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-- Table structure for table `atlas`
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CREATE TABLE `atlas` (
  `id` smallint(4) NOT NULL auto_increment,
  `membrane_id` smallint(4) NOT NULL,
  `species_id` smallint(4) NOT NULL,
  `cell` char(255) NOT NULL,
  `pub` text NOT NULL,
  `publink` text NOT NULL,
  `pc` decimal(3,1) NOT NULL,
  `pe` decimal(3,1) NOT NULL,
  `pi` decimal(3,1) NOT NULL,
  `ps` decimal(3,1) NOT NULL,
  `pa` decimal(3,1) NOT NULL,
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  `ch` decimal(3,1) NOT NULL,
  `cb` decimal(3,1) NOT NULL,
  `sl` decimal(3,1) NOT NULL,
  `pips` decimal(3,1) NOT NULL,
  `pilpe` decimal(3,1) NOT NULL,
  `lpc` decimal(3,1) NOT NULL,
  `pg` decimal(3,1) NOT NULL,
  `other` text NOT NULL,
  PRIMARY KEY  (`id`)
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--
-- Dumping data for table `atlas`
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INSERT INTO `atlas` (`id`, `membrane_id`, `species_id`, `cell`, `pub`, `publink`, `pc`, `pe`, `pi`, `ps`, `pa`, `cl`, `sph`, `ch`, `cb`, `sl`, `pips`, `pilpe`, `lpc`, `pg`, `other`) VALUES
(1, 4, 53, 'Fibroblast (NIH 3T3 cell line)', 'Chem Biol Interact. 2006 Dec 15;164(3):167-73. The plasma membrane lipid composition affects fusion between cells and model membranes.', 'http://www.ncbi.nlm.nih.gov/pubmed/17098217?ordinalpos=2&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum', 43.2, 16.1, 7.6, 6.4, 1.5, 0.0, 12.2, 13.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(2, 4, 14, 'Schwann (NF1T cell line)', 'J Neurosci Res. 1997 Aug 1;49(3):372-80. Lipid composition and phospholipid asymmetry of membranes from a Schwann cell line.', 'http://www.ncbi.nlm.nih.gov/pubmed/9260748?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 44.0, 14.0, 9.6, 2.8, 0.0, 0.0, 29.6, 0.6, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(3, 6, 55, 'Rat Liver (male Wistar)', 'Biochem J. 1974 Jun;140(3):461-8. Studies on the lipid composition of the rat liver endoplasmic reticulum after induction with phenobarbitone and 20-methylcholanthrene.', 'http://www.ncbi.nlm.nih.gov/pubmed/4447625?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 53.0, 20.2, 0.0, 0.0, 0.0, 0.0, 3.7, 0.0, 0.0, 0.0, 14.1, 0.0, 0.0, 0.0, ''),
(4, 4, 55, 'Neuronal Cell Bodies (NS) from Cultured Dorsal Root Ganglia (embryonic day 15 rat pups)', 'J Neurochem. 1995 Jan;64(1):424-9. Lipid composition of neuronal cell bodies and neurites from cultured dorsal root ganglia.', 'http://www.ncbi.nlm.nih.gov/pubmed/7798942?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 28.9, 16.5, 5.8, 3.1, 0.0, 0.0, 2.8, 15.4, 3.1, 1.6, 0.0, 0.0, 0.0, 0.0, ''),
(5, 4, 55, 'Neurites (NP) from Cultured Dorsal Root Ganglia (embryonic day 15 rat pups)', 'J Neurochem. 1995 Jan;64(1):424-9. Lipid composition of neuronal cell bodies and neurites from cultured dorsal root ganglia.', 'http://www.ncbi.nlm.nih.gov/pubmed/7798942?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 27.0, 22.3, 6.3, 6.2, 0.0, 0.0, 4.5, 22.1, 5.2, 2.6, 0.0, 0.0, 0.0, 0.0, ''),
(6, 4, 6, 'Bovine Adrenal Chromaffin cells', 'Lipids. 1986 Jun;21(6):417-9. Plasma membrane lipids of bovine adrenal chromaffin cells.', 'http://www.ncbi.nlm.nih.gov/pubmed/3736352?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 48.0, 32.2, 0.0, 0.0, 0.0, 0.0, 9.3, 0.0, 0.0, 0.0, 10.4, 0.0, 0.0, 0.0, ''),
(7, 6, 157, 'Barley Roots', 'Plant Physiol. 1989 Jul;90(3):955-961. Lipid Composition of Plasma Membranes and Endomembranes Prepared from Roots of Barley (Hordeum vulgare L.) : Effects of Salt.', 'http://www.ncbi.nlm.nih.gov/pubmed/16666904?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=3&log$=relatedarticles&logdbfrom=pubmed', 58.0, 20.9, 0.0, 1.4, 1.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 10.0, 2.2, 6.4, ''),
(8, 13, 157, 'Barley Roots', 'Plant Physiol. 1989 Jul;90(3):955-961. Lipid Composition of Plasma Membranes and Endomembranes Prepared from Roots of Barley (Hordeum vulgare L.) : Effects of Salt.', 'http://www.ncbi.nlm.nih.gov/pubmed/16666904?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=3&log$=relatedarticles&logdbfrom=pubmed', 53.6, 23.0, 0.0, 2.9, 1.9, 0.6, 0.0, 0.0, 0.0, 0.0, 0.0, 8.7, 3.2, 6.0, ''),
