FMO DATABASE

FMODB ID: 497NN

Calculation Name: 1FDP-A-Xray372

Preferred Name: Complement factor D

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1FDP

Chain ID: A

ChEMBL ID: CHEMBL2176771

UniProt ID: P00746

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	215
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2453870.334477
FMO2-HF: Nuclear repulsion	2370626.595084
FMO2-HF: Total energy	-83243.739393
FMO2-MP2: Total energy	-83483.181074

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:17:LEU)

Summations of interaction energy for fragment #1(A:17:LEU)

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.
-0.231	1.539	-0.021	-0.844	-0.905	0

Interaction energy analysis for fragmet #1(A:17:LEU)

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 : -0.026

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].
3	A	19	GLY	0	0.012	0.012	3.857	0.396	2.092	-0.020	-0.839	-0.837
4	A	20	ARG	1	0.909	0.934	6.588	-0.118	-0.118	0.000	0.000	0.000
5	A	21	GLU	-1	-0.961	-0.962	9.237	0.054	0.054	0.000	0.000	0.000
6	A	22	ALA	0	0.056	0.030	8.333	-0.069	-0.069	0.000	0.000	0.000
7	A	23	GLU	-1	-0.918	-0.951	7.380	-0.444	-0.444	0.000	0.000	0.000
8	A	24	ALA	0	-0.082	-0.040	4.553	0.030	0.104	-0.001	-0.005	-0.068
9	A	25	HIS	0	0.053	0.033	6.642	-0.046	-0.046	0.000	0.000	0.000
10	A	26	ALA	0	-0.017	-0.027	8.803	0.025	0.025	0.000	0.000	0.000
11	A	27	ARG	1	0.818	0.894	10.153	0.215	0.215	0.000	0.000	0.000
12	A	28	PRO	0	0.020	0.009	8.846	0.022	0.022	0.000	0.000	0.000
13	A	29	TYR	0	0.047	0.040	11.567	0.029	0.029	0.000	0.000	0.000
14	A	30	MET	0	-0.033	-0.003	14.713	0.012	0.012	0.000	0.000	0.000
15	A	31	ALA	0	-0.003	0.002	16.934	0.007	0.007	0.000	0.000	0.000
16	A	32	SER	0	-0.038	-0.056	19.679	-0.007	-0.007	0.000	0.000	0.000
17	A	33	VAL	0	0.016	0.006	22.592	0.011	0.011	0.000	0.000	0.000
18	A	34	GLN	0	-0.019	-0.034	24.585	-0.003	-0.003	0.000	0.000	0.000
19	A	35	LEU	0	0.064	0.032	28.032	0.006	0.006	0.000	0.000	0.000
20	A	36	ASN	0	-0.035	-0.034	31.732	0.000	0.000	0.000	0.000	0.000
21	A	38	GLY	0	0.004	0.008	29.131	-0.002	-0.002	0.000	0.000	0.000
22	A	39	ALA	0	-0.007	0.014	28.737	-0.004	-0.004	0.000	0.000	0.000
23	A	40	HIS	0	-0.016	0.016	23.917	0.007	0.007	0.000	0.000	0.000
24	A	41	LEU	0	-0.014	0.010	27.608	-0.002	-0.002	0.000	0.000	0.000
25	A	42	CYS	0	-0.148	-0.081	27.417	-0.007	-0.007	0.000	0.000	0.000
26	A	43	GLY	0	0.022	0.026	23.356	0.003	0.003	0.000	0.000	0.000
27	A	44	GLY	0	0.034	0.014	21.935	0.005	0.005	0.000	0.000	0.000
28	A	45	VAL	0	-0.019	-0.011	18.110	-0.008	-0.008	0.000	0.000	0.000
