FMO DATABASE

FMODB ID: 8G48Y

Calculation Name: 1JJT-A-Xray547

Preferred Name: Beta-lactamase

Target Type: SINGLE PROTEIN

Ligand Name: 2,3-bis-benzo[1,3]dioxol-5-ylmethyl-succinic acid | acetate ion

Ligand 3-letter code: BDS | ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1JJT

Chain ID: A

ChEMBL ID: CHEMBL1293244

UniProt ID: Q79MP6

Base Structure: X-ray

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	220
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2670974.568711
FMO2-HF: Nuclear repulsion	2587803.969525
FMO2-HF: Total energy	-83170.599185
FMO2-MP2: Total energy	-83420.541853

3D Structure Molmil

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.
5.25	6.694	-0.016	-0.675	-0.753	-0.001

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 : 1 / q_Mulliken : 0.837 / q_NPA : 0.903

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	0.012	0.007	3.857	1.595	3.039	-0.016	-0.675	-0.753	-0.001
4	A	6	ASP	-1	-0.834	-0.913	6.562	-32.608	-32.608	0.000	0.000	0.000	0.000
5	A	7	LEU	0	-0.080	-0.036	7.842	1.874	1.874	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.834	0.912	11.233	19.492	19.492	0.000	0.000	0.000	0.000
7	A	9	ILE	0	0.013	-0.005	14.117	0.419	0.419	0.000	0.000	0.000	0.000
8	A	10	GLU	-1	-0.829	-0.891	17.401	-16.417	-16.417	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.843	0.925	20.380	10.614	10.614	0.000	0.000	0.000	0.000
10	A	12	LEU	0	-0.017	0.000	24.222	0.008	0.008	0.000	0.000	0.000	0.000
11	A	13	ASP	-1	-0.780	-0.891	26.113	-9.184	-9.184	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.851	-0.939	28.858	-9.821	-9.821	0.000	0.000	0.000	0.000
13	A	15	GLY	0	-0.014	0.003	29.991	0.093	0.093	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.039	-0.015	26.849	-0.186	-0.186	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.051	0.017	22.227	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.001	0.002	19.313	0.139	0.139	0.000	0.000	0.000	0.000
17	A	19	HIS	0	-0.041	-0.009	17.088	-1.021	-1.021	0.000	0.000	0.000	0.000
18	A	20	THR	0	0.018	-0.004	14.107	0.772	0.772	0.000	0.000	0.000	0.000
19	A	21	SER	0	0.026	0.026	11.230	-0.855	-0.855	0.000	0.000	0.000	0.000
20	A	22	PHE	0	0.007	-0.025	8.491	2.065	2.065	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.864	-0.924	7.742	-38.011	-38.011	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.920	-0.953	6.991	-31.374	-31.374	0.000	0.000	0.000	0.000
23	A	25	VAL	0	-0.040	-0.026	8.930	1.696	1.696	0.000	0.000	0.000	0.000
24	A	26	ASN	0	0.016	-0.010	12.600	0.534	0.534	0.000	0.000	0.000	0.000
25	A	27	GLY	0	0.011	0.007	14.214	-0.876	-0.876	0.000	0.000	0.000	0.000
26	A	28	TRP	0	-0.068	-0.037	15.415	0.885	0.885	0.000	0.000	0.000	0.000
27	A	29	GLY	0	0.037	0.050	11.516	0.066	0.066	0.000	0.000	0.000	0.000
28	A	30	VAL	0	0.013	-0.008	7.463	-0.144	-0.144	0.000	0.000	0.000	0.000
29	A	31	VAL	0	-0.020	0.000	10.256	2.339	2.339	0.000	0.000	0.000	0.000
