FMO DATABASE

FMODB ID: QKLNY

Calculation Name: 1AOE-A-Xray547

Preferred Name: Dihydrofolate reductase

Target Type: SINGLE PROTEIN

Ligand Name: nadph dihydro-nicotinamide-adenine-dinucleotide phosphate | 7-(1-ethyl-propyl)-7h-pyrrolo-[3,2-f]quinazoline-1,3-diamine

Ligand 3-letter code: NDP | GW3

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1AOE

Chain ID: A

ChEMBL ID: CHEMBL2329

UniProt ID: P22906

Base Structure: X-ray

Registration Date: 2025-09-02

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	192
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2248981.440901
FMO2-HF: Nuclear repulsion	2172204.761183
FMO2-HF: Total energy	-76776.679718
FMO2-MP2: Total energy	-77003.784968

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:1:MET)

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

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.
-153.153	-143.868	29.98	-17.566	-21.698	-0.179

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.756 / q_NPA : 0.873

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	3	LYS	1	0.834	0.886	3.407	33.423	35.318	0.034	-0.830	-1.099	-0.002
4	A	4	PRO	0	0.037	0.035	2.393	1.856	2.018	4.225	-1.053	-3.334	0.004
5	A	5	ASN	0	0.009	0.000	4.220	1.475	1.610	0.002	-0.088	-0.050	0.000
100	A	100	LEU	0	0.019	0.009	3.100	-3.678	-2.037	0.072	-0.645	-1.068	-0.001
101	A	101	ASN	0	-0.026	-0.018	1.786	-47.490	-49.005	12.631	-6.499	-4.616	-0.078
102	A	102	LEU	0	-0.005	0.006	3.092	-10.170	-8.920	0.218	-0.557	-0.911	-0.008
103	A	103	VAL	0	-0.032	-0.001	2.374	3.527	4.404	2.664	-1.067	-2.474	-0.004
104	A	104	SER	0	-0.019	-0.023	1.890	-40.302	-38.219	7.311	-4.969	-4.425	-0.066
105	A	105	ASP	-1	-0.867	-0.930	4.078	-31.207	-31.027	0.000	-0.029	-0.150	0.000
106	A	106	VAL	0	-0.042	-0.023	2.333	3.465	4.111	1.213	-0.353	-1.506	0.000
107	A	107	GLU	-1	-0.746	-0.846	2.406	-29.339	-27.922	1.579	-1.394	-1.602	-0.024
108	A	108	ARG	1	0.867	0.916	4.813	19.349	19.482	-0.001	-0.005	-0.127	0.000
109	A	109	VAL	0	0.028	0.012	4.220	-1.205	-0.824	0.032	-0.077	-0.336	0.000
6	A	6	VAL	0	-0.033	-0.015	7.013	-0.552	-0.552	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.021	0.014	8.758	1.611	1.611	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.019	-0.005	11.833	-0.572	-0.572	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.015	0.003	14.779	0.471	0.471	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.015	0.002	16.856	-0.068	-0.068	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.027	0.029	20.472	0.235	0.235	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.000	-0.014	24.073	0.008	0.008	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.027	0.007	26.805	0.111	0.111	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.818	0.922	29.971	9.133	9.133	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.035	-0.003	32.217	0.147	0.147	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.000	-0.014	32.260	-0.178	-0.178	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.041	0.025	26.285	-0.238	-0.238	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.035	0.009	27.839	-0.316	-0.316	0.000	0.000	0.000	0.000
19	A	19	ILE	0	0.006	-0.033	23.745	-0.091	-0.091	0.000	0.000	0.000	0.000
20	A	20	GLY	0	-0.024	-0.017	27.057	-0.230	-0.230	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.056	0.014	29.015	0.287	0.287	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.875	0.930	32.286	8.373	8.373	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.011	0.006	28.674	0.026	0.026	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.910	0.982	28.105	8.721	8.721	0.000	0.000	0.000	0.000
25	A	25	MET	0	0.047	0.017	24.802	0.013	0.013	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.049	-0.024	28.964	0.279	0.279	0.000	0.000	0.000	0.000