29	A	46	LEU	0	-0.003	0.019	15.263	0.008	0.008	0.000	0.000	0.000
30	A	47	VAL	0	-0.002	-0.006	17.728	-0.002	-0.002	0.000	0.000	0.000
31	A	48	ALA	0	-0.008	-0.007	18.970	0.006	0.006	0.000	0.000	0.000
32	A	49	GLU	-1	-0.919	-0.967	16.637	0.249	0.249	0.000	0.000	0.000
33	A	50	GLN	0	-0.068	-0.037	18.713	0.005	0.005	0.000	0.000	0.000
34	A	51	TRP	0	0.040	0.032	21.492	-0.011	-0.011	0.000	0.000	0.000
35	A	52	VAL	0	0.017	0.010	20.718	0.002	0.002	0.000	0.000	0.000
36	A	53	LEU	0	-0.040	-0.011	22.778	-0.001	-0.001	0.000	0.000	0.000
37	A	54	SER	0	0.012	-0.013	24.097	-0.007	-0.007	0.000	0.000	0.000
38	A	55	ALA	0	0.028	0.010	26.696	0.001	0.001	0.000	0.000	0.000
39	A	56	ALA	0	-0.028	-0.016	30.206	0.002	0.002	0.000	0.000	0.000
40	A	57	HIS	1	0.790	0.868	31.933	0.012	0.012	0.000	0.000	0.000
41	A	59	LEU	0	-0.076	-0.038	31.570	0.001	0.001	0.000	0.000	0.000
42	A	60	GLU	-1	-0.835	-0.917	34.406	0.002	0.002	0.000	0.000	0.000
43	A	61	ASP	-1	-0.967	-0.983	37.576	0.002	0.002	0.000	0.000	0.000
44	A	61	ALA	0	0.013	0.023	36.602	0.000	0.000	0.000	0.000	0.000
45	A	61	ALA	0	-0.023	-0.013	37.553	0.001	0.001	0.000	0.000	0.000
46	A	61	ASP	-1	-0.978	-1.009	38.823	0.019	0.019	0.000	0.000	0.000
47	A	62	GLY	0	-0.052	-0.021	36.566	0.002	0.002	0.000	0.000	0.000
48	A	63	LYS	1	0.848	0.933	30.717	-0.043	-0.043	0.000	0.000	0.000
49	A	64	VAL	0	0.045	0.021	29.732	-0.004	-0.004	0.000	0.000	0.000
50	A	65	GLN	0	-0.113	-0.063	26.616	0.001	0.001	0.000	0.000	0.000
51	A	66	VAL	0	0.016	0.017	21.604	-0.008	-0.008	0.000	0.000	0.000
52	A	67	LEU	0	-0.013	-0.001	19.954	0.010	0.010	0.000	0.000	0.000
53	A	68	LEU	0	-0.019	-0.021	16.578	-0.010	-0.010	0.000	0.000	0.000
54	A	69	GLY	0	0.072	0.021	13.652	0.006	0.006	0.000	0.000	0.000
55	A	70	ALA	0	-0.036	-0.011	14.515	-0.019	-0.019	0.000	0.000	0.000
56	A	71	HIS	0	-0.009	0.010	13.880	-0.008	-0.008	0.000	0.000	0.000
57	A	72	SER	0	-0.009	-0.024	15.829	0.013	0.013	0.000	0.000	0.000
58	A	73	LEU	0	-0.037	-0.019	19.138	0.012	0.012	0.000	0.000	0.000
59	A	74	SER	0	-0.052	-0.027	22.079	0.007	0.007	0.000	0.000	0.000
60	A	75	GLN	0	-0.006	0.002	18.489	-0.012	-0.012	0.000	0.000	0.000
61	A	76	PRO	0	-0.004	0.012	19.840	0.009	0.009	0.000	0.000	0.000
62	A	77	GLU	-1	-0.681	-0.846	14.925	-0.138	-0.138	0.000	0.000	0.000
63	A	78	PRO	0	0.026	0.020	12.315	0.025	0.025	0.000	0.000	0.000
64	A	79	SER	0	-0.034	-0.026	11.678	0.031	0.031	0.000	0.000	0.000
65	A	80	LYS	1	0.767	0.888	13.765	0.068	0.068	0.000	0.000	0.000
66	A	81	ARG	1	0.925	0.954	17.298	-0.173	-0.173	0.000	0.000	0.000
