I don't know if I'm parsing in correctly or if i'm printing out incorrectly from a the hashmap? I think i must be parsing incorrectly because when I check the values I get null.
main.java
public static void main(String[] args) throws Exception
{
SAXParserFactory spf = SAXParserFactory.newInstance();
SAXParser sp = spf.newSAXParser();
XMLReader xr = sp.getXMLReader();
xr.setContentHandler(new DrugbankHandler());
xr.parse("c:\\drugbank.xml");
System.out.println(DrugbankHandler.lookupCache);
// DrugbankHandler.printMap();
contenthandler.java
public class DrugbankHandler implements ContentHandler {
boolean drugFound;
boolean nameFound;
boolean drugInteraction;
boolean drugID;
boolean packager;
boolean calculatedProperties;
boolean kindFound;
boolean inChiKeyValueFound;
boolean nextValueIsInChiKey;
boolean isSmallMolecule;
boolean property;
boolean previousTagWasDrugID;
DrugModel tempDrugModel;
/**
* stores key (drugbank-id), value (drug model) pairs
*/
public final static HashMap<String, DrugModel> lookupCache = new HashMap<String, DrugModel>(
7000);
@Override
public void startElement(String uri, String localName, String qName,
Attributes atts) throws SAXException {
//System.out.print(atts);
if (tempDrugModel != null && tempDrugModel.drugbankID.equals("DB00002")) {
System.out.println(localName);
if (localName.equals("value")) {
System.out.print("");
}
}
if (localName.equals("drug-interaction")) {
drugInteraction = true;
return;
}
if (localName.equals("drug") && !drugInteraction
&& atts.getLength() > 0) {
if (atts.getValue("type").equals("biotech"))
return;
drugFound = true;
tempDrugModel = new DrugModel();
String type = atts.getValue("type");
if (type.startsWith("small"))
isSmallMolecule = true;
else
isSmallMolecule = false;
tempDrugModel.isSmallMolecule = isSmallMolecule;
return;
}
if (localName.equals("drugbank-id")) {
drugID = true;
return;
}
if (previousTagWasDrugID && localName.equals("name")) {
nameFound = true;
return;
}
// if drug is a small molecule read its InChIKey value
/**
* <calculated-properties> <property> <kind>InChI</kind>
* <value>InChIKey=hurensohn</value> <source>JChem</source> </property>
* .... </calculated-properties>
*/
if (isSmallMolecule) {
if (calculatedProperties && localName.equals("property")) {
property = true;
return;
}
if (property && localName.equals("kind")) {
kindFound = true;
return;
}
if (localName.equals("calculated-properties")) {
calculatedProperties = true;
return;
}
if (nextValueIsInChiKey && localName.equals("value")) {
inChiKeyValueFound = true;
nextValueIsInChiKey = false;
return;
}
} else {
// TODO which id or feature to lookup peptides in chembl?
}
}
@Override
public void endElement(String uri, String localName, String qName)
throws SAXException {
if (drugFound && !drugInteraction && localName.equals("drug")) {
drugFound = false;
lookupCache.put(tempDrugModel.drugbankID, tempDrugModel);
return;
}
if (localName.equals("drugbank-id")) {
previousTagWasDrugID = true;
}
if (localName.equals("drug-interaction")) {
drugInteraction = false;
}
}
@Override
public void characters(char[] ch, int start, int length)
throws SAXException {
if (!drugFound)
return;
if (nameFound) {
tempDrugModel.name = new String(ch, start, length);
previousTagWasDrugID = false;
nameFound = false;
return;
}
if (drugID) {
tempDrugModel.drugbankID = new String(ch, start, length);
drugID = false;
return;
}
if (kindFound) {
String kind = new String(ch, start, length);
if (kind.equals("InChIKey")) {
nextValueIsInChiKey = true;
}
kindFound = false;
return;
}
if (inChiKeyValueFound) {
// skip the "InChIKey=" prefix of length 9
String k = new String(ch, start + 9, length - 9);
tempDrugModel.InChiKey = k;
inChiKeyValueFound = false;
return;
}
}
public static void printMap() {
/*Iterator it = lookupCache.entrySet().iterator();
while (it.hasNext()) {
Map.Entry entry = (Map.Entry) it.next();
Integer key = (Integer)entry.getKey();
String val = (String)entry.getValue();
System.out.println(lookupCache);
}*/
System.out.println(lookupCache);
}
// ignored methods following...