30	A	32	PRO	0	0.021	0.011	12.588	-1.081	-1.081	0.000	0.000	0.000	0.000
31	A	33	LYS	1	0.736	0.854	14.247	17.775	17.775	0.000	0.000	0.000	0.000
32	A	34	HIS	1	0.788	0.879	15.796	16.072	16.072	0.000	0.000	0.000	0.000
33	A	35	GLY	0	0.039	0.017	18.553	0.311	0.311	0.000	0.000	0.000	0.000
34	A	36	LEU	0	-0.044	-0.015	20.634	0.039	0.039	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.017	0.003	21.137	-0.181	-0.181	0.000	0.000	0.000	0.000
36	A	38	VAL	0	-0.007	-0.002	23.965	0.216	0.216	0.000	0.000	0.000	0.000
37	A	39	LEU	0	-0.007	-0.002	26.170	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	40	VAL	0	-0.021	-0.019	29.538	0.305	0.305	0.000	0.000	0.000	0.000
39	A	41	ASN	0	-0.027	-0.018	33.058	0.099	0.099	0.000	0.000	0.000	0.000
40	A	42	ALA	0	0.058	0.031	31.992	-0.142	-0.142	0.000	0.000	0.000	0.000
41	A	43	GLU	-1	-0.864	-0.928	30.607	-9.233	-9.233	0.000	0.000	0.000	0.000
42	A	44	ALA	0	0.021	0.008	25.571	-0.037	-0.037	0.000	0.000	0.000	0.000
43	A	45	TYR	0	-0.039	-0.038	27.031	0.043	0.043	0.000	0.000	0.000	0.000
44	A	46	LEU	0	0.004	-0.001	20.407	-0.191	-0.191	0.000	0.000	0.000	0.000
45	A	47	ILE	0	-0.013	-0.014	23.547	0.402	0.402	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.672	-0.789	20.331	-14.343	-14.343	0.000	0.000	0.000	0.000
47	A	49	THR	0	-0.012	0.003	17.484	0.274	0.274	0.000	0.000	0.000	0.000
48	A	50	PRO	0	-0.025	-0.017	13.547	-0.151	-0.151	0.000	0.000	0.000	0.000
49	A	51	PHE	0	0.010	0.013	11.576	0.964	0.964	0.000	0.000	0.000	0.000
50	A	52	THR	0	0.053	0.034	9.089	1.024	1.024	0.000	0.000	0.000	0.000
51	A	53	ALA	0	0.081	0.045	12.409	0.879	0.879	0.000	0.000	0.000	0.000
52	A	54	LYS	1	0.995	1.001	8.295	28.682	28.682	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.826	-0.935	9.259	-28.242	-28.242	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.013	-0.025	12.049	1.574	1.574	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.892	-0.940	14.462	-16.927	-16.927	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.836	0.930	7.965	29.148	29.148	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.009	-0.001	14.395	0.849	0.849	0.000	0.000	0.000	0.000
58	A	60	VAL	0	-0.016	-0.014	16.865	0.928	0.928	0.000	0.000	0.000	0.000
59	A	61	THR	0	-0.011	-0.018	17.116	0.897	0.897	0.000	0.000	0.000	0.000
60	A	62	TRP	0	0.035	0.023	16.662	0.872	0.872	0.000	0.000	0.000	0.000
61	A	63	PHE	0	-0.017	-0.020	19.030	0.583	0.583	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.008	0.002	22.277	0.621	0.621	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.969	-0.983	19.270	-13.653	-13.653	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.863	0.939	19.542	13.722	13.722	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.005	0.011	25.547	0.380	0.380	0.000	0.000	0.000	0.000
66	A	68	TYR	0	-0.049	-0.018	25.991	0.265	0.265	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.969	0.983	26.180	9.105	9.105	0.000	0.000	0.000	0.000
