FMO DATABASE

FMODB ID: 39JZL

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	OptHSide
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	-1862399.255144
FMO2-HF: Nuclear repulsion	1786943.495787
FMO2-HF: Total energy	-75455.759357
FMO2-MP2: Total energy	-75657.95852

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.
-6.996	-1.325	2.111	-2.559	-5.226	-0.004

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 : 0.011 / q_NPA : 0.003

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	0.039	0.017	2.680	-3.787	-0.151	0.597	-1.925	-2.308	-0.006
4	A	14	VAL	0	-0.047	-0.018	5.052	0.526	0.618	-0.001	-0.005	-0.086	0.000
5	A	15	TYR	0	0.004	-0.009	7.494	-0.056	-0.056	0.000	0.000	0.000	0.000
6	A	16	VAL	0	0.027	0.005	11.036	0.097	0.097	0.000	0.000	0.000	0.000
7	A	17	GLY	0	0.035	0.026	13.999	-0.014	-0.014	0.000	0.000	0.000	0.000
8	A	18	GLY	0	0.053	0.032	17.682	0.025	0.025	0.000	0.000	0.000	0.000
9	A	19	PHE	0	-0.044	-0.016	21.092	-0.010	-0.010	0.000	0.000	0.000	0.000
10	A	20	LEU	0	-0.028	-0.016	21.324	0.003	0.003	0.000	0.000	0.000	0.000
11	A	21	ALA	0	0.007	-0.007	24.926	0.016	0.016	0.000	0.000	0.000	0.000
12	A	22	ARG	1	0.832	0.924	28.180	0.163	0.163	0.000	0.000	0.000	0.000
13	A	23	TYR	0	-0.013	-0.021	30.946	0.001	0.001	0.000	0.000	0.000	0.000
14	A	24	ASP	-1	-0.966	-0.962	34.282	-0.114	-0.114	0.000	0.000	0.000	0.000
15	A	34	LEU	0	-0.017	-0.027	30.605	0.003	0.003	0.000	0.000	0.000	0.000
16	A	35	PRO	0	0.031	0.021	34.175	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	36	ARG	1	0.845	0.919	33.558	0.140	0.140	0.000	0.000	0.000	0.000
18	A	37	ASP	-1	-0.895	-0.956	35.108	-0.121	-0.121	0.000	0.000	0.000	0.000
19	A	38	VAL	0	-0.003	0.004	34.732	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	39	VAL	0	-0.080	-0.044	29.861	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	40	GLU	-1	-0.848	-0.900	31.893	-0.161	-0.161	0.000	0.000	0.000	0.000
22	A	41	HIS	0	-0.057	-0.036	32.606	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	42	TRP	0	-0.088	-0.049	31.188	0.006	0.006	0.000	0.000	0.000	0.000
24	A	55	VAL	0	0.010	-0.013	20.682	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	56	ALA	0	-0.026	-0.001	17.256	0.011	0.011	0.000	0.000	0.000	0.000
26	A	57	LEU	0	0.020	0.017	18.460	0.000	0.000	0.000	0.000	0.000	0.000
27	A	58	PRO	0	0.051	0.035	15.804	-0.058	-0.058	0.000	0.000	0.000	0.000
28	A	59	LEU	0	0.002	-0.009	12.932	0.042	0.042	0.000	0.000	0.000	0.000
29	A	60	ASN	0	-0.003	-0.011	14.157	-0.035	-0.035	0.000	0.000	0.000	0.000
30	A	61	ILE	0	-0.010	0.005	12.970	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	62	ASN	0	0.022	-0.012	16.898	0.019	0.019	0.000	0.000	0.000	0.000
32	A	63	HIS	0	-0.031	-0.014	20.365	0.023	0.023	0.000	0.000	0.000	0.000