27	A	27	TRP	0	0.035	0.034	26.834	0.451	0.451	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.920	0.941	30.251	8.377	8.377	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.010	0.030	28.380	0.255	0.255	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.916	0.941	27.763	8.174	8.174	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.796	0.873	27.319	8.869	8.869	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.806	-0.874	23.394	-12.170	-12.170	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.034	0.013	23.124	-0.459	-0.459	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.856	0.935	22.105	9.888	9.888	0.000	0.000	0.000	0.000
35	A	35	TYR	0	0.090	0.052	19.871	-0.493	-0.493	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.030	0.013	17.168	-0.621	-0.621	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.849	0.928	17.262	11.773	11.773	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.823	-0.892	16.731	-13.338	-13.338	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.017	-0.011	14.810	-0.656	-0.656	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.031	-0.026	12.749	-0.957	-0.957	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.060	-0.042	11.889	-1.359	-1.359	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.821	0.905	12.313	14.348	14.348	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.037	0.003	8.612	-0.224	-0.224	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.131	-0.095	10.357	1.477	1.477	0.000	0.000	0.000	0.000
45	A	45	LYS	0	-0.024	-0.001	5.399	-0.195	-0.195	0.000	0.000	0.000	0.000
46	A	46	PRO	0	0.004	0.008	10.324	-0.432	-0.432	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.030	-0.025	11.097	1.129	1.129	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.007	0.011	6.380	-1.509	-1.509	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.882	0.942	7.218	28.673	28.673	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.018	-0.014	6.365	-4.199	-4.199	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.015	0.006	6.420	0.175	0.175	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.025	-0.015	8.014	1.395	1.395	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.007	0.005	7.741	-0.151	-0.151	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.007	0.011	11.987	1.899	1.899	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.030	0.016	15.451	-0.652	-0.652	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.862	0.907	17.956	13.706	13.706	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.933	0.960	20.070	12.916	12.916	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.014	0.022	19.791	0.489	0.489	0.000	0.000	0.000	0.000
59	A	59	TRP	0	0.078	0.025	17.506	0.286	0.286	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.896	-0.944	20.566	-12.386	-12.386	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.059	-0.031	23.786	0.467	0.467	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.040	0.032	20.114	0.454	0.454	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.001	-0.007	24.383	-0.038	-0.038	0.000	0.000	0.000	0.000
64	A	64	GLN	0	0.005	-0.021	25.089	-0.082	-0.082	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.932	0.978	25.492	10.168	10.168	0.000	0.000	0.000	0.000
66	A	66	PHE	0	-0.022	-0.018	23.694	0.169	0.169	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.879	0.977	20.234	12.816	12.816	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.024	0.008	16.321	0.437	0.437	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.046	-0.019	16.032	0.698	0.698	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.030	0.019	15.640	-0.980	-0.980	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.860	-0.931	14.402	-15.709	-15.709	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.813	0.902	10.847	16.018	16.018	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.003	0.012	6.825	0.454	0.454	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.050	-0.032	10.405	0.868	0.868	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.031	0.015	7.051	-0.245	-0.245	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.042	-0.012	11.611	1.448	1.448	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.016	0.002	11.219	-0.488	-0.488	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.020	-0.032	15.123	1.734	1.734	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.813	0.880	17.318	13.818	13.818	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.015	0.001	19.212	0.248	0.248	0.000	0.000	0.000	0.000