68	A	70	ILE	0	-0.004	-0.006	23.083	0.171	0.171	0.000	0.000	0.000	0.000
69	A	71	LYS	1	0.881	0.951	26.667	9.320	9.320	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.021	0.010	27.087	0.270	0.270	0.000	0.000	0.000	0.000
71	A	73	SER	0	-0.028	-0.007	23.365	-0.110	-0.110	0.000	0.000	0.000	0.000
72	A	74	ILE	0	-0.016	-0.005	25.468	0.461	0.461	0.000	0.000	0.000	0.000
73	A	75	SER	0	-0.005	-0.018	22.544	-0.297	-0.297	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.054	-0.052	23.905	0.392	0.392	0.000	0.000	0.000	0.000
75	A	77	HIS	1	0.813	0.915	21.591	14.187	14.187	0.000	0.000	0.000	0.000
76	A	78	PHE	0	0.056	0.018	24.144	-0.501	-0.501	0.000	0.000	0.000	0.000
77	A	79	HIS	0	-0.012	-0.007	20.246	-0.740	-0.740	0.000	0.000	0.000	0.000
78	A	80	SER	0	0.082	0.026	16.597	0.389	0.389	0.000	0.000	0.000	0.000
79	A	81	ASP	-1	-0.809	-0.900	16.394	-16.620	-16.620	0.000	0.000	0.000	0.000
80	A	82	SER	0	-0.052	-0.061	17.415	0.001	0.001	0.000	0.000	0.000	0.000
81	A	83	THR	0	0.013	0.014	19.664	0.191	0.191	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.026	0.027	16.239	0.364	0.364	0.000	0.000	0.000	0.000
83	A	85	GLY	0	0.006	0.000	16.560	-0.621	-0.621	0.000	0.000	0.000	0.000
84	A	86	ILE	0	-0.040	-0.028	17.897	0.403	0.403	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.916	-0.950	19.637	-14.241	-14.241	0.000	0.000	0.000	0.000
86	A	88	TRP	0	-0.005	-0.006	17.268	0.601	0.601	0.000	0.000	0.000	0.000
87	A	89	LEU	0	0.015	0.005	19.728	0.435	0.435	0.000	0.000	0.000	0.000
88	A	90	ASN	0	0.081	0.066	22.329	0.610	0.610	0.000	0.000	0.000	0.000
89	A	91	SER	0	-0.053	-0.025	21.573	0.294	0.294	0.000	0.000	0.000	0.000
90	A	92	ARG	1	0.851	0.922	19.439	14.435	14.435	0.000	0.000	0.000	0.000
91	A	93	SER	0	-0.022	-0.009	24.570	0.437	0.437	0.000	0.000	0.000	0.000
92	A	94	ILE	0	-0.042	-0.011	23.094	0.300	0.300	0.000	0.000	0.000	0.000
93	A	95	PRO	0	-0.006	0.000	26.520	-0.201	-0.201	0.000	0.000	0.000	0.000
94	A	96	THR	0	0.019	0.004	24.225	-0.223	-0.223	0.000	0.000	0.000	0.000
95	A	97	TYR	0	0.007	-0.001	27.180	0.486	0.486	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.023	0.004	27.711	-0.454	-0.454	0.000	0.000	0.000	0.000
97	A	99	SER	0	0.028	0.011	29.505	0.442	0.442	0.000	0.000	0.000	0.000
98	A	100	GLU	-1	-0.797	-0.906	31.839	-8.464	-8.464	0.000	0.000	0.000	0.000
99	A	101	LEU	0	0.005	0.011	32.531	-0.129	-0.129	0.000	0.000	0.000	0.000
100	A	102	THR	0	-0.031	-0.038	27.182	-0.073	-0.073	0.000	0.000	0.000	0.000
101	A	103	ASN	0	0.050	0.020	28.527	-0.745	-0.745	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.842	-0.908	30.178	-9.308	-9.308	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.064	-0.027	28.145	-0.055	-0.055	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.018	-0.012	23.561	-0.282	-0.282	0.000	0.000	0.000	0.000