33	A	64	ASP	-1	-0.737	-0.815	19.029	-0.091	-0.091	0.000	0.000	0.000	0.000
34	A	65	ASP	-1	-0.960	-0.978	18.327	-0.142	-0.142	0.000	0.000	0.000	0.000
35	A	66	THR	0	-0.032	-0.033	18.005	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	67	ALA	0	-0.045	-0.044	14.841	0.015	0.015	0.000	0.000	0.000	0.000
37	A	68	VAL	0	0.013	0.004	12.917	-0.051	-0.051	0.000	0.000	0.000	0.000
38	A	69	VAL	0	-0.033	-0.036	9.866	0.000	0.000	0.000	0.000	0.000	0.000
39	A	70	GLY	0	0.036	0.017	8.955	-0.296	-0.296	0.000	0.000	0.000	0.000
40	A	71	HIS	0	-0.060	-0.021	10.919	0.233	0.233	0.000	0.000	0.000	0.000
41	A	72	VAL	0	-0.026	-0.012	13.964	-0.077	-0.077	0.000	0.000	0.000	0.000
42	A	73	ALA	0	-0.037	-0.029	14.551	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	74	ALA	0	-0.024	-0.016	16.502	0.041	0.041	0.000	0.000	0.000	0.000
44	A	75	MET	0	-0.019	-0.015	20.096	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	76	GLN	0	0.049	0.037	23.119	0.003	0.003	0.000	0.000	0.000	0.000
46	A	77	SER	0	0.006	0.035	25.909	0.004	0.004	0.000	0.000	0.000	0.000
47	A	78	VAL	0	0.027	-0.005	27.256	0.004	0.004	0.000	0.000	0.000	0.000
48	A	79	ARG	1	0.873	0.928	30.168	0.159	0.159	0.000	0.000	0.000	0.000
49	A	80	ASP	-1	-0.728	-0.847	29.987	-0.150	-0.150	0.000	0.000	0.000	0.000
50	A	81	GLY	0	0.035	0.005	29.819	0.005	0.005	0.000	0.000	0.000	0.000
51	A	82	LEU	0	-0.005	0.028	25.680	-0.008	-0.008	0.000	0.000	0.000	0.000
52	A	83	PHE	0	-0.005	-0.006	20.288	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	84	CYS	0	-0.049	-0.012	19.809	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	85	LEU	0	0.025	0.007	14.823	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	86	GLY	0	0.017	0.004	14.506	0.007	0.007	0.000	0.000	0.000	0.000
56	A	87	CAS	0	-0.051	-0.024	9.768	0.021	0.021	0.000	0.000	0.000	0.000
57	A	88	VAL	0	0.013	0.003	7.816	0.081	0.081	0.000	0.000	0.000	0.000
58	A	89	THR	0	-0.004	-0.053	5.434	-0.338	-0.338	0.000	0.000	0.000	0.000
59	A	90	SER	0	-0.025	-0.025	4.218	-0.751	-0.648	-0.001	-0.029	-0.074	0.000
60	A	91	PRO	0	0.024	0.004	2.411	-1.181	-0.094	0.942	-0.412	-1.618	0.002
61	A	92	ARG	1	0.886	0.949	3.809	-0.169	0.003	0.001	0.040	-0.214	0.000
62	A	93	PHE	0	0.033	0.018	6.837	0.037	0.037	0.000	0.000	0.000	0.000
63	A	94	LEU	0	0.024	-0.003	2.466	-0.517	0.013	0.574	-0.224	-0.879	0.000
64	A	95	GLU	-1	-0.797	-0.870	5.057	1.005	1.005	0.000	0.000	0.000	0.000
65	A	96	ILE	0	-0.048	-0.026	6.026	0.023	0.023	0.000	0.000	0.000	0.000
66	A	97	VAL	0	0.008	0.005	7.993	0.020	0.020	0.000	0.000	0.000	0.000
67	A	98	ARG	1	0.805	0.883	6.525	-0.611	-0.611	0.000	0.000	0.000	0.000
68	A	99	ARG	1	0.871	0.942	8.652	-0.498	-0.498	0.000	0.000	0.000	0.000
