FMO DATABASE

FMODB ID: RY548

Calculation Name: 3ERB-A-Xray372

Preferred Name: Complement C2

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3ERB

Chain ID: A

ChEMBL ID: CHEMBL4295701

UniProt ID: P06681

Base Structure: X-ray

Registration Date: 2023-09-26

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	182
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1724207.103738
FMO2-HF: Nuclear repulsion	1651088.959696
FMO2-HF: Total energy	-73118.144042
FMO2-MP2: Total energy	-73323.485091

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:3:SER)

Summations of interaction energy for fragment #1(A:3:SER)

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.
-2.661	2.051	1.067	-2.417	-3.363	-0.002

Interaction energy analysis for fragmet #1(A:3:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / q_NPA : -0.019

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	5	PRO	0	0.010	0.017	3.844	0.043	1.130	-0.014	-0.481	-0.592	0.002
4	A	6	GLN	0	0.063	0.016	5.564	0.929	0.929	0.000	0.000	0.000	0.000
5	A	7	ASN	0	-0.036	0.001	8.446	0.084	0.084	0.000	0.000	0.000	0.000
6	A	8	VAL	0	0.000	-0.002	10.350	0.074	0.074	0.000	0.000	0.000	0.000
7	A	9	ASN	0	0.047	0.046	12.937	0.120	0.120	0.000	0.000	0.000	0.000
8	A	10	ILE	0	-0.023	0.000	15.967	-0.014	-0.014	0.000	0.000	0.000	0.000
9	A	11	SER	0	-0.053	-0.037	19.219	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	12	GLY	0	0.051	0.016	22.514	0.017	0.017	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.026	0.006	22.448	0.015	0.015	0.000	0.000	0.000	0.000
12	A	14	THR	0	-0.053	-0.012	19.069	-0.014	-0.014	0.000	0.000	0.000	0.000
13	A	15	PHE	0	0.026	-0.016	11.615	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	16	THR	0	0.019	0.032	15.007	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	17	LEU	0	-0.021	-0.021	8.400	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	18	SER	0	-0.002	-0.007	11.864	-0.018	-0.018	0.000	0.000	0.000	0.000
17	A	19	HIS	0	0.057	0.047	9.210	-0.045	-0.045	0.000	0.000	0.000	0.000
18	A	20	GLY	0	0.037	0.018	7.496	0.605	0.605	0.000	0.000	0.000	0.000
19	A	21	TRP	0	0.047	0.014	3.293	-1.387	-0.672	0.071	-0.290	-0.495	0.002
20	A	22	ALA	0	0.030	0.030	2.860	1.094	2.888	0.528	-1.107	-1.215	-0.008
21	A	23	PRO	0	0.045	-0.011	2.610	-2.462	-1.862	0.238	-0.268	-0.570	0.000
22	A	24	GLY	0	-0.026	-0.006	5.521	-0.380	-0.380	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.075	-0.030	7.194	-0.572	-0.572	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.041	0.006	8.828	-0.081	-0.081	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.035	-0.011	10.900	-0.040	-0.040	0.000	0.000	0.000	0.000
26	A	28	THR	0	0.037	0.004	12.575	-0.046	-0.046	0.000	0.000	0.000	0.000
27	A	29	TYR	0	-0.060	-0.062	14.905	-0.031	-0.031	0.000	0.000	0.000	0.000
28	A	30	SER	0	0.029	0.014	18.560	0.014	0.014	0.000	0.000	0.000	0.000
