FMO DATABASE

FMODB ID: JLQY9

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	OptH
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	-1861244.74738
FMO2-HF: Nuclear repulsion	1785789.767967
FMO2-HF: Total energy	-75454.979413
FMO2-MP2: Total energy	-75657.202039

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.
-6.038	-1.413	2.072	-1.92	-4.778	-0.012

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 : 0.005 / q_NPA : -0.015

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	0.031	0.017	2.533	-3.772	-1.234	1.078	-1.402	-2.214	-0.013
4	A	14	VAL	0	-0.032	-0.008	4.916	0.663	0.760	-0.001	-0.005	-0.091	0.000
5	A	15	TYR	0	-0.005	-0.009	7.380	-0.049	-0.049	0.000	0.000	0.000	0.000
6	A	16	VAL	0	0.027	0.007	10.914	0.085	0.085	0.000	0.000	0.000	0.000
7	A	17	GLY	0	0.031	0.021	13.898	0.001	0.001	0.000	0.000	0.000	0.000
8	A	18	GLY	0	0.057	0.032	17.574	0.015	0.015	0.000	0.000	0.000	0.000
9	A	19	PHE	0	-0.038	-0.013	20.994	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	20	LEU	0	-0.033	-0.017	21.242	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	21	ALA	0	0.010	-0.005	24.847	0.014	0.014	0.000	0.000	0.000	0.000
12	A	22	ARG	1	0.863	0.924	28.005	0.197	0.197	0.000	0.000	0.000	0.000
13	A	23	TYR	0	-0.038	-0.025	30.855	0.000	0.000	0.000	0.000	0.000	0.000
14	A	24	ASP	-1	-0.971	-0.965	34.186	-0.128	-0.128	0.000	0.000	0.000	0.000
15	A	34	LEU	0	-0.008	-0.025	30.438	0.002	0.002	0.000	0.000	0.000	0.000
16	A	35	PRO	0	0.016	0.019	34.097	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	36	ARG	1	0.867	0.919	33.461	0.147	0.147	0.000	0.000	0.000	0.000
18	A	37	ASP	-1	-0.896	-0.957	35.006	-0.132	-0.132	0.000	0.000	0.000	0.000
19	A	38	VAL	0	-0.007	0.004	34.650	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	39	VAL	0	-0.073	-0.039	29.784	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	40	GLU	-1	-0.878	-0.925	31.797	-0.171	-0.171	0.000	0.000	0.000	0.000
22	A	41	HIS	0	-0.068	-0.044	32.499	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	42	TRP	0	-0.073	-0.029	31.018	0.010	0.010	0.000	0.000	0.000	0.000
24	A	55	VAL	0	0.017	-0.008	20.832	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	56	ALA	0	-0.024	-0.003	17.286	0.008	0.008	0.000	0.000	0.000	0.000
26	A	57	LEU	0	0.023	0.015	18.622	-0.015	-0.015	0.000	0.000	0.000	0.000
27	A	58	PRO	0	0.041	0.034	15.714	-0.062	-0.062	0.000	0.000	0.000	0.000
28	A	59	LEU	0	0.011	-0.012	12.933	0.058	0.058	0.000	0.000	0.000	0.000
29	A	60	ASN	0	-0.008	-0.003	14.070	-0.068	-0.068	0.000	0.000	0.000	0.000
30	A	61	ILE	0	0.007	0.010	13.212	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	62	ASN	0	0.015	-0.021	17.008	0.037	0.037	0.000	0.000	0.000	0.000
32	A	63	HIS	0	-0.041	-0.026	20.237	0.036	0.036	0.000	0.000	0.000	0.000