67	A	82	LEU	0	-0.004	0.001	19.404	-0.008	-0.008	0.000	0.000	0.000
68	A	83	TYR	0	0.013	0.014	17.903	0.024	0.024	0.000	0.000	0.000
69	A	84	ASP	-1	-0.774	-0.889	24.231	0.049	0.049	0.000	0.000	0.000
70	A	85	VAL	0	-0.004	-0.013	27.016	0.007	0.007	0.000	0.000	0.000
71	A	86	LEU	0	-0.050	-0.007	28.693	-0.002	-0.002	0.000	0.000	0.000
72	A	87	ARG	1	0.889	0.919	30.357	-0.064	-0.064	0.000	0.000	0.000
73	A	88	ALA	0	0.031	0.020	30.407	0.002	0.002	0.000	0.000	0.000
74	A	89	VAL	0	-0.038	-0.027	31.308	-0.001	-0.001	0.000	0.000	0.000
75	A	90	PRO	0	0.062	0.035	32.224	0.000	0.000	0.000	0.000	0.000
76	A	91	HIS	0	0.003	0.015	34.144	0.002	0.002	0.000	0.000	0.000
77	A	92	PRO	0	-0.022	-0.007	35.408	-0.001	-0.001	0.000	0.000	0.000
78	A	93	ASP	-1	-0.910	-0.972	38.676	0.012	0.012	0.000	0.000	0.000
79	A	94	SER	0	-0.091	-0.036	36.780	-0.002	-0.002	0.000	0.000	0.000
80	A	95	GLN	0	-0.006	-0.021	38.829	0.000	0.000	0.000	0.000	0.000
81	A	96	PRO	0	0.052	0.019	40.242	-0.002	-0.002	0.000	0.000	0.000
82	A	97	ASP	-1	-1.013	-1.001	41.301	-0.007	-0.007	0.000	0.000	0.000
83	A	98	THR	0	-0.027	0.012	40.171	-0.001	-0.001	0.000	0.000	0.000
84	A	99	ILE	0	-0.017	-0.006	36.461	0.000	0.000	0.000	0.000	0.000
85	A	100	ASP	-1	-0.946	-0.979	36.740	-0.007	-0.007	0.000	0.000	0.000
86	A	101	HIS	0	0.044	0.033	35.317	0.002	0.002	0.000	0.000	0.000
87	A	102	ASP	-1	-0.702	-0.809	33.598	-0.002	-0.002	0.000	0.000	0.000
88	A	103	LEU	0	-0.068	-0.033	28.680	-0.002	-0.002	0.000	0.000	0.000
89	A	104	LEU	0	0.021	0.013	29.553	0.003	0.003	0.000	0.000	0.000
90	A	105	LEU	0	-0.025	-0.002	25.994	0.000	0.000	0.000	0.000	0.000
91	A	106	LEU	0	0.002	0.002	26.167	0.002	0.002	0.000	0.000	0.000
92	A	107	GLN	0	0.046	0.046	25.656	-0.001	-0.001	0.000	0.000	0.000
93	A	108	LEU	0	0.015	-0.008	21.073	-0.004	-0.004	0.000	0.000	0.000
94	A	109	SER	0	0.011	-0.010	25.294	0.003	0.003	0.000	0.000	0.000
95	A	110	GLU	-1	-0.941	-0.974	22.135	0.161	0.161	0.000	0.000	0.000
96	A	111	LYS	1	0.931	0.965	19.663	-0.190	-0.190	0.000	0.000	0.000
97	A	112	ALA	0	0.046	0.024	17.249	0.009	0.009	0.000	0.000	0.000
98	A	113	THR	0	-0.025	-0.008	13.613	0.016	0.016	0.000	0.000	0.000
99	A	114	LEU	0	-0.014	-0.003	11.533	-0.024	-0.024	0.000	0.000	0.000
100	A	115	GLY	0	-0.007	-0.014	8.666	0.118	0.118	0.000	0.000	0.000
101	A	118	PRO	0	-0.048	-0.030	4.984	-0.041	-0.041	0.000	0.000	0.000
102	A	119	ALA	0	0.060	0.033	6.587	-0.128	-0.128	0.000	0.000	0.000
103	A	120	VAL	0	-0.006	0.013	9.801	-0.018	-0.018	0.000	0.000	0.000
104	A	121	ARG	1	0.947	0.962	6.219	-0.271	-0.271	0.000	0.000	0.000