(9, 4, 157, 'Barley Roots', 'Plant Physiol. 1989 Jul;90(3):955-961. Lipid Composition of Plasma Membranes and Endomembranes Prepared from Roots of Barley (Hordeum vulgare L.) : Effects of Salt.', 'http://www.ncbi.nlm.nih.gov/pubmed/16666904?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=3&log$=relatedarticles&logdbfrom=pubmed', 36.9, 32.1, 0.0, 7.1, 6.3, 2.0, 0.0, 0.0, 0.0, 0.0, 0.0, 7.6, 5.0, 3.0, ''),
(10, 4, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 16.8, 20.3, 17.7, 33.6, 3.9, 0.2, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(11, 14, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 35.0, 22.3, 19.1, 12.9, 1.2, 0.7, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(12, 13, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 46.5, 19.4, 18.3, 4.4, 2.1, 1.6, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(13, 10, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 44.6, 26.9, 15.1, 5.9, 2.2, 1.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(14, 11, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 48.2, 22.9, 15.8, 4.5, 1.6, 7.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(15, 6, 36, 'Light Microsomes', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 51.3, 33.4, 7.5, 6.6, 0.2, 0.4, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(16, 19, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 45.6, 32.6, 10.2, 1.2, 4.4, 5.9, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(17, 5, 36, 'Budding Yeast', 'J Bacteriol. 1991 Mar;173(6):2026-34. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae.', 'http://www.ncbi.nlm.nih.gov/pubmed/2002005?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed', 38.4, 24.0, 16.2, 3.8, 1.5, 16.1, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(18, 4, 113, 'Erythrocytes', 'Biochimie. 2007 Feb;89(2):205-12. Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies.', 'http://www.ncbi.nlm.nih.gov/pubmed/17157973?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum', 43.2, 28.3, 0.0, 0.0, 0.0, 0.0, 12.1, 0.0, 0.0, 0.0, 15.8, 0.0, 0.0, 0.0, ''),
(19, 4, 55, 'Mast Cells (RBL-2H3 rat cell line, Wistar, leukemia, basophilic)', 'Biochimie. 2007 Feb;89(2):205-12. Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies.', 'http://www.ncbi.nlm.nih.gov/pubmed/17157973?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum', 50.0, 25.0, 0.0, 0.0, 0.0, 0.0, 5.0, 0.0, 0.0, 0.0, 15.0, 0.0, 5.0, 0.0, ''),
(20, 4, 14, 'Dendritic cells', 'Biochimie. 2007 Feb;89(2):205-12. Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies.', 'http://www.ncbi.nlm.nih.gov/pubmed/17157973?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum', 43.0, 23.0, 0.0, 0.0, 0.0, 0.0, 9.0, 0.0, 0.0, 0.0, 12.0, 0.0, 13.0, 0.0, ''),
(21, 4, 14, 'Reticular Nucleus (RN) cells', 'J Biol Chem. 2003 Mar 28;278(13):10963-72. Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation.', 'http://www.ncbi.nlm.nih.gov/pubmed/12519789?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=3&log$=relatedarticles&logdbfrom=pubmed', 34.0, 27.5, 0.0, 0.0, 0.0, 6.3, 12.6, 19.6, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(22, 4, 14, 'Human T cell Lymphotropic Virus-I (HTLV-I) carrying cells (MT-4 cell line)', 'Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2641-6. The HIV lipidome: a raft with an unusual composition.', 'http://www.ncbi.nlm.nih.gov/pubmed/16481622?ordinalpos=2&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum', 43.0, 32.9, 0.0, 7.4, 0.0, 0.0, 10.4, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, ''),
(23, 15, 159, 'HIV-1', 'Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2641-6. The HIV lipidome: a raft with an unusual composition.', 'http://www.ncbi.nlm.nih.gov/pubmed/16481622?ordinalpos=2&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum', 16.0, 35.2, 0.0, 15.5, 0.0, 0.0, 33.1, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, 0.0, '');

