FMO DATABASE

FMODB ID: R98L8

Calculation Name: 1LAY-A-Xray372

Preferred Name: Human herpes virus 5 capsid protein P40

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1LAY

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:

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	206
LigandCharge	DGL=-1,DAR=1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2357942.274569
FMO2-HF: Nuclear repulsion	2278313.23632
FMO2-HF: Total energy	-79629.03825
FMO2-MP2: Total energy	-79861.877113

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:9:GLN)

Summations of interaction energy for fragment #1(A:9:GLN)

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.
-7.054	-2.073	0.759	-2.401	-3.339	-0.005

Interaction energy analysis for fragmet #1(A:9:GLN)

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 : 0.006

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	11	VAL	0	0.010	0.003	2.976	-3.989	-1.342	0.157	-1.178	-1.626	0.008
4	A	12	ALA	0	-0.010	0.006	2.744	-3.280	-1.069	0.602	-1.194	-1.619	-0.013
5	A	13	PRO	0	0.029	-0.004	4.038	0.002	0.125	0.000	-0.029	-0.094	0.000
6	A	14	VAL	0	0.003	0.014	7.807	-0.351	-0.351	0.000	0.000	0.000	0.000
7	A	15	TYR	0	0.002	0.006	10.206	0.214	0.214	0.000	0.000	0.000	0.000
8	A	16	VAL	0	0.027	0.007	13.493	-0.107	-0.107	0.000	0.000	0.000	0.000
9	A	17	GLY	0	0.018	0.009	16.615	0.053	0.053	0.000	0.000	0.000	0.000
10	A	18	GLY	0	0.050	0.016	19.857	-0.029	-0.029	0.000	0.000	0.000	0.000
11	A	19	PHE	0	-0.011	0.018	23.335	0.024	0.024	0.000	0.000	0.000	0.000
12	A	20	LEU	0	0.027	0.020	24.589	0.001	0.001	0.000	0.000	0.000	0.000
13	A	21	ALA	0	-0.053	-0.046	27.957	0.013	0.013	0.000	0.000	0.000	0.000
14	A	22	ARG	1	0.858	0.940	29.104	0.181	0.181	0.000	0.000	0.000	0.000
15	A	23	TYR	0	-0.052	0.002	33.754	0.011	0.011	0.000	0.000	0.000	0.000
16	A	24	ASP	-1	-0.835	-0.893	35.516	-0.116	-0.116	0.000	0.000	0.000	0.000
17	A	56	ALA	0	0.027	0.011	21.923	0.000	0.000	0.000	0.000	0.000	0.000
18	A	57	LEU	0	-0.049	-0.027	22.776	0.011	0.011	0.000	0.000	0.000	0.000
19	A	58	PRO	0	0.033	0.034	20.801	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	59	LEU	0	-0.012	-0.019	16.773	-0.025	-0.025	0.000	0.000	0.000	0.000
21	A	60	ASN	0	-0.003	-0.019	19.123	0.012	0.012	0.000	0.000	0.000	0.000
22	A	61	ILE	0	0.037	0.023	16.852	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	62	ASN	0	-0.022	-0.032	20.829	0.002	0.002	0.000	0.000	0.000	0.000
24	A	63	HIS	0	0.006	-0.002	24.216	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	64	ASP	-1	-0.764	-0.836	23.880	0.080	0.080	0.000	0.000	0.000	0.000
26	A	65	ASP	-1	-0.842	-0.946	23.651	0.044	0.044	0.000	0.000	0.000	0.000