105	A	122	PRO	0	0.012	0.004	12.023	-0.036	-0.036	0.000	0.000	0.000
106	A	123	LEU	0	-0.013	0.002	13.915	0.000	0.000	0.000	0.000	0.000
107	A	124	PRO	0	-0.030	-0.022	14.779	0.005	0.005	0.000	0.000	0.000
108	A	124	TRP	0	0.037	0.022	18.040	-0.019	-0.019	0.000	0.000	0.000
109	A	125	GLN	0	-0.002	-0.005	21.635	0.013	0.013	0.000	0.000	0.000
110	A	126	ARG	1	0.773	0.836	23.939	-0.035	-0.035	0.000	0.000	0.000
111	A	127	VAL	0	-0.053	-0.020	26.435	0.002	0.002	0.000	0.000	0.000
112	A	128	ASP	-1	-0.807	-0.892	28.602	-0.010	-0.010	0.000	0.000	0.000
113	A	129	ARG	1	0.939	0.967	30.329	0.019	0.019	0.000	0.000	0.000
114	A	129	ASP	-1	-0.798	-0.859	30.092	-0.026	-0.026	0.000	0.000	0.000
115	A	130	VAL	0	0.007	0.010	26.431	-0.002	-0.002	0.000	0.000	0.000
116	A	131	ALA	0	0.000	-0.005	28.816	0.001	0.001	0.000	0.000	0.000
117	A	132	PRO	0	0.047	0.034	29.587	-0.005	-0.005	0.000	0.000	0.000
118	A	133	GLY	0	-0.042	-0.018	30.669	-0.002	-0.002	0.000	0.000	0.000
119	A	134	THR	0	-0.064	-0.065	24.646	-0.008	-0.008	0.000	0.000	0.000
120	A	135	LEU	0	-0.025	-0.009	23.577	0.004	0.004	0.000	0.000	0.000
121	A	136	CYS	0	-0.020	-0.005	20.613	-0.015	-0.015	0.000	0.000	0.000
122	A	137	ASP	-1	-0.829	-0.899	17.476	-0.146	-0.146	0.000	0.000	0.000
123	A	138	VAL	0	0.015	0.022	20.585	0.012	0.012	0.000	0.000	0.000
124	A	139	ALA	0	0.006	-0.010	18.796	-0.011	-0.011	0.000	0.000	0.000
125	A	140	GLY	0	0.011	-0.012	20.755	0.014	0.014	0.000	0.000	0.000
126	A	141	TRP	0	-0.066	-0.025	18.201	-0.005	-0.005	0.000	0.000	0.000
127	A	142	GLY	0	-0.017	-0.005	23.828	0.008	0.008	0.000	0.000	0.000
128	A	152	PRO	0	0.017	-0.005	24.920	0.002	0.002	0.000	0.000	0.000
129	A	153	ASP	-1	-0.927	-0.950	23.392	-0.086	-0.086	0.000	0.000	0.000
130	A	154	SER	0	0.016	-0.017	18.908	0.002	0.002	0.000	0.000	0.000
131	A	155	LEU	0	-0.046	0.009	16.143	0.007	0.007	0.000	0.000	0.000
132	A	156	GLN	0	-0.068	-0.034	18.972	-0.020	-0.020	0.000	0.000	0.000
133	A	157	HIS	0	-0.010	-0.017	17.210	-0.006	-0.006	0.000	0.000	0.000
134	A	158	VAL	0	-0.013	0.002	20.533	-0.009	-0.009	0.000	0.000	0.000
135	A	159	LEU	0	0.008	0.013	19.467	0.005	0.005	0.000	0.000	0.000
136	A	160	LEU	0	-0.019	-0.017	23.022	0.002	0.002	0.000	0.000	0.000
137	A	161	PRO	0	-0.002	0.013	26.258	0.000	0.000	0.000	0.000	0.000
138	A	162	VAL	0	0.065	0.023	27.429	0.005	0.005	0.000	0.000	0.000
139	A	163	LEU	0	-0.057	-0.021	30.002	-0.001	-0.001	0.000	0.000	0.000
140	A	164	ASP	-1	-0.789	-0.846	33.810	-0.035	-0.035	0.000	0.000	0.000
141	A	165	ARG	1	0.839	0.848	34.527	0.023	0.023	0.000	0.000	0.000