33	A	64	ASP	-1	-0.748	-0.825	18.981	-0.295	-0.295	0.000	0.000	0.000	0.000
34	A	65	ASP	-1	-0.944	-0.974	18.280	-0.335	-0.335	0.000	0.000	0.000	0.000
35	A	66	THR	0	-0.034	-0.038	18.016	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	67	ALA	0	-0.061	-0.049	14.827	-0.033	-0.033	0.000	0.000	0.000	0.000
37	A	68	VAL	0	0.015	0.002	12.912	-0.046	-0.046	0.000	0.000	0.000	0.000
38	A	69	VAL	0	-0.023	-0.033	9.741	-0.071	-0.071	0.000	0.000	0.000	0.000
39	A	70	GLY	0	0.032	0.013	8.862	-0.400	-0.400	0.000	0.000	0.000	0.000
40	A	71	HIS	0	-0.057	-0.010	10.820	0.297	0.297	0.000	0.000	0.000	0.000
41	A	72	VAL	0	-0.027	-0.007	13.832	-0.076	-0.076	0.000	0.000	0.000	0.000
42	A	73	ALA	0	-0.030	-0.024	14.521	0.007	0.007	0.000	0.000	0.000	0.000
43	A	74	ALA	0	-0.043	-0.029	16.385	0.060	0.060	0.000	0.000	0.000	0.000
44	A	75	MET	0	-0.009	-0.007	19.952	-0.022	-0.022	0.000	0.000	0.000	0.000
45	A	76	GLN	0	0.057	0.047	23.009	0.011	0.011	0.000	0.000	0.000	0.000
46	A	77	SER	0	0.007	0.045	25.789	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	78	VAL	0	0.025	0.006	27.225	0.009	0.009	0.000	0.000	0.000	0.000
48	A	79	ARG	1	0.953	0.979	30.045	0.150	0.150	0.000	0.000	0.000	0.000
49	A	80	ASP	-1	-0.753	-0.866	29.781	-0.164	-0.164	0.000	0.000	0.000	0.000
50	A	81	GLY	0	0.001	-0.023	29.692	0.000	0.000	0.000	0.000	0.000	0.000
51	A	82	LEU	0	0.009	0.031	25.553	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	83	PHE	0	-0.002	-0.003	19.957	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	84	CYS	0	-0.043	-0.013	19.377	-0.018	-0.018	0.000	0.000	0.000	0.000
54	A	85	LEU	0	0.024	0.009	14.654	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	86	GLY	0	0.009	0.000	14.406	0.017	0.017	0.000	0.000	0.000	0.000
56	A	87	CAS	0	-0.035	-0.021	9.643	0.029	0.029	0.000	0.000	0.000	0.000
57	A	88	VAL	0	0.001	0.004	7.150	0.070	0.070	0.000	0.000	0.000	0.000
58	A	89	THR	0	0.007	-0.031	5.286	-0.386	-0.386	0.000	0.000	0.000	0.000
59	A	90	SER	0	-0.028	-0.031	4.150	-1.094	-0.979	-0.001	-0.037	-0.078	0.000
60	A	91	PRO	0	0.022	0.002	2.494	-1.206	-0.156	0.940	-0.419	-1.571	0.001
61	A	92	ARG	1	0.899	0.959	3.693	0.774	0.912	0.001	0.073	-0.212	0.000
62	A	93	PHE	0	0.038	0.024	6.766	0.169	0.169	0.000	0.000	0.000	0.000
63	A	94	LEU	0	0.030	-0.002	3.210	-0.360	0.259	0.056	-0.122	-0.553	0.000
64	A	95	GLU	-1	-0.816	-0.878	5.043	0.472	0.472	0.000	0.000	0.000	0.000
65	A	96	ILE	0	-0.047	-0.025	6.185	0.209	0.209	0.000	0.000	0.000	0.000
66	A	97	VAL	0	0.003	0.004	8.084	0.117	0.117	0.000	0.000	0.000	0.000
67	A	98	ARG	1	0.875	0.921	6.549	-0.066	-0.066	0.000	0.000	0.000	0.000
68	A	99	ARG	1	0.897	0.969	8.659	0.064	0.064	0.000	0.000	0.000	0.000
69	A	100	ALA	0	0.015	0.007	11.509	0.047	0.047	0.000	0.000	0.000	0.000
70	A	101	SER	0	-0.045	-0.027	11.280	0.027	0.027	0.000	0.000	0.000	0.000