27	A	66	THR	0	-0.072	-0.045	23.535	0.019	0.019	0.000	0.000	0.000	0.000
28	A	67	ALA	0	-0.035	-0.015	19.925	0.031	0.031	0.000	0.000	0.000	0.000
29	A	68	VAL	0	-0.015	-0.015	18.458	-0.028	-0.028	0.000	0.000	0.000	0.000
30	A	69	VAL	0	-0.013	-0.020	14.399	0.036	0.036	0.000	0.000	0.000	0.000
31	A	70	GLY	0	0.022	0.014	13.923	0.010	0.010	0.000	0.000	0.000	0.000
32	A	71	HIS	0	-0.022	0.031	15.048	-0.032	-0.032	0.000	0.000	0.000	0.000
33	A	72	VAL	0	-0.002	-0.011	17.594	-0.036	-0.036	0.000	0.000	0.000	0.000
34	A	73	ALA	0	0.014	-0.008	17.447	0.023	0.023	0.000	0.000	0.000	0.000
35	A	74	ALA	0	0.021	0.008	19.580	0.013	0.013	0.000	0.000	0.000	0.000
36	A	75	MET	0	-0.029	-0.023	22.786	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	76	GLN	0	0.034	0.015	25.768	0.018	0.018	0.000	0.000	0.000	0.000
38	A	77	SER	0	-0.011	0.009	28.483	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	78	VAL	0	-0.003	0.011	27.905	0.004	0.004	0.000	0.000	0.000	0.000
40	A	79	ARG	1	0.864	0.906	31.163	0.173	0.173	0.000	0.000	0.000	0.000
41	A	80	ASP	-1	-0.780	-0.895	31.997	-0.148	-0.148	0.000	0.000	0.000	0.000
42	A	81	GLY	0	0.015	-0.007	31.906	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	82	LEU	0	-0.059	-0.007	28.746	0.002	0.002	0.000	0.000	0.000	0.000
44	A	83	PHE	0	0.008	-0.002	21.635	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	84	CYS	0	-0.017	-0.017	21.728	0.030	0.030	0.000	0.000	0.000	0.000
46	A	85	LEU	0	0.008	0.014	16.931	-0.035	-0.035	0.000	0.000	0.000	0.000
47	A	86	GLY	0	-0.029	-0.023	17.932	0.044	0.044	0.000	0.000	0.000	0.000
48	A	87	CYS	0	-0.044	-0.023	12.760	-0.042	-0.042	0.000	0.000	0.000	0.000
49	A	88	VAL	0	-0.001	0.004	11.321	0.073	0.073	0.000	0.000	0.000	0.000
50	A	89	THR	0	-0.012	-0.030	9.969	-0.059	-0.059	0.000	0.000	0.000	0.000
51	A	90	SER	0	-0.034	-0.035	10.139	0.102	0.102	0.000	0.000	0.000	0.000
52	A	91	PRO	0	0.043	0.016	8.268	-0.015	-0.015	0.000	0.000	0.000	0.000
53	A	92	ARG	1	0.796	0.887	9.446	-0.210	-0.210	0.000	0.000	0.000	0.000
54	A	93	PHE	0	0.032	0.021	12.371	-0.020	-0.020	0.000	0.000	0.000	0.000
55	A	94	LEU	0	0.014	-0.005	6.500	-0.024	-0.024	0.000	0.000	0.000	0.000
56	A	95	GLU	-1	-0.725	-0.837	9.090	1.487	1.487	0.000	0.000	0.000	0.000
57	A	96	ILE	0	-0.062	-0.016	10.039	-0.070	-0.070	0.000	0.000	0.000	0.000
58	A	97	VAL	0	-0.003	-0.020	11.192	-0.052	-0.052	0.000	0.000	0.000	0.000
59	A	98	ARG	1	0.776	0.855	6.467	-1.293	-1.293	0.000	0.000	0.000	0.000
60	A	99	ARG	1	0.856	0.919	10.157	-0.880	-0.880	0.000	0.000	0.000	0.000
61	A	100	ALA	0	0.004	0.012	12.731	-0.084	-0.084	0.000	0.000	0.000	0.000
62	A	101	SER	0	-0.043	-0.028	11.347	-0.127	-0.127	0.000	0.000	0.000	0.000
63	A	102	GLU	-1	-0.852	-0.901	9.606	0.334	0.334	0.000	0.000	0.000	0.000