29	A	31	CYS	0	-0.057	0.000	21.985	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	32	PRO	0	0.048	0.028	24.973	0.011	0.011	0.000	0.000	0.000	0.000
31	A	33	GLN	0	0.063	0.019	28.261	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	34	GLY	0	0.009	0.012	31.113	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.021	-0.007	28.107	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	36	TYR	0	-0.002	-0.005	25.539	0.010	0.010	0.000	0.000	0.000	0.000
35	A	37	PRO	0	0.026	0.013	20.937	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	38	SER	0	0.002	0.024	22.432	0.019	0.019	0.000	0.000	0.000	0.000
37	A	39	PRO	0	-0.066	-0.057	17.420	-0.038	-0.038	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.123	0.053	19.665	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	41	SER	0	-0.002	0.006	15.699	0.027	0.027	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.871	0.922	11.714	-0.081	-0.081	0.000	0.000	0.000	0.000
41	A	43	LEU	0	0.042	0.028	10.576	0.048	0.048	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.949	0.979	7.240	-0.258	-0.258	0.000	0.000	0.000	0.000
43	A	46	SER	0	0.038	0.001	5.903	1.050	1.050	0.000	0.000	0.000	0.000
44	A	47	SER	0	-0.033	-0.025	5.996	0.810	0.810	0.000	0.000	0.000	0.000
45	A	48	GLY	0	0.062	0.041	2.912	-0.095	0.455	0.239	-0.329	-0.461	0.001
46	A	49	GLN	0	-0.013	-0.004	3.677	-3.085	-3.119	0.005	0.058	-0.030	0.001
47	A	50	TRP	0	-0.005	-0.030	7.004	0.625	0.625	0.000	0.000	0.000	0.000
48	A	51	GLN	0	-0.031	-0.013	9.340	-0.119	-0.119	0.000	0.000	0.000	0.000
49	A	52	THR	0	-0.009	-0.001	12.560	0.064	0.064	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.045	0.039	15.366	-0.033	-0.033	0.000	0.000	0.000	0.000
51	A	61	LYS	1	0.912	0.955	17.516	0.199	0.199	0.000	0.000	0.000	0.000
52	A	62	ALA	0	0.003	0.011	17.657	0.022	0.022	0.000	0.000	0.000	0.000
53	A	63	VAL	0	-0.007	-0.018	19.441	-0.027	-0.027	0.000	0.000	0.000	0.000
54	A	65	LYS	1	0.903	0.961	25.342	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	66	PRO	0	0.049	0.016	28.443	0.009	0.009	0.000	0.000	0.000	0.000
56	A	67	VAL	0	-0.009	0.013	30.753	0.003	0.003	0.000	0.000	0.000	0.000
57	A	68	ARG	1	0.896	0.944	32.755	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	69	CYS	0	-0.088	0.008	35.930	0.013	0.013	0.000	0.000	0.000	0.000
59	A	70	PRO	0	0.011	0.002	37.938	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	71	ALA	0	0.042	0.027	40.095	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	72	PRO	0	-0.005	0.002	43.491	0.003	0.003	0.000	0.000	0.000	0.000
62	A	73	VAL	0	-0.044	-0.013	44.132	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	74	SER	0	-0.044	-0.027	46.786	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	75	PHE	0	-0.027	-0.018	50.065	0.002	0.002	0.000	0.000	0.000	0.000
65	A	76	GLU	-1	-0.931	-0.963	52.566	0.031	0.031	0.000	0.000	0.000	0.000
66	A	77	ASN	0	-0.034	-0.012	55.919	0.002	0.002	0.000	0.000	0.000	0.000
67	A	78	GLY	0	0.110	0.047	57.444	0.000	0.000	0.000	0.000	0.000	0.000