@Override
public void ignorableWhitespace(char[] ch, int start, int length)
throws SAXException {
}
@Override
public void processingInstruction(String target, String data)
throws SAXException {
}
@Override
public void skippedEntity(String name) throws SAXException {
}
@Override
public void setDocumentLocator(Locator locator) {
}
@Override
public void startDocument() throws SAXException {
}
@Override
public void endDocument() throws SAXException {
}
@Override
public void startPrefixMapping(String prefix, String uri)
throws SAXException {
}
@Override
public void endPrefixMapping(String prefix) throws SAXException {
}
}
sample xml
<?xml version="1.0" encoding="UTF-8"?>
<drugs xmlns="http://drugbank.ca" xmlns:xs="http://www.w3.org/2001/XMLSchema-instance" schemaVersion="2.0" xs:schemaLocation="http://www.drugbank.ca/docs/drugbank.xsd">
<drug type="biotech" created="2005-06-13 07:24:05 -0600" updated="2013-05-12 21:37:25 -0600" version="4.0">
<drugbank-id>DB00001</drugbank-id>
<name>Lepirudin</name>
<description>Lepirudin is identical to natural hirudin except for substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. It is produced via yeast cells.
</description>
<cas-number>120993-53-5</cas-number>
<general-references># Smythe MA, Stephens JL, Koerber JM, Mattson JC: A comparison of lepirudin and argatroban outcomes. Clin Appl Thromb Hemost. 2005 Oct;11(4):371-4. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16244762
# Tardy B, Lecompte T, Boelhen F, Tardy-Poncet B, Elalamy I, Morange P, Gruel Y, Wolf M, Francois D, Racadot E, Camarasa P, Blouch MT, Nguyen F, Doubine S, Dutrillaux F, Alhenc-Gelas M, Martin-Toutain I, Bauters A, Ffrench P, de Maistre E, Grunebaum L, Mouton C, Huisse MG, Gouault-Heilmann M, Lucke V: Predictive factors for thrombosis and major bleeding in an observational study in 181 patients with heparin-induced thrombocytopenia treated with lepirudin. Blood. 2006 Sep 1;108(5):1492-6. Epub 2006 May 11. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16690967
# Lubenow N, Eichler P, Lietz T, Greinacher A: Lepirudin in patients with heparin-induced thrombocytopenia - results of the third prospective study (HAT-3) and a combined analysis of HAT-1, HAT-2, and HAT-3. J Thromb Haemost. 2005 Nov;3(11):2428-36. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16241940
# Askari AT, Lincoff AM: Antithrombotic Drug Therapy in Cardiovascular Disease. 2009 Oct; pp. 440–. ISBN 9781603272346. "Google books":http://books.google.com/books?id=iadLoXoQkWEC&pg=PA440. </general-references>
<synthesis-reference/>
<indication>For the treatment of heparin-induced thrombocytopenia</indication>
<pharmacology>Lepirudin is used to break up clots and to reduce thrombocytopenia. It binds to thrombin and prevents thrombus or clot formation. It is a highly potent, selective, and essentially irreversible inhibitor of thrombin and clot-bond thrombin. Lepirudin requires no cofactor for its anticoagulant action. Lepirudin is a recombinant form of hirudin, an endogenous anticoagulant found in medicinal leeches.</pharmacology>
<mechanism-of-action>Lepirudin forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen and initiate the clotting cascade. The inhibition of thrombin prevents the blood clotting cascade. </mechanism-of-action>
<toxicity>In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased.</toxicity>
<biotransformation>Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. However, con-clusive data are not available. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) and other fragments of the parent drug.</biotransformation>
<absorption>Bioavailability is 100% following injection.</absorption>
<half-life>Approximately 1.3 hours</half-life>
<protein-binding/>
<route-of-elimination>Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) and other fragments of the parent drug.</route-of-elimination>
<volume-of-distribution>* 12.2 L [Healthy young subjects (n = 18, age 18-60 years)]
* 18.7 L [Healthy elderly subjects (n = 10, age 65-80 years)]
* 18 L [Renally impaired patients (n = 16, creatinine clearance below 80 mL/min)]
* 32.1 L [HIT patients (n = 73)]</volume-of-distribution>
<clearance>* 164 ml/min [Healthy 18-60 yrs]
* 139 ml/min [Healthy 65-80 yrs]
* 61 ml/min [renal impaired]
* 114 ml/min [HIT (Heparin-induced thrombocytopenia)]</clearance>
<secondary-accession-numbers>
<secondary-accession-number>BIOD00024</secondary-accession-number>
<secondary-accession-number>BTD00024</secondary-accession-number>
</secondary-accession-numbers>
<groups>
<group>approved</group>
</groups>
<taxonomy>
<kingdom/>
<substructures/>
</taxonomy>
<synonyms>
<synonym>Hirudin variant-1</synonym>
</synonyms>
<salts/>
<brands>
<brand>Refludan</brand>
</brands>
<mixtures/>
<packagers>
<packager>
<name>Bayer Healthcare</name>
<url>http://www.bayerhealthcare.com</url>
</packager>
<packager>
<name>Berlex Labs</name>
<url>http://www.berlex.com</url>
</packager>
</packagers>
<manufacturers>
<manufacturer generic="false">Bayer healthcare pharmaceuticals inc</manufacturer>
</manufacturers>
<prices>
<price>
<description>Refludan 50 mg vial</description>