64	A	103	LYS	1	0.893	0.954	13.639	0.006	0.006	0.000	0.000	0.000	0.000
65	A	104	SER	0	0.015	0.013	16.268	-0.014	-0.014	0.000	0.000	0.000	0.000
66	A	105	GLU	-1	-0.799	-0.880	17.230	-0.325	-0.325	0.000	0.000	0.000	0.000
67	A	106	LEU	0	0.007	-0.003	18.500	-0.049	-0.049	0.000	0.000	0.000	0.000
68	A	107	VAL	0	0.001	-0.010	12.658	-0.054	-0.054	0.000	0.000	0.000	0.000
69	A	108	SER	0	-0.053	-0.040	14.288	-0.140	-0.140	0.000	0.000	0.000	0.000
70	A	109	ARG	1	0.807	0.905	15.870	0.312	0.312	0.000	0.000	0.000	0.000
71	A	110	GLY	0	0.005	0.035	14.239	-0.026	-0.026	0.000	0.000	0.000	0.000
72	A	111	PRO	0	-0.031	-0.033	12.514	0.131	0.131	0.000	0.000	0.000	0.000
73	A	112	VAL	0	0.015	0.017	15.728	0.032	0.032	0.000	0.000	0.000	0.000
74	A	113	SER	0	-0.033	-0.040	17.450	0.071	0.071	0.000	0.000	0.000	0.000
75	A	114	PRO	0	-0.007	0.009	16.100	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	115	LEU	0	-0.028	0.001	12.917	-0.121	-0.121	0.000	0.000	0.000	0.000
77	A	116	GLN	0	0.031	0.018	7.216	-0.379	-0.379	0.000	0.000	0.000	0.000
78	A	117	PRO	0	0.044	0.018	9.591	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	118	ASP	-1	-0.774	-0.835	6.732	-3.709	-3.709	0.000	0.000	0.000	0.000
80	A	119	LYS	1	0.966	0.966	8.087	1.100	1.100	0.000	0.000	0.000	0.000
81	A	120	VAL	0	0.057	0.030	7.539	0.247	0.247	0.000	0.000	0.000	0.000
82	A	121	VAL	0	0.020	0.011	8.620	0.239	0.239	0.000	0.000	0.000	0.000
83	A	122	GLU	-1	-0.804	-0.898	10.795	-0.968	-0.968	0.000	0.000	0.000	0.000
84	A	123	PHE	0	0.016	0.005	12.577	0.127	0.127	0.000	0.000	0.000	0.000
85	A	124	LEU	0	-0.026	0.002	11.631	0.095	0.095	0.000	0.000	0.000	0.000
86	A	125	SER	0	-0.005	-0.021	14.662	0.073	0.073	0.000	0.000	0.000	0.000
87	A	126	GLY	0	-0.016	0.001	17.001	0.037	0.037	0.000	0.000	0.000	0.000
88	A	127	SER	0	-0.083	-0.037	17.809	0.065	0.065	0.000	0.000	0.000	0.000
89	A	128	TYR	0	-0.059	-0.050	17.176	0.040	0.040	0.000	0.000	0.000	0.000
90	A	129	ALA	0	0.055	0.040	20.164	-0.022	-0.022	0.000	0.000	0.000	0.000
91	A	130	GLY	0	0.035	0.021	21.941	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	131	LEU	0	-0.026	0.008	20.548	0.016	0.016	0.000	0.000	0.000	0.000
93	A	132	SER	0	-0.052	-0.041	24.387	0.012	0.012	0.000	0.000	0.000	0.000
94	A	133	LEU	0	0.015	0.017	26.103	0.005	0.005	0.000	0.000	0.000	0.000
95	A	134	SER	0	-0.029	-0.035	28.090	0.001	0.001	0.000	0.000	0.000	0.000
96	A	135	SER	0	0.014	0.008	29.806	0.003	0.003	0.000	0.000	0.000	0.000
97	A	136	ARG	1	0.854	0.903	32.000	-0.031	-0.031	0.000	0.000	0.000	0.000
98	A	137	ARG	1	0.818	0.897	34.524	0.000	0.000	0.000	0.000	0.000	0.000
99	A	138	CYS	0	-0.035	-0.027	37.758	0.003	0.003	0.000	0.000	0.000	0.000