105	A	107	LYS	1	0.842	0.913	26.577	9.189	9.189	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.916	0.962	29.244	10.389	10.389	0.000	0.000	0.000	0.000
107	A	109	ASP	-1	-0.906	-0.944	22.757	-13.584	-13.584	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.007	0.014	24.341	-0.454	-0.454	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.806	0.897	19.666	14.568	14.568	0.000	0.000	0.000	0.000
110	A	112	VAL	0	0.003	-0.001	23.104	0.599	0.599	0.000	0.000	0.000	0.000
111	A	113	GLN	0	0.026	0.014	24.779	0.056	0.056	0.000	0.000	0.000	0.000
112	A	114	ALA	0	-0.028	-0.017	26.957	-0.206	-0.206	0.000	0.000	0.000	0.000
113	A	115	THR	0	-0.020	-0.018	27.810	0.400	0.400	0.000	0.000	0.000	0.000
114	A	116	ASN	0	-0.060	-0.028	30.196	0.232	0.232	0.000	0.000	0.000	0.000
115	A	117	SER	0	0.044	0.013	31.345	-0.399	-0.399	0.000	0.000	0.000	0.000
116	A	118	PHE	0	-0.030	-0.009	31.019	0.253	0.253	0.000	0.000	0.000	0.000
117	A	119	SER	0	0.029	-0.004	35.672	-0.117	-0.117	0.000	0.000	0.000	0.000
118	A	120	GLY	0	-0.028	-0.005	38.380	0.088	0.088	0.000	0.000	0.000	0.000
119	A	121	VAL	0	-0.017	-0.017	38.062	-0.188	-0.188	0.000	0.000	0.000	0.000
120	A	122	ASN	0	0.009	-0.006	37.970	-0.228	-0.228	0.000	0.000	0.000	0.000
121	A	123	TYR	0	0.057	0.047	33.669	0.283	0.283	0.000	0.000	0.000	0.000
122	A	124	TRP	0	-0.021	-0.019	35.713	-0.254	-0.254	0.000	0.000	0.000	0.000
123	A	125	LEU	0	0.008	0.024	29.991	0.110	0.110	0.000	0.000	0.000	0.000
124	A	126	VAL	0	0.041	0.022	33.185	0.063	0.063	0.000	0.000	0.000	0.000
125	A	127	LYS	1	1.000	0.997	35.937	7.072	7.072	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.044	-0.035	39.269	-0.011	-0.011	0.000	0.000	0.000	0.000
127	A	129	LYS	1	0.855	0.923	34.796	8.382	8.382	0.000	0.000	0.000	0.000
128	A	130	ILE	0	0.005	-0.003	30.125	-0.236	-0.236	0.000	0.000	0.000	0.000
129	A	131	GLU	-1	-0.790	-0.868	33.869	-8.126	-8.126	0.000	0.000	0.000	0.000
130	A	132	VAL	0	-0.005	-0.001	31.300	-0.330	-0.330	0.000	0.000	0.000	0.000
131	A	133	PHE	0	-0.003	-0.014	33.339	0.332	0.332	0.000	0.000	0.000	0.000
132	A	134	TYR	0	0.012	-0.001	33.635	-0.151	-0.151	0.000	0.000	0.000	0.000
133	A	135	PRO	0	-0.048	-0.021	33.441	0.287	0.287	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.038	0.021	36.061	0.262	0.262	0.000	0.000	0.000	0.000
135	A	137	PRO	0	-0.009	-0.014	33.682	-0.274	-0.274	0.000	0.000	0.000	0.000
136	A	138	GLY	0	0.024	0.002	31.819	0.243	0.243	0.000	0.000	0.000	0.000
137	A	139	HIS	0	-0.037	0.002	23.014	0.105	0.105	0.000	0.000	0.000	0.000
138	A	140	THR	0	0.000	-0.022	26.118	-0.257	-0.257	0.000	0.000	0.000	0.000
139	A	141	PRO	0	0.023	-0.005	29.059	0.301	0.301	0.000	0.000	0.000	0.000
140	A	142	ASP	-1	-0.720	-0.822	28.432	-11.028	-11.028	0.000	0.000	0.000	0.000
141	A	143	ASN	0	-0.048	-0.013	28.504	-0.201	-0.201	0.000	0.000	0.000	0.000
142	A	144	VAL	0	-0.012	0.000	29.271	0.451	0.451	0.000	0.000	0.000	0.000
143	A	145	VAL	0	-0.051	-0.015	28.909	-0.427	-0.427	0.000	0.000	0.000	0.000