81	A	81	TYR	0	-0.067	-0.033	15.764	0.629	0.629	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.839	-0.915	15.543	-18.580	-18.580	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.060	-0.054	10.000	-0.867	-0.867	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.915	-0.949	11.913	-18.812	-18.812	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.010	-0.014	8.503	-1.250	-1.250	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.025	-0.005	12.484	1.231	1.231	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.826	-0.928	15.053	-17.460	-17.460	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.833	-0.910	12.018	-25.917	-25.917	0.000	0.000	0.000	0.000
89	A	89	ASN	0	-0.031	-0.018	11.865	-2.176	-2.176	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.025	-0.002	13.639	-0.060	-0.060	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.061	0.028	7.798	-0.481	-0.481	0.000	0.000	0.000	0.000
92	A	92	HIS	1	0.827	0.917	11.999	20.943	20.943	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.092	0.043	10.320	-1.819	-1.819	0.000	0.000	0.000	0.000
94	A	94	SER	0	0.049	0.034	12.444	1.030	1.030	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.036	-0.013	11.528	0.200	0.200	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.075	0.040	8.511	-1.840	-1.840	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.789	-0.866	6.861	-37.044	-37.044	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.014	-0.001	6.087	-6.094	-6.094	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.027	-0.040	6.507	-3.318	-3.318	0.000	0.000	0.000	0.000
110	A	110	PHE	0	0.028	0.014	6.964	1.568	1.568	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.030	-0.012	10.765	-0.272	-0.272	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.023	-0.006	13.015	1.071	1.071	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.013	0.035	16.082	0.897	0.897	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.020	-0.007	17.969	-0.621	-0.621	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.060	0.005	20.414	-0.499	-0.499	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.854	-0.908	21.676	-13.335	-13.335	0.000	0.000	0.000	0.000
117	A	117	ILE	0	0.017	0.011	15.538	-0.223	-0.223	0.000	0.000	0.000	0.000
118	A	118	TYR	0	0.003	-0.018	17.421	-0.227	-0.227	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.019	-0.025	19.060	-0.154	-0.154	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.914	-0.930	18.653	-14.203	-14.203	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.018	-0.028	12.791	-0.447	-0.447	0.000	0.000	0.000	0.000
122	A	122	ILE	0	0.023	0.031	15.362	-0.685	-0.685	0.000	0.000	0.000	0.000
123	A	123	ASN	0	-0.006	-0.006	17.645	0.292	0.292	0.000	0.000	0.000	0.000
124	A	124	ASN	0	-0.010	0.007	11.727	-0.454	-0.454	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.033	0.006	13.383	-0.326	-0.326	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.004	0.004	6.708	-0.223	-0.223	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.049	-0.008	9.798	-0.483	-0.483	0.000	0.000	0.000	0.000
128	A	128	SER	0	0.043	0.004	11.608	0.747	0.747	0.000	0.000	0.000	0.000
129	A	129	HIS	0	0.005	0.009	13.241	0.390	0.390	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.014	0.000	14.703	-0.590	-0.590	0.000	0.000	0.000	0.000
131	A	131	LEU	0	-0.020	-0.008	15.506	0.507	0.507	0.000	0.000	0.000	0.000
132	A	132	ILE	0	0.024	0.003	18.463	-0.184	-0.184	0.000	0.000	0.000	0.000
133	A	133	THR	0	-0.031	-0.027	21.895	0.255	0.255	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.806	-0.883	24.456	-9.930	-9.930	0.000	0.000	0.000	0.000
135	A	135	ILE	0	0.002	-0.008	27.613	0.210	0.210	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.871	-0.944	30.259	-8.662	-8.662	0.000	0.000	0.000	0.000
137	A	137	HIS	0	0.057	0.015	33.954	-0.040	-0.040	0.000	0.000	0.000	0.000
138	A	138	PRO	0	-0.015	-0.002	37.162	0.003	0.003	0.000	0.000	0.000	0.000
139	A	139	SER	0	-0.035	-0.026	40.153	0.184	0.184	0.000	0.000	0.000	0.000
