<?xml version="1.0" ?>
<disprot version="5.2"><protein id="DP00301">
<general><name>Dihydrofolate reductase</name><synonyms><synonym>DYR_ECOLI</synonym><synonym>EC 1.5.1.3</synonym><synonym>DHFR</synonym></synonyms><uniprot>P0ABQ4</uniprot><unigene></unigene><swissprot>DYR_ECOLI</swissprot><trembl></trembl><ncbi>81175282</ncbi><source_organism>Escherichia coli</source_organism><native_sequence>MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR</native_sequence><functional_narrative></functional_narrative></general><regions><region id="3"><type>Disordered</type><name>G-H loop</name><start>142</start><end>150</end><sequence>DADAQNSHS</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>1DDS</id><chain>A</chain></pdb><pdb><id>1DDS</id><chain>B</chain></pdb><pdb><id>1DDR</id><chain>A</chain></pdb><pdb><id>1DDR</id><chain>B</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="D-O">Function arises via a disorder to order transition</structural_functional_type></structural_functional_types><functional_classes></functional_classes><functional_subclasses><functional_subclass id="h">Substrate/ligand binding</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K"></temperature><ph></ph></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference></references><comments></comments></region><region id="2"><type>Disordered</type><name>F-G loop</name><start>116</start><end>132</end><sequence>DAEVEGDTHFPDYEPDD</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>1DDS</id><chain>A</chain></pdb><pdb><id>1DDS</id><chain>B</chain></pdb><pdb><id>1DDR</id><chain>A</chain></pdb><pdb><id>1DDR</id><chain>B</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="D-O">Function arises via a disorder to order transition</structural_functional_type></structural_functional_types><functional_classes></functional_classes><functional_subclasses><functional_subclass id="h">Substrate/ligand binding</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K"></temperature><ph></ph></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference></references><comments></comments></region><region id="1"><type>Disordered</type><name>Met20 loop</name><start>9</start><end>24</end><sequence>AVDRVIGMENAMPWNL</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>1DDS</id><chain>A</chain></pdb><pdb><id>1DDS</id><chain>B</chain></pdb><pdb><id>1DDR</id><chain>A</chain></pdb><pdb><id>1DDR</id><chain>B</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="D-O">Function arises via a disorder to order transition</structural_functional_type></structural_functional_types><functional_classes></functional_classes><functional_subclasses><functional_subclass id="h">Substrate/ligand binding</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K"></temperature><ph></ph></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference></references><comments></comments></region><region id="7"><type>Disordered</type><name>Met20 loop</name><start>16</start><end>22</end><sequence>MENAMPW</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>1RG7</id><chain>A</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="D-O">Function arises via a disorder to order transition</structural_functional_type></structural_functional_types><functional_classes><functional_class id="3">Molecular assembly</functional_class></functional_classes><functional_subclasses><functional_subclass id="h">Substrate/ligand binding</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K"></temperature><ph></ph><additives><additive><name>CaCl2</name><type></type><concentration unit="mM">50</concentration></additive><additive><name>imidazole</name><type>pH 7.0</type><concentration unit="mM">20</concentration></additive><additive><name>imidazole (second aliquot)</name><type>pH 7.2</type><concentration unit="mM">60</concentration></additive><additive><name>PEG 6000</name><type>w/v</type><concentration unit="%">25</concentration></additive></additives></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference></references><comments></comments></region><region id="6"><type>Disordered</type><name></name><start>95</start><end>96</end><sequence>GG</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>5DFR</id><chain>A</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="U">Relationship to function unknown</structural_functional_type></structural_functional_types><functional_classes><functional_class id="0">Unknown</functional_class></functional_classes><functional_subclasses><functional_subclass id="x">Unknown</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K">277</temperature><ph></ph></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference></references><comments></comments></region><region id="5"><type>Disordered</type><name>Met20 loop</name><start>16</start><end>20</end><sequence>MENAM</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>5DFR</id><chain>A</chain></pdb><pdb><id>6DFR</id><chain>A</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="D-O">Function arises via a disorder to order transition</structural_functional_type></structural_functional_types><functional_classes><functional_class id="3">Molecular assembly</functional_class></functional_classes><functional_subclasses><functional_subclass id="h">Substrate/ligand binding</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K">277</temperature><ph></ph><additives><additive><name>DHFR</name><type>40 to 50 mg/ml</type><concentration></concentration></additive></additives></detection><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K">298</temperature><ph></ph><additives><additive><name>CaCl2</name><type></type><concentration unit="mM">50</concentration></additive><additive><name>imidazole</name><type>pH 7.0</type><concentration unit="mM">20</concentration></additive><additive><name>imidazole (second aliquot)</name><type>pH 7.2</type><concentration unit="mM">60</concentration></additive><additive><name>PEG 6000</name><type>(w/v)</type><concentration unit="%">25</concentration></additive></additives></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference></references><comments><comment>PDB ID 5DFR had V10, L28, E120, D122, and D127 containing disordered side chains.  </comment><comment>PDB ID 6DFR had the side chains beyond the CB of E120 and D127 being disordered.</comment></comments></region><region id="4"><type>Disordered</type><name></name><start>63</start><end>72</end><sequence>SSQPGTDDRV</sequence><modification_types><modification_type>Complex</modification_type></modification_types><pdbs><pdb><id>1DDR</id><chain>A</chain></pdb><pdb><id>1DDR</id><chain>B</chain></pdb><pdb><id>1DDS</id><chain>A</chain></pdb><pdb><id>1DDS</id><chain>B</chain></pdb></pdbs><structural_functional_types><structural_functional_type id="D-O">Function arises via a disorder to order transition</structural_functional_type></structural_functional_types><functional_classes><functional_class id="0">Unknown</functional_class></functional_classes><functional_subclasses><functional_subclass id="x">Unknown</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K"></temperature><ph></ph></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>9012674</pmid><author>Sawaya MR, Kraut J</author><title>Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence</title><year>1997</year><publication>Biochemistry</publication><volume>36</volume><number>3</number><pages>586-603</pages></reference><reference type="Journal article"><pmid>14717591</pmid><author>Schnell JR, Dyson HJ, Wright PE</author><title>Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase</title><year>2004</year><publication>Biochemistry</publication><volume>43</volume><number>2</number><pages>374-83</pages></reference></references><comments></comments></region></regions><comments></comments></protein>
</disprot>