69	A	100	ALA	0	0.030	0.020	11.453	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	101	SER	0	-0.036	-0.020	11.299	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	102	GLU	-1	-0.899	-0.944	11.716	0.325	0.325	0.000	0.000	0.000	0.000
72	A	103	LYS	1	0.787	0.887	14.584	-0.193	-0.193	0.000	0.000	0.000	0.000
73	A	104	SER	0	0.018	0.015	16.788	-0.022	-0.022	0.000	0.000	0.000	0.000
74	A	105	GLU	-1	-0.782	-0.870	19.107	0.027	0.027	0.000	0.000	0.000	0.000
75	A	106	LEU	0	-0.037	-0.014	18.238	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	107	VAL	0	-0.043	-0.003	14.792	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	108	SER	0	-0.014	-0.011	18.079	0.023	0.023	0.000	0.000	0.000	0.000
78	A	109	ARG	1	0.817	0.873	18.644	-0.042	-0.042	0.000	0.000	0.000	0.000
79	A	110	GLY	0	0.022	0.025	19.712	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	111	PRO	0	-0.002	-0.007	17.506	0.000	0.000	0.000	0.000	0.000	0.000
81	A	112	VAL	0	0.052	0.025	14.038	-0.015	-0.015	0.000	0.000	0.000	0.000
82	A	113	SER	0	-0.009	-0.001	16.538	0.007	0.007	0.000	0.000	0.000	0.000
83	A	114	PRO	0	0.036	-0.014	15.835	-0.016	-0.016	0.000	0.000	0.000	0.000
84	A	115	LEU	0	-0.030	-0.006	16.910	-0.032	-0.032	0.000	0.000	0.000	0.000
85	A	116	GLN	0	-0.052	-0.015	17.201	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	117	PRO	0	-0.018	-0.005	14.239	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	118	ASP	-1	-0.744	-0.859	9.284	-0.369	-0.369	0.000	0.000	0.000	0.000
88	A	119	LYS	1	0.893	0.929	11.709	0.010	0.010	0.000	0.000	0.000	0.000
89	A	120	VAL	0	0.021	0.021	6.609	0.002	0.002	0.000	0.000	0.000	0.000
90	A	121	VAL	0	-0.001	0.004	9.311	-0.050	-0.050	0.000	0.000	0.000	0.000
91	A	122	GLU	-1	-0.772	-0.872	11.237	-0.093	-0.093	0.000	0.000	0.000	0.000
92	A	123	PHE	0	0.034	0.012	12.439	0.016	0.016	0.000	0.000	0.000	0.000
93	A	124	LEU	0	-0.012	0.009	8.881	0.011	0.011	0.000	0.000	0.000	0.000
94	A	125	SER	0	-0.035	-0.029	13.372	0.000	0.000	0.000	0.000	0.000	0.000
95	A	126	GLY	0	-0.006	0.008	16.221	0.021	0.021	0.000	0.000	0.000	0.000
96	A	127	SER	0	-0.084	-0.037	15.111	0.008	0.008	0.000	0.000	0.000	0.000
97	A	128	TYR	0	0.059	0.016	13.984	0.021	0.021	0.000	0.000	0.000	0.000
98	A	129	ALA	0	0.048	0.039	17.314	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	130	GLY	0	0.014	0.007	19.728	0.002	0.002	0.000	0.000	0.000	0.000
100	A	131	LEU	0	0.023	0.026	17.036	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	132	SER	0	-0.023	-0.012	20.695	0.027	0.027	0.000	0.000	0.000	0.000
102	A	133	LEU	0	0.047	0.027	22.392	-0.018	-0.018	0.000	0.000	0.000	0.000
103	A	134	SER	0	-0.007	0.000	24.086	0.020	0.020	0.000	0.000	0.000	0.000
104	A	155	PHE	0	0.012	-0.011	24.724	0.003	0.003	0.000	0.000	0.000	0.000
105	A	156	LYS	1	0.967	1.004	23.729	0.162	0.162	0.000	0.000	0.000	0.000
