	0.000
134	A	185	PRO	0	-0.007	-0.015	24.318	0.000	0.000	0.000	0.000	0.000	0.000
135	A	186	ASP	-1	-0.838	-0.887	27.702	-0.164	-0.164	0.000	0.000	0.000	0.000
136	A	187	LEU	0	-0.037	0.004	23.511	0.007	0.007	0.000	0.000	0.000	0.000
137	A	188	THR	0	0.009	-0.018	27.615	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	189	ALA	0	-0.003	-0.017	27.984	-0.015	-0.015	0.000	0.000	0.000	0.000
139	A	190	ALA	0	0.072	0.035	27.891	-0.015	-0.015	0.000	0.000	0.000	0.000
140	A	191	ASP	-1	-0.785	-0.872	26.941	-0.211	-0.211	0.000	0.000	0.000	0.000
141	A	192	ARG	1	0.841	0.913	23.820	0.210	0.210	0.000	0.000	0.000	0.000
142	A	193	ASP	-1	-0.827	-0.918	23.483	-0.286	-0.286	0.000	0.000	0.000	0.000
143	A	194	GLY	0	0.020	0.022	25.215	-0.012	-0.012	0.000	0.000	0.000	0.000
144	A	195	LEU	0	-0.030	-0.018	20.638	-0.014	-0.014	0.000	0.000	0.000	0.000
145	A	196	ARG	1	0.799	0.869	20.492	0.289	0.289	0.000	0.000	0.000	0.000
146	A	197	ALA	0	0.007	0.003	20.803	-0.030	-0.030	0.000	0.000	0.000	0.000
147	A	198	GLN	0	-0.088	-0.049	21.068	0.005	0.005	0.000	0.000	0.000	0.000
148	A	199	TRP	0	0.097	0.036	16.033	-0.046	-0.046	0.000	0.000	0.000	0.000
149	A	200	GLN	0	-0.003	-0.008	15.894	-0.056	-0.056	0.000	0.000	0.000	0.000
150	A	201	ARG	1	0.911	0.958	17.037	0.315	0.315	0.000	0.000	0.000	0.000
151	A	202	CAS	0	-0.036	-0.004	12.838	0.009	0.009	0.000	0.000	0.000	0.000
152	A	203	GLY	0	-0.006	0.016	12.936	-0.098	-0.098	0.000	0.000	0.000	0.000
153	A	204	SER	0	-0.052	-0.030	14.210	0.031	0.031	0.000	0.000	0.000	0.000
154	A	205	THR	0	-0.040	-0.032	14.897	0.092	0.092	0.000	0.000	0.000	0.000
155	A	206	ALA	0	-0.026	-0.009	13.654	-0.088	-0.088	0.000	0.000	0.000	0.000
156	A	207	VAL	0	0.046	0.016	10.025	0.048	0.048	0.000	0.000	0.000	0.000
157	A	208	ASP	-1	-0.801	-0.879	8.371	-1.128	-1.128	0.000	0.000	0.000	0.000
158	A	209	ALA	0	0.016	0.014	9.923	0.111	0.111	0.000	0.000	0.000	0.000
159	A	210	SER	0	-0.035	-0.009	11.977	0.069	0.069	0.000	0.000	0.000	0.000
160	A	211	GLY	0	-0.016	-0.003	9.702	0.106	0.106	0.000	0.000	0.000	0.000
161	A	212	ASP	-1	-0.768	-0.876	7.025	-0.106	-0.106	0.000	0.000	0.000	0.000
162	A	213	PRO	0	0.024	0.028	8.585	0.122	0.122	0.000	0.000	0.000	0.000
163	A	214	PHE	0	-0.006	0.007	9.900	0.051	0.051	0.000	0.000	0.000	0.000
164	A	215	ARG	1	0.779	0.864	11.846	0.096	0.096	0.000	0.000	0.000	0.000
165	A	216	SER	0	0.057	0.039	14.622	0.052	0.052	0.000	0.000	0.000	0.000
166	A	217	ASP	-1	-0.830	-0.911	12.954	0.195	0.195	0.000	0.000	0.000	0.000
167	A	218	SER	0	0.015	-0.003	13.791	-0.026	-0.026	0.000	0.000	0.000	0.000
168	A	219	TYR	0	-0.040	-0.019	14.887	-0.028	-0.028	0.000	0.000	0.000	0.000
169	A	220	GLY	0	0.022	0.018	17.622	-0.019	-0.019	0.000	0.000	0.000	0.000
170	A	221	LEU	0	-0.029	-0.020	11.970	-0.027	-0.027	0.000	0.000	0.000	0.000
171	A	222	LEU	0	-0.019	-0.004	16.652	-0.019	-0.019	0.000	0.000	0.000	0.000
172	A	223	GLY	0	0.023	0.016	19.387	-0.009	-0.009	0.000	0.000	0.000	0.000
173	A	224	ASN	0	0.002	-0.013	18.558	-0.018	-0.018	0.000	0.000	0.000	0.000
174	A	225	TYR	0	-0.093	-0.072	17.550	-0.007	-0.007	0.000	0.000	0.000	0.000
175	A	226	VAL	0	-0.026	-0.013	20.722	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	227	ASP	-1	-0.888	-0.944	24.009	-0.028	-0.028	0.000	0.000	0.000	0.000
177	A	228	ALA	0	-0.044	-0.015	22.594	-0.003	-0.003	0.000	0.000	0.000	0.000
178	A	229	LEU	0	-0.104	-0.047	24.567	-0.006	-0.006	0.000	0.000	0.000	0.000
179	A	230	TYR	0	-0.079	-0.043	26.325	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:VAL)