140	A	140	PRO	0	0.026	0.026	36.483	-0.056	-0.056	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.868	-0.924	37.715	-7.444	-7.444	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.050	-0.029	40.093	0.080	0.080	0.000	0.000	0.000	0.000
143	A	143	ILE	0	-0.065	-0.029	34.631	-0.064	-0.064	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.911	-0.950	36.774	-7.745	-7.745	0.000	0.000	0.000	0.000
145	A	145	MET	0	-0.097	-0.039	31.895	-0.395	-0.395	0.000	0.000	0.000	0.000
146	A	146	ASP	-1	-0.826	-0.899	31.917	-9.335	-9.335	0.000	0.000	0.000	0.000
147	A	147	THR	0	-0.068	-0.029	26.850	-0.260	-0.260	0.000	0.000	0.000	0.000
148	A	148	PHE	0	0.031	0.012	28.300	-0.045	-0.045	0.000	0.000	0.000	0.000
149	A	149	LEU	0	-0.034	0.001	22.507	-0.408	-0.408	0.000	0.000	0.000	0.000
150	A	150	LYS	1	0.931	0.965	24.582	12.157	12.157	0.000	0.000	0.000	0.000
151	A	151	PHE	0	0.034	-0.001	19.763	-0.418	-0.418	0.000	0.000	0.000	0.000
152	A	152	PRO	0	0.040	0.037	22.502	0.375	0.375	0.000	0.000	0.000	0.000
153	A	153	LEU	0	0.018	-0.007	23.028	-0.262	-0.262	0.000	0.000	0.000	0.000
154	A	154	GLU	-1	-0.864	-0.923	25.591	-10.395	-10.395	0.000	0.000	0.000	0.000
155	A	155	SER	0	-0.031	-0.016	23.320	0.119	0.119	0.000	0.000	0.000	0.000
156	A	156	TRP	0	-0.046	-0.025	16.299	-0.654	-0.654	0.000	0.000	0.000	0.000
157	A	157	THR	0	-0.005	-0.012	22.656	0.679	0.679	0.000	0.000	0.000	0.000
158	A	158	LYS	1	0.847	0.929	22.748	9.709	9.709	0.000	0.000	0.000	0.000
159	A	159	GLN	0	-0.002	-0.017	20.819	0.636	0.636	0.000	0.000	0.000	0.000
160	A	160	PRO	0	0.021	0.012	23.972	0.173	0.173	0.000	0.000	0.000	0.000
161	A	161	LYS	1	0.838	0.885	24.212	9.379	9.379	0.000	0.000	0.000	0.000
162	A	162	SER	0	0.021	0.016	23.943	-0.137	-0.137	0.000	0.000	0.000	0.000
163	A	163	GLU	-1	-0.818	-0.890	20.428	-12.629	-12.629	0.000	0.000	0.000	0.000
164	A	164	LEU	0	-0.002	0.009	19.317	-0.658	-0.658	0.000	0.000	0.000	0.000
165	A	165	GLN	0	-0.015	-0.026	19.383	-0.120	-0.120	0.000	0.000	0.000	0.000
166	A	166	LYS	1	0.829	0.886	18.663	12.149	12.149	0.000	0.000	0.000	0.000
167	A	167	PHE	0	-0.023	0.008	12.249	-0.628	-0.628	0.000	0.000	0.000	0.000
168	A	168	VAL	0	0.002	-0.005	14.875	-0.912	-0.912	0.000	0.000	0.000	0.000
169	A	169	GLY	0	0.035	0.045	17.136	-0.083	-0.083	0.000	0.000	0.000	0.000
170	A	170	ASP	-1	-0.833	-0.908	18.284	-12.280	-12.280	0.000	0.000	0.000	0.000
171	A	171	THR	0	-0.083	-0.044	18.209	0.346	0.346	0.000	0.000	0.000	0.000
172	A	172	VAL	0	0.018	0.002	20.935	0.114	0.114	0.000	0.000	0.000	0.000
173	A	173	LEU	0	-0.005	0.010	21.687	-0.077	-0.077	0.000	0.000	0.000	0.000
174	A	174	GLU	-1	-0.846	-0.893	25.440	-8.873	-8.873	0.000	0.000	0.000	0.000
175	A	175	ASP	-1	-0.826	-0.905	28.166	-9.625	-9.625	0.000	0.000	0.000	0.000
176	A	176	ASP	-1	-0.880	-0.925	30.802	-8.176	-8.176	0.000	0.000	0.000	0.000
177	A	177	ILE	0	-0.001	0.012	27.807	0.280	0.280	0.000	0.000	0.000	0.000
178	A	178	LYS	1	0.895	0.937	31.949	7.891	7.891	0.000	0.000	0.000	0.000
179	A	179	GLU	-1	-0.838	-0.908	30.848	-9.227	-9.227	0.000	0.000	0.000	0.000
180	A	180	GLY	0	-0.003	0.001	35.116	-0.064	-0.064	0.000	0.000	0.000	0.000
181	A	181	ASP	-1	-0.893	-0.949	38.403	-7.253	-7.253	0.000	0.000	0.000	0.000
182	A	182	PHE	0	-0.037	-0.016	33.286	-0.067	-0.067	0.000	0.000	0.000	0.000
183	A	183	THR	0	0.005	-0.009	33.831	0.102	0.102	0.000	0.000	0.000	0.000
184	A	184	TYR	0	-0.035	-0.047	27.268	-0.237	-0.237	0.000	0.000	0.000	0.000
185	A	185	ASN	0	0.020	0.005	28.330	-0.002	-0.002	0.000	0.000	0.000	0.000
186	A	186	TYR	0	0.025	0.009	22.746	-0.205	-0.205	0.000	0.000	0.000	0.000
187	A	187	THR	0	-0.033	-0.032	23.217	0.221	0.221	0.000	0.000	0.000	0.000
188	A	188	LEU	0	0.024	0.015	16.725	-0.473	-0.473	0.000	0.000	0.000	0.000
189	A	189	TRP	0	-0.013	-0.012	19.321	0.628	0.628	0.000	0.000	0.000	0.000
190	A	190	THR	0	0.007	0.005	17.446	-0.647	-0.647	0.000	0.000	0.000	0.000
191	A	191	ARG	1	0.850	0.924	15.110	16.842	16.842	0.000	0.000	0.000	0.000
192	A	192	LYS	0	-0.054	-0.009	19.721	-1.668	-1.668	0.000	0.000	0.000	0.000

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