106	A	157	HIS	0	0.033	-0.010	19.601	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	158	VAL	0	-0.009	0.002	18.569	0.025	0.025	0.000	0.000	0.000	0.000
108	A	159	ALA	0	-0.006	0.016	18.187	-0.029	-0.029	0.000	0.000	0.000	0.000
109	A	160	LEU	0	-0.012	-0.006	12.680	0.004	0.004	0.000	0.000	0.000	0.000
110	A	161	CAS	0	-0.042	-0.028	17.346	0.035	0.035	0.000	0.000	0.000	0.000
111	A	162	SER	0	0.044	0.021	19.434	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	163	VAL	0	-0.037	-0.020	20.956	0.016	0.016	0.000	0.000	0.000	0.000
113	A	164	GLY	0	0.054	0.049	24.751	-0.010	-0.010	0.000	0.000	0.000	0.000
114	A	165	ARG	1	0.887	0.945	24.879	0.166	0.166	0.000	0.000	0.000	0.000
115	A	166	ARG	1	0.917	0.937	27.870	0.093	0.093	0.000	0.000	0.000	0.000
116	A	167	ARG	1	0.907	0.943	21.109	0.110	0.110	0.000	0.000	0.000	0.000
117	A	168	GLY	0	0.041	0.023	22.913	-0.012	-0.012	0.000	0.000	0.000	0.000
118	A	169	THR	0	-0.013	-0.025	23.201	0.013	0.013	0.000	0.000	0.000	0.000
119	A	170	LEU	0	-0.036	0.014	21.807	0.000	0.000	0.000	0.000	0.000	0.000
120	A	171	ALA	0	-0.003	0.015	17.488	-0.012	-0.012	0.000	0.000	0.000	0.000
121	A	172	VAL	0	-0.009	-0.005	16.776	0.016	0.016	0.000	0.000	0.000	0.000
122	A	173	TYR	0	0.015	-0.019	11.513	-0.073	-0.073	0.000	0.000	0.000	0.000
123	A	174	GLY	0	0.018	-0.006	11.975	0.089	0.089	0.000	0.000	0.000	0.000
124	A	175	ARG	1	0.810	0.889	4.235	0.850	0.901	-0.001	-0.004	-0.047	0.000
125	A	176	ASP	-1	-0.784	-0.899	9.955	-0.724	-0.724	0.000	0.000	0.000	0.000
126	A	177	PRO	0	0.037	0.028	12.495	0.079	0.079	0.000	0.000	0.000	0.000
127	A	178	GLU	-1	-0.822	-0.872	15.105	-0.313	-0.313	0.000	0.000	0.000	0.000
128	A	179	TRP	0	-0.004	-0.003	15.626	0.044	0.044	0.000	0.000	0.000	0.000
129	A	180	VAL	0	0.004	-0.003	13.967	0.051	0.051	0.000	0.000	0.000	0.000
130	A	181	THR	0	0.008	-0.017	17.077	0.048	0.048	0.000	0.000	0.000	0.000
131	A	182	GLN	0	-0.069	-0.030	20.186	0.049	0.049	0.000	0.000	0.000	0.000
132	A	183	ARG	1	0.836	0.932	19.161	0.315	0.315	0.000	0.000	0.000	0.000
133	A	184	PHE	0	-0.031	-0.015	19.529	0.023	0.023	0.000	0.000	0.000	0.000
134	A	185	PRO	0	-0.027	-0.021	24.318	0.000	0.000	0.000	0.000	0.000	0.000
135	A	186	ASP	-1	-0.903	-0.946	27.778	-0.171	-0.171	0.000	0.000	0.000	0.000
136	A	187	LEU	0	0.000	0.009	23.417	0.006	0.006	0.000	0.000	0.000	0.000
137	A	188	THR	0	0.002	-0.014	27.448	0.002	0.002	0.000	0.000	0.000	0.000
138	A	189	ALA	0	-0.004	-0.016	27.630	-0.016	-0.016	0.000	0.000	0.000	0.000
139	A	190	ALA	0	0.080	0.041	27.626	-0.015	-0.015	0.000	0.000	0.000	0.000
140	A	191	ASP	-1	-0.798	-0.874	26.913	-0.215	-0.215	0.000	0.000	0.000	0.000
141	A	192	ARG	1	0.864	0.912	23.551	0.213	0.213	0.000	0.000	0.000	0.000
142	A	193	ASP	-1	-0.850	-0.929	23.448	-0.287	-0.287	0.000	0.000	0.000	0.000
143	A	194	GLY	0	-0.010	0.005	25.179	-0.011	-0.011	0.000	0.000	0.000	0.000