68	A	79	ILE	0	-0.078	-0.009	55.492	0.000	0.000	0.000	0.000	0.000	0.000
69	A	80	TYR	0	0.005	-0.015	48.381	0.001	0.001	0.000	0.000	0.000	0.000
70	A	81	THR	0	-0.043	0.008	51.885	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	82	PRO	0	0.083	0.033	47.639	0.001	0.001	0.000	0.000	0.000	0.000
72	A	83	ARG	1	1.015	1.017	46.983	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	84	LEU	0	-0.040	-0.023	43.843	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	85	GLY	0	-0.006	-0.010	42.912	0.002	0.002	0.000	0.000	0.000	0.000
75	A	86	SER	0	-0.067	-0.030	38.758	0.003	0.003	0.000	0.000	0.000	0.000
76	A	87	TYR	0	0.032	-0.015	40.081	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	88	PRO	0	0.010	0.015	38.508	0.004	0.004	0.000	0.000	0.000	0.000
78	A	89	VAL	0	0.042	-0.002	34.912	0.003	0.003	0.000	0.000	0.000	0.000
79	A	90	GLY	0	-0.025	-0.005	38.361	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	91	GLY	0	-0.031	0.001	41.453	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	92	ASN	0	0.026	-0.003	43.818	0.006	0.006	0.000	0.000	0.000	0.000
82	A	93	VAL	0	-0.067	-0.027	46.691	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	94	SER	0	-0.023	-0.015	48.583	0.002	0.002	0.000	0.000	0.000	0.000
84	A	95	PHE	0	-0.045	-0.039	48.280	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	96	GLU	-1	-0.895	-0.947	54.142	0.016	0.016	0.000	0.000	0.000	0.000
86	A	97	CYS	0	-0.040	0.017	54.709	0.000	0.000	0.000	0.000	0.000	0.000
87	A	98	GLU	-1	-0.861	-0.930	59.996	0.019	0.019	0.000	0.000	0.000	0.000
88	A	99	ASP	-1	-0.878	-0.956	62.924	0.017	0.017	0.000	0.000	0.000	0.000
89	A	100	GLY	0	-0.056	-0.030	66.216	0.000	0.000	0.000	0.000	0.000	0.000
90	A	101	PHE	0	-0.068	-0.032	61.399	0.002	0.002	0.000	0.000	0.000	0.000
91	A	102	ILE	0	0.004	0.001	61.608	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	103	LEU	0	-0.009	-0.016	54.928	0.001	0.001	0.000	0.000	0.000	0.000
93	A	104	ARG	1	0.860	0.931	53.838	-0.040	-0.040	0.000	0.000	0.000	0.000
94	A	105	GLY	0	0.044	0.015	52.821	0.000	0.000	0.000	0.000	0.000	0.000
95	A	106	SER	0	-0.032	-0.020	50.066	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	107	PRO	0	0.074	0.041	51.922	0.000	0.000	0.000	0.000	0.000	0.000
97	A	108	VAL	0	-0.009	-0.002	49.988	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	109	ARG	1	0.857	0.944	45.008	-0.043	-0.043	0.000	0.000	0.000	0.000
99	A	110	GLN	0	0.037	0.014	42.925	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	112	ARG	1	1.027	1.007	37.314	-0.070	-0.070	0.000	0.000	0.000	0.000
101	A	113	PRO	0	0.053	0.004	34.297	0.001	0.001	0.000	0.000	0.000	0.000
102	A	114	ASN	0	0.002	-0.011	32.771	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	115	GLY	0	0.022	0.000	33.749	0.006	0.006	0.000	0.000	0.000	0.000
104	A	116	MET	0	-0.068	-0.028	35.602	0.000	0.000	0.000	0.000	0.000	0.000
105	A	117	TRP	0	0.001	-0.014	38.518	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	118	ASP	-1	-0.882	-0.926	42.164	0.045	0.045	0.000	0.000	0.000	0.000