100	A	139	ASP	-1	-0.848	-0.918	39.415	0.006	0.006	0.000	0.000	0.000	0.000
101	A	140	ASP	-1	-0.810	-0.893	34.939	0.009	0.009	0.000	0.000	0.000	0.000
102	A	141	VAL	0	0.034	0.016	35.136	0.002	0.002	0.000	0.000	0.000	0.000
103	A	142	GLU	-1	-0.857	-0.890	33.466	0.046	0.046	0.000	0.000	0.000	0.000
104	A	154	PRO	0	-0.016	-0.020	29.750	0.000	0.000	0.000	0.000	0.000	0.000
105	A	155	PHE	0	-0.027	-0.039	30.415	0.006	0.006	0.000	0.000	0.000	0.000
106	A	156	LYS	1	0.895	0.957	28.795	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	157	HIS	0	0.035	0.047	24.399	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	158	VAL	0	-0.029	-0.015	22.383	-0.013	-0.013	0.000	0.000	0.000	0.000
109	A	159	ALA	0	0.019	0.031	22.339	0.010	0.010	0.000	0.000	0.000	0.000
110	A	160	LEU	0	-0.032	-0.016	16.773	-0.022	-0.022	0.000	0.000	0.000	0.000
111	A	161	CYS	0	-0.007	-0.011	21.261	0.031	0.031	0.000	0.000	0.000	0.000
112	A	162	SER	0	0.031	0.025	23.233	-0.031	-0.031	0.000	0.000	0.000	0.000
113	A	163	VAL	0	0.009	-0.005	24.839	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	164	GLY	0	0.032	0.046	27.002	0.018	0.018	0.000	0.000	0.000	0.000
115	A	165	ARG	1	0.872	0.910	28.264	0.069	0.069	0.000	0.000	0.000	0.000
116	A	166	ARG	1	0.886	0.944	30.597	0.091	0.091	0.000	0.000	0.000	0.000
117	A	167	ARG	1	0.818	0.885	31.087	0.107	0.107	0.000	0.000	0.000	0.000
118	A	168	GLY	0	0.045	0.010	29.401	0.007	0.007	0.000	0.000	0.000	0.000
119	A	169	THR	0	-0.091	-0.039	26.996	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	170	LEU	0	0.006	0.008	22.690	0.005	0.005	0.000	0.000	0.000	0.000
121	A	171	ALA	0	-0.039	-0.004	19.607	0.000	0.000	0.000	0.000	0.000	0.000
122	A	172	VAL	0	0.001	0.002	17.116	-0.038	-0.038	0.000	0.000	0.000	0.000
123	A	173	TYR	0	-0.023	-0.043	13.358	0.044	0.044	0.000	0.000	0.000	0.000
124	A	174	GLY	0	0.034	-0.002	11.731	-0.075	-0.075	0.000	0.000	0.000	0.000
125	A	175	ARG	1	0.744	0.841	6.043	2.395	2.395	0.000	0.000	0.000	0.000
126	A	176	ASP	-1	-0.825	-0.917	9.238	-0.446	-0.446	0.000	0.000	0.000	0.000
127	A	177	PRO	0	0.029	0.027	11.345	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	178	GLU	-1	-0.730	-0.840	14.602	-0.264	-0.264	0.000	0.000	0.000	0.000
129	A	179	TRP	0	-0.035	-0.022	13.091	-0.016	-0.016	0.000	0.000	0.000	0.000
130	A	180	VAL	0	0.005	0.002	14.216	0.010	0.010	0.000	0.000	0.000	0.000
131	A	181	THR	0	-0.033	-0.017	16.607	0.044	0.044	0.000	0.000	0.000	0.000
132	A	182	GLN	0	-0.084	-0.072	18.014	0.065	0.065	0.000	0.000	0.000	0.000
133	A	183	ARG	1	0.772	0.896	16.355	0.658	0.658	0.000	0.000	0.000	0.000
134	A	184	PHE	0	0.008	-0.002	20.321	0.024	0.024	0.000	0.000	0.000	0.000
135	A	185	PRO	0	0.056	0.037	23.787	0.017	0.017	0.000	0.000	0.000	0.000