142	A	166	ALA	0	-0.008	0.013	38.021	0.002	0.002	0.000	0.000	0.000
143	A	167	THR	0	-0.089	-0.104	38.506	0.001	0.001	0.000	0.000	0.000
144	A	168	CYS	0	-0.027	-0.010	32.620	0.002	0.002	0.000	0.000	0.000
145	A	169	ASN	0	0.074	0.047	38.845	0.002	0.002	0.000	0.000	0.000
146	A	170	ARG	1	0.929	0.976	41.966	0.030	0.030	0.000	0.000	0.000
147	A	170	ARG	1	0.754	0.846	36.375	0.045	0.045	0.000	0.000	0.000
148	A	170	THR	0	-0.060	-0.034	39.667	-0.001	-0.001	0.000	0.000	0.000
149	A	171	HIS	0	-0.030	-0.022	42.353	0.001	0.001	0.000	0.000	0.000
150	A	172	HIS	0	-0.058	-0.022	44.904	0.002	0.002	0.000	0.000	0.000
151	A	173	ASP	-1	-0.816	-0.921	43.842	-0.018	-0.018	0.000	0.000	0.000
152	A	174	GLY	0	-0.057	-0.027	44.509	0.001	0.001	0.000	0.000	0.000
153	A	175	ALA	0	0.035	0.038	41.215	0.001	0.001	0.000	0.000	0.000
154	A	176	ILE	0	-0.066	-0.041	37.200	0.000	0.000	0.000	0.000	0.000
155	A	177	THR	0	0.088	0.045	38.526	0.000	0.000	0.000	0.000	0.000
156	A	178	GLU	-1	-0.928	-0.966	37.312	-0.009	-0.009	0.000	0.000	0.000
157	A	179	ARG	1	0.904	0.931	34.805	-0.004	-0.004	0.000	0.000	0.000
158	A	180	LEU	0	0.000	0.019	33.599	0.000	0.000	0.000	0.000	0.000
159	A	181	MET	0	-0.005	0.001	27.714	0.000	0.000	0.000	0.000	0.000
160	A	183	ALA	0	0.054	0.044	28.798	-0.002	-0.002	0.000	0.000	0.000
161	A	184	GLU	-1	-0.827	-0.897	30.799	-0.051	-0.051	0.000	0.000	0.000
162	A	185	SER	0	0.042	0.009	30.593	-0.001	-0.001	0.000	0.000	0.000
163	A	186	ASN	0	-0.035	0.026	30.197	0.006	0.006	0.000	0.000	0.000
164	A	187	ARG	1	0.944	0.956	33.760	0.046	0.046	0.000	0.000	0.000
165	A	188	ARG	1	0.973	1.000	29.579	0.068	0.068	0.000	0.000	0.000
166	A	189	ASP	-1	-0.759	-0.893	28.662	-0.065	-0.065	0.000	0.000	0.000
167	A	190	SER	0	-0.035	-0.021	31.293	0.004	0.004	0.000	0.000	0.000
168	A	191	CYS	0	-0.123	-0.068	33.603	0.001	0.001	0.000	0.000	0.000
169	A	192	LYS	1	0.865	0.915	31.434	0.050	0.050	0.000	0.000	0.000
170	A	193	GLY	0	0.012	0.026	28.551	-0.003	-0.003	0.000	0.000	0.000
171	A	194	ASP	-1	-0.768	-0.875	24.737	-0.031	-0.031	0.000	0.000	0.000
172	A	195	SER	0	0.065	0.007	27.409	0.000	0.000	0.000	0.000	0.000
173	A	196	GLY	0	0.067	0.044	27.273	0.004	0.004	0.000	0.000	0.000
174	A	197	GLY	0	-0.037	-0.001	23.827	0.002	0.002	0.000	0.000	0.000
175	A	198	PRO	0	-0.007	-0.001	20.254	0.002	0.002	0.000	0.000	0.000
176	A	199	LEU	0	-0.021	-0.004	23.014	-0.010	-0.010	0.000	0.000	0.000
177	A	200	VAL	0	0.014	-0.007	17.210	0.009	0.009	0.000	0.000	0.000
178	A	202	GLY	0	0.027	0.012	18.800	0.006	0.006	0.000	0.000	0.000