144	A	146	VAL	0	0.008	-0.005	28.372	0.230	0.230	0.000	0.000	0.000	0.000
145	A	147	TRP	0	-0.026	-0.007	30.583	-0.184	-0.184	0.000	0.000	0.000	0.000
146	A	148	LEU	0	0.050	0.034	28.889	0.115	0.115	0.000	0.000	0.000	0.000
147	A	149	PRO	0	-0.027	-0.018	33.512	0.057	0.057	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.836	-0.912	35.772	-8.394	-8.394	0.000	0.000	0.000	0.000
149	A	151	ARG	1	0.841	0.910	32.442	9.127	9.127	0.000	0.000	0.000	0.000
150	A	152	LYS	1	0.916	0.975	34.627	7.788	7.788	0.000	0.000	0.000	0.000
151	A	153	ILE	0	0.032	0.021	28.760	-0.065	-0.065	0.000	0.000	0.000	0.000
152	A	154	LEU	0	0.005	-0.001	30.968	0.094	0.094	0.000	0.000	0.000	0.000
153	A	155	PHE	0	0.024	0.015	22.361	-0.210	-0.210	0.000	0.000	0.000	0.000
154	A	156	GLY	0	0.028	0.000	27.566	0.265	0.265	0.000	0.000	0.000	0.000
155	A	157	GLY	0	0.069	0.035	24.298	0.110	0.110	0.000	0.000	0.000	0.000
156	A	158	CYS	0	-0.054	-0.018	21.724	-0.370	-0.370	0.000	0.000	0.000	0.000
157	A	159	PHE	0	0.013	0.012	24.598	0.134	0.134	0.000	0.000	0.000	0.000
158	A	160	ILE	0	-0.045	-0.018	27.056	0.271	0.271	0.000	0.000	0.000	0.000
159	A	161	LYS	1	0.830	0.920	23.277	12.270	12.270	0.000	0.000	0.000	0.000
160	A	162	PRO	0	0.031	0.016	26.401	0.276	0.276	0.000	0.000	0.000	0.000
161	A	163	TYR	0	0.034	0.001	25.825	0.447	0.447	0.000	0.000	0.000	0.000
162	A	164	GLY	0	0.052	0.037	27.237	0.004	0.004	0.000	0.000	0.000	0.000
163	A	165	LEU	0	-0.006	-0.008	26.127	-0.445	-0.445	0.000	0.000	0.000	0.000
164	A	166	GLY	0	0.024	0.020	23.134	-0.241	-0.241	0.000	0.000	0.000	0.000
165	A	167	ASN	0	0.010	0.004	20.816	0.611	0.611	0.000	0.000	0.000	0.000
166	A	168	LEU	0	0.029	-0.009	22.875	0.304	0.304	0.000	0.000	0.000	0.000
167	A	169	GLY	0	-0.008	0.011	24.735	0.393	0.393	0.000	0.000	0.000	0.000
168	A	170	ASP	-1	-0.835	-0.903	25.417	-11.867	-11.867	0.000	0.000	0.000	0.000
169	A	171	ALA	0	-0.024	-0.011	28.127	0.294	0.294	0.000	0.000	0.000	0.000
170	A	172	ASN	0	0.000	-0.007	29.763	0.370	0.370	0.000	0.000	0.000	0.000
171	A	173	ILE	0	0.044	0.006	31.085	0.127	0.127	0.000	0.000	0.000	0.000
172	A	174	GLU	-1	-0.799	-0.886	34.229	-8.188	-8.188	0.000	0.000	0.000	0.000
173	A	175	ALA	0	-0.029	-0.003	36.681	0.229	0.229	0.000	0.000	0.000	0.000
174	A	176	TRP	0	-0.006	0.021	27.505	0.069	0.069	0.000	0.000	0.000	0.000
175	A	177	PRO	0	0.030	0.006	35.229	0.028	0.028	0.000	0.000	0.000	0.000
176	A	178	LYS	1	0.923	0.958	37.888	7.572	7.572	0.000	0.000	0.000	0.000
177	A	179	SER	0	0.027	-0.008	35.699	0.220	0.220	0.000	0.000	0.000	0.000
178	A	180	ALA	0	0.025	0.010	35.020	-0.009	-0.009	0.000	0.000	0.000	0.000
179	A	181	LYS	1	0.919	0.968	36.587	7.680	7.680	0.000	0.000	0.000	0.000
180	A	182	LEU	0	-0.004	0.014	39.563	0.160	0.160	0.000	0.000	0.000	0.000
181	A	183	LEU	0	0.012	0.008	32.502	0.077	0.077	0.000	0.000	0.000	0.000
182	A	184	LYS	1	0.944	0.969	37.163	7.826	7.826	0.000	0.000	0.000	0.000