136	A	186	ASP	-1	-0.863	-0.916	26.767	-0.198	-0.198	0.000	0.000	0.000	0.000
137	A	187	LEU	0	-0.061	-0.027	23.410	0.023	0.023	0.000	0.000	0.000	0.000
138	A	188	THR	0	0.001	0.000	26.334	-0.017	-0.017	0.000	0.000	0.000	0.000
139	A	189	ALA	0	-0.009	-0.019	25.840	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	190	ALA	0	0.083	0.037	26.446	0.004	0.004	0.000	0.000	0.000	0.000
141	A	191	ASP	-1	-0.820	-0.897	27.125	-0.152	-0.152	0.000	0.000	0.000	0.000
142	A	192	ARG	1	0.855	0.903	21.431	0.302	0.302	0.000	0.000	0.000	0.000
143	A	193	ASP	-1	-0.846	-0.897	23.207	-0.144	-0.144	0.000	0.000	0.000	0.000
144	A	194	GLY	0	-0.015	-0.006	25.262	0.016	0.016	0.000	0.000	0.000	0.000
145	A	195	LEU	0	-0.035	-0.021	22.369	0.013	0.013	0.000	0.000	0.000	0.000
146	A	196	ARG	1	0.863	0.891	19.752	0.216	0.216	0.000	0.000	0.000	0.000
147	A	197	ALA	0	0.026	0.011	21.357	0.024	0.024	0.000	0.000	0.000	0.000
148	A	198	GLN	0	-0.078	-0.049	23.352	0.033	0.033	0.000	0.000	0.000	0.000
149	A	199	TRP	0	0.069	0.044	16.789	0.012	0.012	0.000	0.000	0.000	0.000
150	A	200	GLN	0	-0.052	-0.022	18.157	0.022	0.022	0.000	0.000	0.000	0.000
151	A	201	ARG	1	0.875	0.945	19.961	0.019	0.019	0.000	0.000	0.000	0.000
152	A	202	CYS	0	-0.052	0.004	18.572	0.021	0.021	0.000	0.000	0.000	0.000
153	A	203	GLY	0	0.054	0.014	14.611	-0.050	-0.050	0.000	0.000	0.000	0.000
154	A	204	SER	0	-0.032	-0.034	9.201	0.021	0.021	0.000	0.000	0.000	0.000
155	A	205	THR	0	-0.031	-0.018	11.010	-0.051	-0.051	0.000	0.000	0.000	0.000
156	A	206	ALA	0	0.049	0.041	13.430	0.039	0.039	0.000	0.000	0.000	0.000
157	A	207	VAL	0	-0.041	-0.032	15.521	0.046	0.046	0.000	0.000	0.000	0.000
158	A	208	ASP	-1	-0.888	-0.938	17.991	0.279	0.279	0.000	0.000	0.000	0.000
159	A	209	ALA	0	-0.013	0.002	18.100	-0.026	-0.026	0.000	0.000	0.000	0.000
160	A	210	SER	0	0.005	-0.011	19.954	0.001	0.001	0.000	0.000	0.000	0.000
161	A	211	GLY	0	-0.007	0.011	16.688	0.000	0.000	0.000	0.000	0.000	0.000
162	A	212	ASP	-1	-0.752	-0.868	13.274	0.416	0.416	0.000	0.000	0.000	0.000
163	A	213	PRO	0	0.005	0.009	14.938	-0.020	-0.020	0.000	0.000	0.000	0.000
164	A	214	PHE	0	0.011	0.006	15.655	-0.041	-0.041	0.000	0.000	0.000	0.000
165	A	215	ARG	1	0.863	0.914	17.536	-0.133	-0.133	0.000	0.000	0.000	0.000
166	A	216	SER	0	0.063	0.077	19.748	-0.008	-0.008	0.000	0.000	0.000	0.000
167	A	217	ASP	-1	-0.835	-0.949	19.017	0.204	0.204	0.000	0.000	0.000	0.000
168	A	218	SER	0	0.007	-0.011	18.763	-0.017	-0.017	0.000	0.000	0.000	0.000
169	A	219	TYR	0	-0.024	-0.016	19.644	-0.030	-0.030	0.000	0.000	0.000	0.000
170	A	220	GLY	0	0.045	0.049	22.611	-0.021	-0.021	0.000	0.000	0.000	0.000