-- --------------------------------------------------------

--
-- Table structure for table `citation`
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CREATE TABLE `citation` (
  `id` smallint(4) NOT NULL auto_increment,
  `protein_id` smallint(4) NOT NULL default '0',
  `citation` text NOT NULL,
  `pmid` int(20) NOT NULL default '0',
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=400 ;

--
-- Dumping data for table `citation`
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INSERT INTO `citation` (`id`, `protein_id`, `citation`, `pmid`) VALUES
(1, 96, 'Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920.', 8130205),
(2, 96, 'Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390.', 9804995),
(3, 98, 'Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920.', 8130205),
(4, 98, 'Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390.', 9804995),
(5, 99, 'Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920.', 8130205),
(6, 99, 'Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390.', 9804995),
(7, 95, 'Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920.', 8130205),
(8, 95, 'Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390.', 9804995),
(9, 178, 'Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920.', 8130205),
(10, 178, 'Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390.', 9804995),
(11, 97, 'Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920.', 8130205),
(12, 97, 'Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390.', 9804995),
(13, 94, 'Blaurock AE, and Wilkins MHF (1972) Structure of retinal photoreceptor membranes. Nature 236: 313-314.', 4552165),
(14, 94, 'Barclay P, and Findlay JBC (1984) Labelling of the cytoplasmic domains of ovine rhodopsin with hydrophilic chemical probes. Biochem. J. 220: 75-84.', 6378185),
(15, 94, 'Davison MD, and Findlay JBC (1986) Modification of ovine opsin with the photosensitive hydrophobic probe 1-azido-4-[125]-iodobenzene. Biochem. J. 234: 413-420.', 2941011),
(16, 94, 'Davison MD, and Findlay JBC (1986) Identification of the sites in opsin modified by photoactivated azido[125]iodobenzene. Biochem. J. 236: 389-395.', 2944512),
(17, 94, 'Hubbell WL, Altenbach C, Hubbell CM, and Khorana HG (2003) Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv. Prot. Chem. 63: 243-290.', 12629973),
(18, 94, 'Krebs A, Edwards PC, Villa C, Li JD, and Schertler GFX (2003) The three-dimensional structure of bovine rhodopsin determined by electron cryomicroscopy. J. Biol. Chem. 278: 50217-50225.', 14514682),
(19, 75, ' Kamihira M, Vosegaard T, Mason AJ, Straus SK, Nielsen NC, and Watts A (2005) Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy. J. Struct. Biol. 149: 7-16.', 15629653),
(20, 170, 'Altenbach C, Marti T, Khorana HG, Hubbell WL (1990) Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science 248: 1088-1092.', 2160734),
(21, 170, 'Altenbach C, Greenhalgh DA, Khorana HG, Hubbell WL (1994) A collision gradient method to determine the immersion dept of nitroxides in lipid bilayers: application ro spin-labeled mutants of bacteiorhdopsin. Proc. Nat. Acad. Sci. USA91: 1667-1671.', 8127863),
(22, 170, 'Dumas F, Lebrun MC, and Tocanne J.F. (1999) Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions? FEBS Lett.458: 271-277.', 10570923),
(23, 170, 'Greenhalgh DA, Altenbach C, Hubbell WL, and Khorana HG (1991) Locations of Arg-82, Asp-85 and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries. Proc. Natl. Acad. Sci. USA 88: 8626-8630.', 1656452),
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(25, 101, 'Andersen OS, Koeppe RE, and Roux B (2005) Gramicidin channels. IEEE Transact. Nanobiosci. 4: 10-20.', 15816168),
(26, 101, 'Andronesi OC, Pfeifer JR, Al-Momani L, Ozdirekcan S, Rijkers DTS, Angerstein B, Luca S, Koert U, Killian JA, and Baldus M (2004) Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR. J. Biomol. NMR 30: 253-265', 15754053),
(27, 101, 'Elliott JR, Needham D, Dilger JP, and Haydon DA (1983) The effects of bilayer thickness and tension on gramicidin single-channel lifetime.  Biochim. Biophys. Acta 735: 95-103.', 2579676),
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(30, 101, 'Nabedryk E, Gingold MP, and Breton J (1982) Orientation of gramicidin A transmembrane channel. Infrared dichroism study of gramicidin in vesicles. Biophys J. 38: 243-249.', 6179549),
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(32, 11, 'Pebay-Peyroula E, Garavito RM, Rosenbusch JP, Zulauf M, and Timmins PA (1995) Detergent structure in tetragonal crystals of OmpF porin. Structure 3:1051-1059.', 8590000),
(33, 83, 'Montecucco C, Smith GA, Dabbeni-sala F, Johansson A, Galante YM, and Bisson R (1982) Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex. FEBS Lett. 144: 145-148.', 6286354),
(34, 48, 'Pape EH, Menke W, Weick D, and Hoseman R (1974) Small-angle X-ray scattering of the thylakoid membranes of Rhodobacter sphaeroides in aqueous solution. Biophys. J. 14: 221.', 4545071),
(35, 48, 'Riegler J, and Mohwald H (1986) Elastic interactions of photosynthetic reaction center proteins affecting phase transitions and protein distributions. Biophys. J. 49: 1111-1118.', 0),
(36, 48, 'Roth M, Arnoux B, Ducruix A, and Reiss-Husson F (1991) Structure of the detergent phase and protein-detergent interactions in crystals of the wild-type (strain Y) Rhodobacter sphaeroides photochemical reaction center. Biochemistry 30: 9403-9413.', 1892841),
(37, 35, 'Perozo E, Kloda A, Cortes DM, and Martinac B (2001) Site-directed spin-labeling analysis of reconstituted MscL in the closed state. J. Gen. Physiol. 118: 193-205.', 11479346),
(38, 35, 'Powl AM, East JM, and Lee AG (2003) Lipid-protein interactions studied by introduction of a tryptophan residue: The mechanosensitive channel MscL. Biochemistry 42: 14306-14317.', 14640699),
(39, 35, 'Powl AM, Wright JN, East JM, and Lee AG (2005) Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: Studies with the mechanosensitive channel MscL. Biochemistry 44: 5713-5721.', 15823029),
(40, 60, 'Gross A, and Hubbell WL (2002) Identification of protein side chains near the membrane-aqueous interface: A site-directed spin labeling study of KcsA. Biochemistry 41: 1123-1128.', 11802710),
(41, 60, 'Gross A, Columbus L, Hideg K, Altenbach C, and Hubbell WL  (1999) Structure of the KcsA potassium channel from Streptomyces lividans: A site-directed spin labeling study of the second transmembrane segment. Biochemistry 38: 10324-10335.', 10441126),
(42, 60, 'Perozo E, Cortes DM, and Cuello LG (1998) Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy Nature Struct. Biol.  5 (6): 459-469.', 9628484),
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(44, 60, 'Williamson IM, Alvis SJ, East JM, and Lee AG (2002) Interactions of phospholipids with the potassium channel KcsA. Biophys. J. 83: 2026-2038.', 12324421),
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-- --------------------------------------------------------