107	A	119	GLY	0	0.052	0.022	44.016	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	120	GLU	-1	-0.940	-0.979	46.196	0.050	0.050	0.000	0.000	0.000	0.000
109	A	121	THR	0	-0.081	-0.101	47.369	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	122	ALA	0	0.000	0.027	49.012	0.000	0.000	0.000	0.000	0.000	0.000
111	A	123	VAL	0	-0.041	-0.029	52.102	0.001	0.001	0.000	0.000	0.000	0.000
112	A	125	ASP	-1	-0.835	-0.931	58.169	0.035	0.035	0.000	0.000	0.000	0.000
113	A	126	ASN	0	0.041	0.020	60.307	0.000	0.000	0.000	0.000	0.000	0.000
114	A	127	GLY	0	-0.020	-0.003	62.861	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	128	ALA	0	-0.030	-0.016	64.399	0.000	0.000	0.000	0.000	0.000	0.000
116	A	129	GLY	0	-0.059	-0.015	62.373	0.000	0.000	0.000	0.000	0.000	0.000
117	A	130	HIS	0	-0.029	-0.020	62.199	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	131	CYS	0	-0.132	-0.005	54.592	0.002	0.002	0.000	0.000	0.000	0.000
119	A	132	PRO	0	0.048	0.029	57.146	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	133	ASN	0	0.102	0.059	55.666	0.004	0.004	0.000	0.000	0.000	0.000
121	A	134	PRO	0	-0.039	-0.002	52.134	0.000	0.000	0.000	0.000	0.000	0.000
122	A	135	GLY	0	0.045	0.017	51.677	0.002	0.002	0.000	0.000	0.000	0.000
123	A	136	ILE	0	-0.023	-0.020	47.604	0.003	0.003	0.000	0.000	0.000	0.000
124	A	137	SER	0	-0.009	-0.007	44.387	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	138	LEU	0	0.001	-0.016	43.551	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	139	GLY	0	0.039	0.024	41.452	0.004	0.004	0.000	0.000	0.000	0.000
127	A	140	ALA	0	0.018	0.009	42.270	0.002	0.002	0.000	0.000	0.000	0.000
128	A	141	VAL	0	-0.034	-0.023	44.136	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	142	ARG	1	0.892	0.956	46.620	-0.037	-0.037	0.000	0.000	0.000	0.000
130	A	143	THR	0	-0.054	-0.020	49.460	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	144	GLY	0	0.042	0.011	51.889	0.002	0.002	0.000	0.000	0.000	0.000
132	A	145	PHE	0	-0.004	-0.016	55.259	0.000	0.000	0.000	0.000	0.000	0.000
133	A	146	ARG	1	0.945	0.992	58.219	-0.034	-0.034	0.000	0.000	0.000	0.000
134	A	147	PHE	0	0.044	0.003	56.353	0.002	0.002	0.000	0.000	0.000	0.000
135	A	148	GLY	0	0.041	0.024	60.112	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	149	HIS	0	0.028	-0.007	60.939	0.002	0.002	0.000	0.000	0.000	0.000
137	A	150	GLY	0	0.008	0.014	59.609	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	151	ASP	-1	-0.901	-0.936	58.916	0.040	0.040	0.000	0.000	0.000	0.000
139	A	152	LYS	1	0.934	0.956	53.542	-0.053	-0.053	0.000	0.000	0.000	0.000
140	A	153	VAL	0	-0.052	-0.006	51.295	-0.002	-0.002	0.000	0.000	0.000	0.000
141	A	154	ARG	1	0.955	0.965	48.287	-0.051	-0.051	0.000	0.000	0.000	0.000
142	A	155	TYR	0	-0.013	-0.032	45.234	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	156	ARG	1	0.946	0.983	41.840	-0.048	-0.048	0.000	0.000	0.000	0.000