171	A	221	LEU	0	-0.026	-0.017	17.035	-0.018	-0.018	0.000	0.000	0.000	0.000
172	A	222	LEU	0	-0.023	-0.013	21.423	-0.026	-0.026	0.000	0.000	0.000	0.000
173	A	223	GLY	0	0.027	0.024	23.452	-0.016	-0.016	0.000	0.000	0.000	0.000
174	A	224	ASN	0	0.016	0.004	23.200	-0.002	-0.002	0.000	0.000	0.000	0.000
175	A	225	SER	0	-0.105	-0.048	23.083	-0.021	-0.021	0.000	0.000	0.000	0.000
176	A	226	VAL	0	0.043	0.002	24.974	-0.017	-0.017	0.000	0.000	0.000	0.000
177	A	227	ASP	-1	-0.830	-0.907	28.501	-0.033	-0.033	0.000	0.000	0.000	0.000
178	A	228	ALA	0	-0.059	-0.031	26.371	-0.009	-0.009	0.000	0.000	0.000	0.000
179	A	229	LEU	0	-0.024	-0.007	27.454	-0.014	-0.014	0.000	0.000	0.000	0.000
180	A	230	TYR	0	-0.050	-0.030	30.191	-0.005	-0.005	0.000	0.000	0.000	0.000
181	A	231	ILE	0	-0.008	0.027	28.901	0.004	0.004	0.000	0.000	0.000	0.000
182	A	232	DAR	1	0.792	0.872	32.242	0.097	0.097	0.000	0.000	0.000	0.000
183	A	233	DGL	-1	-0.801	-0.912	32.300	-0.139	-0.139	0.000	0.000	0.000	0.000
184	A	234	ARG	1	0.924	0.983	23.106	0.195	0.195	0.000	0.000	0.000	0.000
185	A	235	LEU	0	0.042	0.009	26.958	-0.013	-0.013	0.000	0.000	0.000	0.000
186	A	236	PRO	0	-0.020	-0.018	29.321	-0.013	-0.013	0.000	0.000	0.000	0.000
187	A	237	LYS	1	0.847	0.922	30.493	0.154	0.154	0.000	0.000	0.000	0.000
188	A	238	LEU	0	0.028	0.003	24.906	-0.006	-0.006	0.000	0.000	0.000	0.000
189	A	239	ARG	1	0.897	0.946	27.520	0.192	0.192	0.000	0.000	0.000	0.000
190	A	240	TYR	0	0.014	0.008	29.171	-0.006	-0.006	0.000	0.000	0.000	0.000
191	A	241	ASP	-1	-0.721	-0.845	27.815	-0.182	-0.182	0.000	0.000	0.000	0.000
192	A	242	LYS	1	0.835	0.911	24.741	0.350	0.350	0.000	0.000	0.000	0.000
193	A	243	GLN	0	-0.045	-0.018	26.621	-0.002	-0.002	0.000	0.000	0.000	0.000
194	A	244	LEU	0	-0.051	-0.012	29.666	0.003	0.003	0.000	0.000	0.000	0.000
195	A	245	VAL	0	-0.035	-0.032	25.278	0.006	0.006	0.000	0.000	0.000	0.000
196	A	246	GLY	0	0.025	0.021	26.939	-0.008	-0.008	0.000	0.000	0.000	0.000
197	A	247	VAL	0	-0.021	0.018	20.775	-0.016	-0.016	0.000	0.000	0.000	0.000
198	A	248	THR	0	0.019	0.004	22.680	0.005	0.005	0.000	0.000	0.000	0.000
199	A	249	GLU	-1	-0.883	-0.925	20.189	-0.445	-0.445	0.000	0.000	0.000	0.000
200	A	250	ARG	1	0.928	0.940	19.524	0.525	0.525	0.000	0.000	0.000	0.000
201	A	251	GLU	-1	-0.843	-0.926	18.460	-0.581	-0.581	0.000	0.000	0.000	0.000
202	A	252	SER	0	0.015	0.006	15.958	-0.037	-0.037	0.000	0.000	0.000	0.000
203	A	253	TYR	0	-0.015	-0.033	9.868	0.065	0.065	0.000	0.000	0.000	0.000
204	A	254	VAL	0	0.003	0.015	15.947	0.042	0.042	0.000	0.000	0.000	0.000
205	A	255	LYS	1	0.883	0.934	15.748	0.722	0.722	0.000	0.000	0.000	0.000
206	A	256	ALA	0	-0.016	0.007	20.464	0.034	0.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:GLN)