71	A	102	GLU	-1	-0.998	-1.010	11.778	0.076	0.076	0.000	0.000	0.000	0.000
72	A	103	LYS	1	0.797	0.901	14.691	0.076	0.076	0.000	0.000	0.000	0.000
73	A	104	SER	0	0.010	0.013	17.002	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	105	GLU	-1	-0.888	-0.951	19.093	-0.078	-0.078	0.000	0.000	0.000	0.000
75	A	106	LEU	0	-0.047	-0.022	18.238	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	107	VAL	0	-0.010	0.005	14.822	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	108	SER	0	-0.019	0.006	17.984	0.030	0.030	0.000	0.000	0.000	0.000
78	A	109	ARG	1	0.908	0.948	18.634	0.043	0.043	0.000	0.000	0.000	0.000
79	A	110	GLY	0	0.027	0.022	19.703	0.000	0.000	0.000	0.000	0.000	0.000
80	A	111	PRO	0	-0.021	-0.015	17.533	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	112	VAL	0	0.056	0.026	13.916	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	113	SER	0	0.005	0.000	16.478	0.020	0.020	0.000	0.000	0.000	0.000
83	A	114	PRO	0	0.022	-0.016	15.685	-0.025	-0.025	0.000	0.000	0.000	0.000
84	A	115	LEU	0	-0.033	-0.011	16.763	-0.020	-0.020	0.000	0.000	0.000	0.000
85	A	116	GLN	0	-0.009	0.009	17.324	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	117	PRO	0	-0.043	-0.011	14.147	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	118	ASP	-1	-0.742	-0.868	9.350	-0.564	-0.564	0.000	0.000	0.000	0.000
88	A	119	LYS	1	0.998	0.988	11.509	0.046	0.046	0.000	0.000	0.000	0.000
89	A	120	VAL	0	0.007	0.010	6.815	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	121	VAL	0	0.010	0.006	9.344	-0.061	-0.061	0.000	0.000	0.000	0.000
91	A	122	GLU	-1	-0.843	-0.926	11.181	-0.200	-0.200	0.000	0.000	0.000	0.000
92	A	123	PHE	0	0.018	0.005	12.395	0.023	0.023	0.000	0.000	0.000	0.000
93	A	124	LEU	0	-0.017	0.002	8.852	0.017	0.017	0.000	0.000	0.000	0.000
94	A	125	SER	0	-0.031	-0.030	13.354	0.021	0.021	0.000	0.000	0.000	0.000
95	A	126	GLY	0	-0.011	0.008	16.177	0.039	0.039	0.000	0.000	0.000	0.000
96	A	127	SER	0	-0.084	-0.042	15.202	0.012	0.012	0.000	0.000	0.000	0.000
97	A	128	TYR	0	0.052	0.010	13.761	0.036	0.036	0.000	0.000	0.000	0.000
98	A	129	ALA	0	0.050	0.043	17.277	-0.032	-0.032	0.000	0.000	0.000	0.000
99	A	130	GLY	0	0.014	0.007	19.689	0.017	0.017	0.000	0.000	0.000	0.000
100	A	131	LEU	0	0.021	0.026	17.022	-0.036	-0.036	0.000	0.000	0.000	0.000
101	A	132	SER	0	-0.033	-0.017	20.640	0.043	0.043	0.000	0.000	0.000	0.000
102	A	133	LEU	0	0.038	0.022	22.352	-0.027	-0.027	0.000	0.000	0.000	0.000
103	A	134	SER	0	-0.006	-0.001	23.783	0.023	0.023	0.000	0.000	0.000	0.000
104	A	155	PHE	0	0.027	-0.003	24.538	0.001	0.001	0.000	0.000	0.000	0.000
105	A	156	LYS	1	0.949	0.996	23.879	0.255	0.255	0.000	0.000	0.000	0.000
106	A	157	HIS	0	0.042	-0.001	19.490	-0.010	-0.010	0.000	0.000	0.000	0.000