183	A	185	SER	0	-0.046	-0.025	38.539	0.146	0.146	0.000	0.000	0.000	0.000
184	A	186	LYS	1	0.764	0.888	38.465	8.267	8.267	0.000	0.000	0.000	0.000
185	A	187	TYR	0	-0.004	-0.029	35.964	0.010	0.010	0.000	0.000	0.000	0.000
186	A	188	GLY	0	0.042	0.031	37.358	-0.171	-0.171	0.000	0.000	0.000	0.000
187	A	189	LYS	1	0.871	0.926	39.778	7.398	7.398	0.000	0.000	0.000	0.000
188	A	190	ALA	0	0.003	0.003	34.217	0.038	0.038	0.000	0.000	0.000	0.000
189	A	191	LYS	1	0.852	0.938	32.253	9.711	9.711	0.000	0.000	0.000	0.000
190	A	192	LEU	0	-0.013	-0.015	29.024	-0.092	-0.092	0.000	0.000	0.000	0.000
191	A	193	VAL	0	-0.011	-0.006	29.025	0.142	0.142	0.000	0.000	0.000	0.000
192	A	194	VAL	0	0.039	0.012	23.779	-0.223	-0.223	0.000	0.000	0.000	0.000
193	A	195	PRO	0	-0.030	-0.009	23.604	0.139	0.139	0.000	0.000	0.000	0.000
194	A	196	SER	0	0.051	0.003	20.447	-0.419	-0.419	0.000	0.000	0.000	0.000
195	A	197	HIS	1	0.784	0.877	16.988	16.559	16.559	0.000	0.000	0.000	0.000
196	A	198	SER	0	-0.002	-0.002	20.190	0.263	0.263	0.000	0.000	0.000	0.000
197	A	199	GLU	-1	-0.800	-0.885	19.667	-16.367	-16.367	0.000	0.000	0.000	0.000
198	A	200	VAL	0	-0.033	-0.021	22.871	0.431	0.431	0.000	0.000	0.000	0.000
199	A	201	GLY	0	0.050	0.031	25.925	0.057	0.057	0.000	0.000	0.000	0.000
200	A	202	ASP	-1	-0.771	-0.862	29.470	-9.316	-9.316	0.000	0.000	0.000	0.000
201	A	203	ALA	0	0.038	-0.001	32.746	-0.180	-0.180	0.000	0.000	0.000	0.000
202	A	204	SER	0	-0.035	-0.038	33.930	0.185	0.185	0.000	0.000	0.000	0.000
203	A	205	LEU	0	0.001	0.001	28.009	-0.008	-0.008	0.000	0.000	0.000	0.000
204	A	206	LEU	0	-0.012	0.009	31.932	-0.131	-0.131	0.000	0.000	0.000	0.000
205	A	207	LYS	1	0.806	0.903	34.292	8.827	8.827	0.000	0.000	0.000	0.000
206	A	208	LEU	0	0.037	0.025	31.505	0.074	0.074	0.000	0.000	0.000	0.000
207	A	209	THR	0	-0.006	-0.007	30.709	-0.224	-0.224	0.000	0.000	0.000	0.000
208	A	210	LEU	0	-0.037	-0.013	32.361	0.074	0.074	0.000	0.000	0.000	0.000
209	A	211	GLU	-1	-0.841	-0.922	35.625	-8.583	-8.583	0.000	0.000	0.000	0.000
210	A	212	GLN	0	0.001	-0.004	30.503	0.172	0.172	0.000	0.000	0.000	0.000
211	A	213	ALA	0	-0.019	0.001	33.200	-0.022	-0.022	0.000	0.000	0.000	0.000
212	A	214	VAL	0	-0.029	-0.024	34.258	0.139	0.139	0.000	0.000	0.000	0.000
213	A	215	LYS	1	0.901	0.964	32.703	9.797	9.797	0.000	0.000	0.000	0.000
214	A	216	GLY	0	0.042	0.019	33.221	0.048	0.048	0.000	0.000	0.000	0.000
215	A	217	LEU	0	-0.028	-0.012	34.038	0.035	0.035	0.000	0.000	0.000	0.000
216	A	218	ASN	0	-0.006	-0.002	37.043	0.215	0.215	0.000	0.000	0.000	0.000
217	A	219	GLU	-1	-0.910	-0.956	32.126	-9.839	-9.839	0.000	0.000	0.000	0.000
218	A	220	SER	0	-0.093	-0.064	35.433	0.064	0.064	0.000	0.000	0.000	0.000
219	A	221	LYS	1	0.765	0.868	36.499	8.217	8.217	0.000	0.000	0.000	0.000
220	A	222	LYS	0	0.047	0.050	38.896	0.407	0.407	0.000	0.000	0.000	0.000

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