<cost currency="USD">273.19</cost>
<unit>vial</unit>
</price>
</prices>
<categories>
<category>Antithrombins</category>
<category>Fibrinolytic Agents</category>
</categories>
<affected-organisms>
<affected-organism>Humans and other mammals</affected-organism>
</affected-organisms>
<dosages>
<dosage>
<form>Powder, for solution</form>
<route>Intravenous</route>
<strength/>
</dosage>
</dosages>
<atc-codes>
<atc-code>B01AE02</atc-code>
<category/>
</atc-codes>
<ahfs-codes>
<ahfs-code>20:12.04.12</ahfs-code>
</ahfs-codes>
<patents>
<patent>
<number>5180668</number>
<country>United States</country>
<approved>1993-01-19</approved>
<expires>2010-01-19</expires>
</patent>
<patent>
<number>1339104</number>
<country>Canada</country>
<approved>1997-07-29</approved>
<expires>2014-07-29</expires>
</patent>
</patents>
<food-interactions/>
<drug-interactions>
<drug-interaction>
<drug>DB01381</drug>
<name>Ginkgo biloba</name>
<description>Additive anticoagulant/antiplatelet effects may increase bleed risk. Concomitant therapy should be avoided.</description>
</drug-interaction>
<drug-interaction>
<drug>DB00374</drug>
<name>Treprostinil</name>
<description>The prostacyclin analogue, Treprostinil, increases the risk of bleeding when combined with the anticoagulant, Lepirudin. Monitor for increased bleeding during concomitant thearpy. </description>
</drug-interaction>
</drug-interactions>
<protein-sequences>
<fasta>
<fasta>#<PolypeptideSequence:0x007f1d1efef190></fasta>
</fasta>
</protein-sequences>
<experimental-properties>
<property>
<kind>Melting Point</kind>
<value>65 °C</value>
<source>Otto, A. & Seckler, R. Eur. J. Biochem. 202:67-73 (1991)</source>
</property>
<property>
<kind>Hydrophobicity</kind>
<value>-0.777</value>
<source/>
</property>
<property>
<kind>Isoelectric Point</kind>
<value>4.04</value>
<source/>
</property>
<property>
<kind>Molecular Weight</kind>
<value>6963.4250</value>
<source/>
</property>
<property>
<kind>Molecular Formula</kind>
<value>C287H440N80O110S6</value>
<source/>
</property>
</experimental-properties>
<external-identifiers>
<external-identifier>
<resource>Drugs Product Database (DPD)</resource>
<identifier>2240996</identifier>
</external-identifier>
<external-identifier>
<resource>KEGG Drug</resource>
<identifier>D06880</identifier>
</external-identifier>
<external-identifier>
<resource>National Drug Code Directory</resource>
<identifier>50419-150-57</identifier>
</external-identifier>
<external-identifier>
<resource>PharmGKB</resource>
<identifier>PA450195</identifier>
</external-identifier>
<external-identifier>
<resource>UniProtKB</resource>
<identifier>P01050</identifier>
</external-identifier>
<external-identifier>
<resource>Wikipedia</resource>
<identifier>Lepirudin</identifier>
</external-identifier>
</external-identifiers>
<external-links>
<external-link>
<resource>RxList</resource>
<url>http://www.rxlist.com/cgi/generic/lepirudin.htm</url>
</external-link>
<external-link>
<resource>Drugs.com</resource>
<url>http://www.drugs.com/cdi/lepirudin.html</url>
</external-link>
</external-links>
<targets>
<target>
<id>BE0000048</id>
<name>Prothrombin</name>
<organism>Human</organism>
<actions>
<action>inhibitor</action>
</actions>
<references># Turpie AG: Anticoagulants in acute coronary syndromes. Am J Cardiol. 1999 Sep 2;84(5A):2M-6M. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10505536
# Warkentin TE: Venous thromboembolism in heparin-induced thrombocytopenia. Curr Opin Pulm Med. 2000 Jul;6(4):343-51. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10912644
# Eriksson BI: New therapeutic options in deep vein thrombosis prophylaxis. Semin Hematol. 2000 Jul;37(3 Suppl 5):7-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11055889
# Fabrizio MC: Use of ecarin clotting time (ECT) with lepirudin therapy in heparin-induced thrombocytopenia and cardiopulmonary bypass. J Extra Corpor Technol. 2001 May;33(2):117-25. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11467439
# Szaba FM, Smiley ST: Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood. 2002 Feb 1;99(3):1053-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11807012
# Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11752352</references>
<known-action>yes</known-action>
<components>
<polypeptide id="P00734">
<name>Prothrombin</name>
<general-function>Involved in blood clotting cascade</general-function>
<specific-function>Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C</specific-function>
<gene-name>F2</gene-name>
<locus>11p11-q12</locus>
<cellular-location>Secreted protein; extracellular space</cellular-location>
<transmembrane-regions>None</transmembrane-regions>
<theoretical-pi>5.7</theoretical-pi>
<molecular-weight>70037.0</molecular-weight>
<chromosome-location/>
<external-identifiers>
<external-identifier>
<resource>HUGO Gene Nomenclature Committee (HGNC)</resource>
<identifier>HGNC:3535</identifier>
</external-identifier>
<external-identifier>
<resource>GenAtlas</resource>
<identifier>F2</identifier>
</external-identifier>
<external-identifier>
<resource>GeneCards</resource>
<identifier>F2</identifier>
</external-identifier>
<external-identifier>