107	A	158	VAL	0	0.010	0.011	18.408	0.037	0.037	0.000	0.000	0.000	0.000
108	A	159	ALA	0	-0.015	0.007	18.074	-0.049	-0.049	0.000	0.000	0.000	0.000
109	A	160	LEU	0	-0.014	-0.004	12.643	0.019	0.019	0.000	0.000	0.000	0.000
110	A	161	CAS	0	-0.033	-0.025	17.320	0.024	0.024	0.000	0.000	0.000	0.000
111	A	162	SER	0	0.026	0.012	19.564	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	163	VAL	0	0.003	0.003	21.022	0.024	0.024	0.000	0.000	0.000	0.000
113	A	164	GLY	0	0.027	0.040	24.769	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	165	ARG	1	0.879	0.932	25.040	0.243	0.243	0.000	0.000	0.000	0.000
115	A	166	ARG	1	0.903	0.932	27.943	0.165	0.165	0.000	0.000	0.000	0.000
116	A	167	ARG	1	0.925	0.952	21.209	0.239	0.239	0.000	0.000	0.000	0.000
117	A	168	GLY	0	0.037	0.023	22.787	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	169	THR	0	-0.004	-0.025	23.056	0.020	0.020	0.000	0.000	0.000	0.000
119	A	170	LEU	0	-0.035	0.018	21.654	0.005	0.005	0.000	0.000	0.000	0.000
120	A	171	ALA	0	-0.003	0.012	17.489	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	172	VAL	0	-0.009	-0.001	16.542	0.011	0.011	0.000	0.000	0.000	0.000
122	A	173	TYR	0	0.013	-0.026	11.497	-0.086	-0.086	0.000	0.000	0.000	0.000
123	A	174	GLY	0	0.026	-0.001	11.861	0.109	0.109	0.000	0.000	0.000	0.000
124	A	175	ARG	1	0.810	0.905	4.018	1.260	1.328	-0.001	-0.008	-0.059	0.000
125	A	176	ASP	-1	-0.823	-0.918	9.814	-0.531	-0.531	0.000	0.000	0.000	0.000
126	A	177	PRO	0	0.030	0.019	12.387	0.043	0.043	0.000	0.000	0.000	0.000
127	A	178	GLU	-1	-0.796	-0.879	14.956	-0.248	-0.248	0.000	0.000	0.000	0.000
128	A	179	TRP	0	-0.004	-0.001	15.409	0.023	0.023	0.000	0.000	0.000	0.000
129	A	180	VAL	0	0.004	-0.005	13.919	0.035	0.035	0.000	0.000	0.000	0.000
130	A	181	THR	0	0.019	0.006	16.944	0.043	0.043	0.000	0.000	0.000	0.000
131	A	182	GLN	0	-0.078	-0.038	20.048	0.039	0.039	0.000	0.000	0.000	0.000
132	A	183	ARG	1	0.859	0.945	19.006	0.298	0.298	0.000	0.000	0.000	0.000
133	A	184	PHE	0	-0.033	-0.015	19.620	0.014	0.014	0.000	0.000	0.000	0.000
134	A	185	PRO	0	-0.033	-0.024	24.194	0.005	0.005	0.000	0.000	0.000	0.000
135	A	186	ASP	-1	-0.927	-0.951	27.649	-0.175	-0.175	0.000	0.000	0.000	0.000
136	A	187	LEU	0	-0.021	-0.005	23.175	0.009	0.009	0.000	0.000	0.000	0.000
137	A	188	THR	0	0.000	0.003	27.312	0.008	0.008	0.000	0.000	0.000	0.000
138	A	189	ALA	0	-0.023	-0.025	27.479	-0.014	-0.014	0.000	0.000	0.000	0.000
139	A	190	ALA	0	0.086	0.043	27.475	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	191	ASP	-1	-0.800	-0.901	26.638	-0.203	-0.203	0.000	0.000	0.000	0.000
141	A	192	ARG	1	0.912	0.942	23.376	0.178	0.178	0.000	0.000	0.000	0.000
142	A	193	ASP	-1	-0.876	-0.950	23.300	-0.207	-0.207	0.000	0.000	0.000	0.000