144	A	195	LEU	0	-0.041	-0.034	20.827	-0.016	-0.016	0.000	0.000	0.000	0.000
145	A	196	ARG	1	0.790	0.873	20.303	0.294	0.294	0.000	0.000	0.000	0.000
146	A	197	ALA	0	0.015	0.008	20.345	-0.032	-0.032	0.000	0.000	0.000	0.000
147	A	198	GLN	0	-0.073	-0.036	20.761	-0.018	-0.018	0.000	0.000	0.000	0.000
148	A	199	TRP	0	0.106	0.039	15.691	-0.047	-0.047	0.000	0.000	0.000	0.000
149	A	200	GLN	0	-0.012	-0.010	15.818	-0.053	-0.053	0.000	0.000	0.000	0.000
150	A	201	ARG	1	0.927	0.969	17.068	0.338	0.338	0.000	0.000	0.000	0.000
151	A	202	CAS	0	-0.041	-0.007	12.711	0.001	0.001	0.000	0.000	0.000	0.000
152	A	203	GLY	0	-0.003	0.020	12.588	-0.088	-0.088	0.000	0.000	0.000	0.000
153	A	204	SER	0	-0.036	-0.018	13.675	0.021	0.021	0.000	0.000	0.000	0.000
154	A	205	THR	0	-0.054	-0.034	14.446	0.101	0.101	0.000	0.000	0.000	0.000
155	A	206	ALA	0	-0.023	-0.011	13.277	-0.090	-0.090	0.000	0.000	0.000	0.000
156	A	207	VAL	0	0.031	0.007	9.451	0.058	0.058	0.000	0.000	0.000	0.000
157	A	208	ASP	-1	-0.797	-0.875	7.908	-1.305	-1.305	0.000	0.000	0.000	0.000
158	A	209	ALA	0	0.024	0.026	9.765	0.119	0.119	0.000	0.000	0.000	0.000
159	A	210	SER	0	-0.040	-0.017	11.978	0.079	0.079	0.000	0.000	0.000	0.000
160	A	211	GLY	0	-0.017	-0.014	9.755	0.101	0.101	0.000	0.000	0.000	0.000
161	A	212	ASP	-1	-0.763	-0.875	7.587	-0.251	-0.251	0.000	0.000	0.000	0.000
162	A	213	PRO	0	0.026	0.028	8.945	0.142	0.142	0.000	0.000	0.000	0.000
163	A	214	PHE	0	0.010	0.013	10.266	0.049	0.049	0.000	0.000	0.000	0.000
164	A	215	ARG	1	0.747	0.853	11.965	0.141	0.141	0.000	0.000	0.000	0.000
165	A	216	SER	0	0.101	0.063	13.861	0.025	0.025	0.000	0.000	0.000	0.000
166	A	217	ASP	-1	-0.847	-0.928	13.292	0.163	0.163	0.000	0.000	0.000	0.000
167	A	218	SER	0	0.014	-0.008	14.019	-0.024	-0.024	0.000	0.000	0.000	0.000
168	A	219	TYR	0	-0.040	-0.019	15.101	-0.026	-0.026	0.000	0.000	0.000	0.000
169	A	220	GLY	0	0.041	0.026	17.795	-0.017	-0.017	0.000	0.000	0.000	0.000
170	A	221	LEU	0	-0.020	-0.009	12.221	-0.025	-0.025	0.000	0.000	0.000	0.000
171	A	222	LEU	0	-0.010	0.009	16.921	-0.018	-0.018	0.000	0.000	0.000	0.000
172	A	223	GLY	0	0.020	0.015	19.702	-0.008	-0.008	0.000	0.000	0.000	0.000
173	A	224	ASN	0	0.009	-0.007	18.796	-0.016	-0.016	0.000	0.000	0.000	0.000
174	A	225	TYR	0	-0.109	-0.085	18.054	-0.006	-0.006	0.000	0.000	0.000	0.000
175	A	226	VAL	0	-0.033	-0.021	21.107	-0.004	-0.004	0.000	0.000	0.000	0.000
176	A	227	ASP	-1	-0.889	-0.944	24.184	-0.045	-0.045	0.000	0.000	0.000	0.000
177	A	228	ALA	0	-0.049	-0.024	23.018	-0.003	-0.003	0.000	0.000	0.000	0.000
178	A	229	LEU	0	-0.110	-0.056	24.966	-0.002	-0.002	0.000	0.000	0.000	0.000
179	A	230	TYR	0	-0.076	-0.025	26.584	0.006	0.006	0.000	0.000	0.000	0.000

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