144	A	157	CYS	0	-0.039	0.015	38.550	0.002	0.002	0.000	0.000	0.000	0.000
145	A	158	SER	0	-0.064	-0.044	39.929	0.000	0.000	0.000	0.000	0.000	0.000
146	A	159	SER	0	0.000	-0.012	36.888	0.003	0.003	0.000	0.000	0.000	0.000
147	A	160	ASN	0	0.011	-0.001	31.410	0.001	0.001	0.000	0.000	0.000	0.000
148	A	161	LEU	0	-0.031	-0.004	33.431	0.007	0.007	0.000	0.000	0.000	0.000
149	A	162	VAL	0	0.015	0.007	31.580	0.001	0.001	0.000	0.000	0.000	0.000
150	A	163	LEU	0	0.019	-0.003	35.038	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	164	THR	0	-0.051	-0.023	36.491	0.010	0.010	0.000	0.000	0.000	0.000
152	A	165	GLY	0	0.072	0.044	38.680	-0.006	-0.006	0.000	0.000	0.000	0.000
153	A	166	SER	0	-0.031	-0.013	42.076	0.002	0.002	0.000	0.000	0.000	0.000
154	A	167	SER	0	0.033	0.014	42.909	-0.003	-0.003	0.000	0.000	0.000	0.000
155	A	168	GLU	-1	-0.943	-0.977	44.871	0.058	0.058	0.000	0.000	0.000	0.000
156	A	169	ARG	1	0.839	0.920	48.470	-0.058	-0.058	0.000	0.000	0.000	0.000
157	A	170	GLU	-1	-0.893	-0.963	51.038	0.052	0.052	0.000	0.000	0.000	0.000
158	A	172	GLN	0	0.028	0.006	54.903	0.001	0.001	0.000	0.000	0.000	0.000
159	A	173	GLY	0	0.078	0.026	58.817	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	174	ASN	0	-0.023	-0.027	57.760	-0.002	-0.002	0.000	0.000	0.000	0.000
161	A	175	GLY	0	0.072	0.043	60.823	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	176	VAL	0	-0.031	-0.018	54.595	0.000	0.000	0.000	0.000	0.000	0.000
163	A	177	TRP	0	-0.026	-0.020	52.830	0.002	0.002	0.000	0.000	0.000	0.000
164	A	178	SER	0	0.046	0.027	52.006	0.002	0.002	0.000	0.000	0.000	0.000
165	A	179	GLY	0	-0.004	0.004	48.214	0.000	0.000	0.000	0.000	0.000	0.000
166	A	180	THR	0	-0.012	-0.018	44.445	0.000	0.000	0.000	0.000	0.000	0.000
167	A	181	GLU	-1	-0.790	-0.876	45.722	0.057	0.057	0.000	0.000	0.000	0.000
168	A	182	PRO	0	-0.015	0.009	43.079	0.004	0.004	0.000	0.000	0.000	0.000
169	A	183	ILE	0	-0.002	0.018	39.308	-0.005	-0.005	0.000	0.000	0.000	0.000
170	A	185	ARG	1	0.977	0.987	33.975	-0.103	-0.103	0.000	0.000	0.000	0.000
171	A	186	GLN	0	0.020	-0.001	32.120	0.004	0.004	0.000	0.000	0.000	0.000
172	A	187	PRO	0	0.024	0.021	29.168	0.008	0.008	0.000	0.000	0.000	0.000
173	A	188	TYR	0	0.050	0.011	26.954	0.008	0.008	0.000	0.000	0.000	0.000
174	A	189	SER	0	-0.046	-0.033	27.191	0.008	0.008	0.000	0.000	0.000	0.000
175	A	190	TYR	0	-0.019	-0.022	27.672	0.000	0.000	0.000	0.000	0.000	0.000
176	A	191	ASP	-1	-0.909	-0.947	23.016	0.197	0.197	0.000	0.000	0.000	0.000
177	A	192	PHE	0	-0.144	-0.066	24.033	0.004	0.004	0.000	0.000	0.000	0.000
178	A	193	PRO	0	-0.010	0.010	24.422	0.005	0.005	0.000	0.000	0.000	0.000
179	A	194	GLU	-1	-0.895	-0.949	26.338	0.130	0.130	0.000	0.000	0.000	0.000
180	A	195	ASP	-1	-0.961	-0.984	28.247	0.153	0.153	0.000	0.000	0.000	0.000
181	A	196	VAL	0	-0.048	-0.021	26.594	0.004	0.004	0.000	0.000	0.000	0.000
182	A	197	ALA	0	-0.024	-0.010	28.288	-0.016	-0.016	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:SER)