<resource>GenBank Gene Database</resource>
<identifier>M17262</identifier>
</external-identifier>
<external-identifier>
<resource>GenBank Protein Database</resource>
<identifier>339641</identifier>
</external-identifier>
<external-identifier>
<resource>UniProtKB</resource>
<identifier>P00734</identifier>
</external-identifier>
</external-identifiers>
<synonyms>
<synonym>Activated Factor II [IIa]</synonym>
<synonym>Coagulation factor II</synonym>
<synonym>EC 3.4.21.5</synonym>
<synonym>Prothrombin precursor</synonym>
<synonym>Thrombin</synonym>
</synonyms>
<amino-acid-sequence>
<fasta>>Prothrombin precursor
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC
VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV
NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE
CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA
QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG
DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI
DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN
DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP
VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST
RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGE</fasta>
</amino-acid-sequence>
<gene-sequence>
<fasta>>1869 bp
ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC
CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG
GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC
GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG
GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT
GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG
AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT
GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC
GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA
TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA
GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG
TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA
CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC
TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT
GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA
GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC
CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT
CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC
GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG
CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG
GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT
GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG
ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC
CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT
GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG
GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC
AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC
CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA
GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC
CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT
GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT
GGAGAGTAG</fasta>
</gene-sequence>
<pfams>
<pfam>
<identifier>PF00594</identifier>
<name>Gla</name>
</pfam>
<pfam>
<identifier>PF00051</identifier>
<name>Kringle</name>
</pfam>
<pfam>
<identifier>PF00089</identifier>
<name>Trypsin</name>
</pfam>
</pfams>
<go-classifiers>
<go-classifier>
<id/>
<category>component</category>
<description>extracellular region</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>binding</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>catalytic activity</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>thrombin activity</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>hydrolase activity</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>calcium ion binding</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>peptidase activity</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>ion binding</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>endopeptidase activity</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>cation binding</description>
</go-classifier>
<go-classifier>
<id/>
<category>function</category>
<description>serine-type endopeptidase activity</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>protein metabolism</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>proteolysis</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>cellular protein metabolism</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>organismal physiological process</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>regulation of body fluids</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>physiological process</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>hemostasis</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>blood coagulation</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>metabolism</description>
</go-classifier>
<go-classifier>
<id/>
<category>process</category>
<description>macromolecule metabolism</description>
</go-classifier>
</go-classifiers>
</polypeptide>
</components>
</target>
</targets>
<enzymes/>
<carriers/>
<transporters/>
https://stackoverflow.com/questions/22586060
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