179	A	207	GLY	0	-0.024	-0.013	15.736	0.001	0.001	0.000	0.000	0.000
180	A	208	VAL	0	-0.007	0.011	16.443	0.016	0.016	0.000	0.000	0.000
181	A	209	LEU	0	-0.028	-0.021	19.195	-0.008	-0.008	0.000	0.000	0.000
182	A	210	GLU	-1	-0.842	-0.940	21.167	-0.024	-0.024	0.000	0.000	0.000
183	A	211	GLY	0	0.013	-0.008	24.525	0.005	0.005	0.000	0.000	0.000
184	A	212	VAL	0	-0.010	0.008	24.906	-0.003	-0.003	0.000	0.000	0.000
185	A	213	VAL	0	-0.080	-0.008	27.074	0.001	0.001	0.000	0.000	0.000
186	A	214	THR	0	0.064	0.015	29.293	0.003	0.003	0.000	0.000	0.000
187	A	215	SER	0	-0.003	-0.016	32.339	0.002	0.002	0.000	0.000	0.000
188	A	216	GLY	0	0.104	0.048	32.392	-0.001	-0.001	0.000	0.000	0.000
189	A	217	SER	0	-0.048	-0.020	34.490	0.001	0.001	0.000	0.000	0.000
190	A	218	ARG	1	0.966	0.979	30.608	0.027	0.027	0.000	0.000	0.000
191	A	219	VAL	0	-0.023	0.010	37.343	-0.002	-0.002	0.000	0.000	0.000
192	A	221	GLY	0	0.072	0.034	39.744	0.001	0.001	0.000	0.000	0.000
193	A	222	ASN	0	-0.073	-0.061	40.954	-0.004	-0.004	0.000	0.000	0.000
194	A	223	ARG	1	0.978	0.977	42.399	0.022	0.022	0.000	0.000	0.000
195	A	223	LYS	1	0.980	0.977	38.900	0.045	0.045	0.000	0.000	0.000
196	A	224	LYS	1	0.975	0.991	37.604	0.032	0.032	0.000	0.000	0.000
197	A	225	PRO	0	0.008	0.024	35.274	-0.003	-0.003	0.000	0.000	0.000
198	A	226	GLY	0	0.040	0.037	31.727	0.002	0.002	0.000	0.000	0.000
199	A	227	ILE	0	0.032	0.008	32.757	-0.001	-0.001	0.000	0.000	0.000
200	A	228	TYR	0	-0.014	-0.015	26.709	0.000	0.000	0.000	0.000	0.000
201	A	229	THR	0	0.074	0.031	30.272	0.000	0.000	0.000	0.000	0.000
202	A	230	ARG	1	0.775	0.867	29.091	0.014	0.014	0.000	0.000	0.000
203	A	231	VAL	0	0.025	-0.001	24.720	0.004	0.004	0.000	0.000	0.000
204	A	232	ALA	0	0.020	0.019	27.824	0.005	0.005	0.000	0.000	0.000
205	A	233	SER	0	0.010	0.029	28.899	0.003	0.003	0.000	0.000	0.000
206	A	234	TYR	0	-0.073	-0.068	30.898	0.001	0.001	0.000	0.000	0.000
207	A	235	ALA	0	0.042	0.016	28.967	0.004	0.004	0.000	0.000	0.000
208	A	236	ALA	0	0.023	0.016	29.865	0.005	0.005	0.000	0.000	0.000
209	A	237	TRP	0	0.036	0.028	30.294	0.003	0.003	0.000	0.000	0.000
210	A	238	ILE	0	0.072	0.039	25.877	0.004	0.004	0.000	0.000	0.000
211	A	239	ASP	-1	-0.771	-0.845	27.258	0.051	0.051	0.000	0.000	0.000
212	A	240	SER	0	-0.141	-0.090	28.978	0.005	0.005	0.000	0.000	0.000
213	A	241	VAL	0	-0.001	0.001	29.300	0.003	0.003	0.000	0.000	0.000
214	A	242	LEU	0	-0.071	-0.036	23.879	0.005	0.005	0.000	0.000	0.000
215	A	243	ALA	0	-0.062	-0.009	27.191	0.009	0.009	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:17:LEU)