143	A	194	GLY	0	-0.023	-0.012	24.768	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	195	LEU	0	-0.045	-0.024	20.749	-0.015	-0.015	0.000	0.000	0.000	0.000
145	A	196	ARG	1	0.817	0.903	19.846	0.214	0.214	0.000	0.000	0.000	0.000
146	A	197	ALA	0	0.004	0.002	19.918	-0.019	-0.019	0.000	0.000	0.000	0.000
147	A	198	GLN	0	-0.089	-0.051	20.549	-0.015	-0.015	0.000	0.000	0.000	0.000
148	A	199	TRP	0	0.110	0.041	15.364	-0.029	-0.029	0.000	0.000	0.000	0.000
149	A	200	GLN	0	-0.026	-0.018	15.432	-0.034	-0.034	0.000	0.000	0.000	0.000
150	A	201	ARG	1	0.958	0.985	16.671	0.302	0.302	0.000	0.000	0.000	0.000
151	A	202	CAS	0	-0.034	0.004	12.361	0.001	0.001	0.000	0.000	0.000	0.000
152	A	203	GLY	0	-0.007	0.014	12.257	-0.055	-0.055	0.000	0.000	0.000	0.000
153	A	204	SER	0	-0.065	-0.029	13.337	0.075	0.075	0.000	0.000	0.000	0.000
154	A	205	THR	0	-0.023	-0.023	14.100	0.053	0.053	0.000	0.000	0.000	0.000
155	A	206	ALA	0	-0.027	-0.014	13.053	-0.062	-0.062	0.000	0.000	0.000	0.000
156	A	207	VAL	0	0.031	0.009	9.373	0.027	0.027	0.000	0.000	0.000	0.000
157	A	208	ASP	-1	-0.819	-0.923	8.193	-1.688	-1.688	0.000	0.000	0.000	0.000
158	A	209	ALA	0	0.020	0.024	10.047	0.082	0.082	0.000	0.000	0.000	0.000
159	A	210	SER	0	-0.051	-0.025	12.144	0.079	0.079	0.000	0.000	0.000	0.000
160	A	211	GLY	0	-0.019	-0.013	9.753	0.080	0.080	0.000	0.000	0.000	0.000
161	A	212	ASP	-1	-0.752	-0.859	7.451	-1.305	-1.305	0.000	0.000	0.000	0.000
162	A	213	PRO	0	0.021	0.039	8.902	0.227	0.227	0.000	0.000	0.000	0.000
163	A	214	PHE	0	0.007	0.013	10.193	0.115	0.115	0.000	0.000	0.000	0.000
164	A	215	ARG	1	0.744	0.834	11.978	0.505	0.505	0.000	0.000	0.000	0.000
165	A	216	SER	0	0.098	0.066	13.784	0.064	0.064	0.000	0.000	0.000	0.000
166	A	217	ASP	-1	-0.848	-0.940	13.230	-0.200	-0.200	0.000	0.000	0.000	0.000
167	A	218	SER	0	0.003	-0.016	14.043	-0.013	-0.013	0.000	0.000	0.000	0.000
168	A	219	TYR	0	-0.042	-0.015	15.129	0.002	0.002	0.000	0.000	0.000	0.000
169	A	220	GLY	0	0.052	0.027	17.737	0.005	0.005	0.000	0.000	0.000	0.000
170	A	221	LEU	0	-0.021	-0.010	12.396	-0.013	-0.013	0.000	0.000	0.000	0.000
171	A	222	LEU	0	-0.013	0.010	17.113	0.002	0.002	0.000	0.000	0.000	0.000
172	A	223	GLY	0	0.021	0.013	19.875	0.009	0.009	0.000	0.000	0.000	0.000
173	A	224	ASN	0	0.025	0.021	18.987	0.000	0.000	0.000	0.000	0.000	0.000
174	A	225	TYR	0	-0.087	-0.067	18.397	0.015	0.015	0.000	0.000	0.000	0.000
175	A	226	VAL	0	-0.042	-0.026	21.254	0.011	0.011	0.000	0.000	0.000	0.000
176	A	227	ASP	-1	-0.899	-0.952	24.275	-0.173	-0.173	0.000	0.000	0.000	0.000
177	A	228	ALA	0	-0.058	-0.025	23.165	0.006	0.006	0.000	0.000	0.000	0.000
178	A	229	LEU	0	-0.109	-0.051	25.110	0.008	0.008	0.000	0.000	0.000	0.000
179	A	230	TYR	0	-0.049	-0.014	26.705	0.020	0.020	0.000	0.000	0.000	0.000

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