--
-- Table structure for table `class`
--

CREATE TABLE `class` (
  `id` smallint(4) NOT NULL auto_increment,
  `number` char(4) NOT NULL default '',
  `name` char(80) NOT NULL default '',
  `description` char(100) NOT NULL default '',
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=17 ;

--
-- Dumping data for table `class`
--

INSERT INTO `class` (`id`, `number`, `name`, `description`) VALUES
(1, '1.1.', 'Alpha-helical polytopic', ''),
(2, '1.3.', 'Beta-barrel transmembrane', ''),
(6, '2.2.', 'All beta monotopic/peripheral', ''),
(5, '2.1.', 'All alpha monotopic/peripheral', ''),
(7, '2.3.', 'Alpha/Beta monotopic/peripheral', ''),
(8, '2.4.', 'Alpha + Beta monotopic/peripheral', ''),
(11, '3.1.', 'Alpha-helical peptides', ''),
(12, '3.3.', 'Pi(Beta)-helical peptides', ''),
(13, '3.2.', 'Beta-hairpin peptides', ''),
(14, '3.4.', 'Nonregular peptides', ''),
(16, '1.2.', 'Alpha-helical bitopic', '');

-- --------------------------------------------------------

--
-- Table structure for table `classification`
--

CREATE TABLE `classification` (
  `id` smallint(3) NOT NULL auto_increment,
  `type_id` smallint(4) NOT NULL default '0',
  `class_id` smallint(4) NOT NULL default '0',
  `superfamily_id` smallint(4) NOT NULL default '0',
  `family_id` smallint(4) NOT NULL default '0',
  PRIMARY KEY  (`id`),
  KEY `family_id` (`family_id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 PACK_KEYS=0 AUTO_INCREMENT=415 ;

--
-- Dumping data for table `classification`
--

INSERT INTO `classification` (`id`, `type_id`, `class_id`, `superfamily_id`, `family_id`) VALUES
(1, 1, 1, 1, 1),
(2, 1, 1, 1, 2),
(3, 1, 1, 2, 3),
(4, 1, 1, 2, 4),
(5, 1, 1, 2, 5),
(6, 1, 1, 3, 6),
(7, 1, 1, 3, 7),
(8, 1, 1, 3, 8),
(9, 1, 1, 3, 9),
(10, 1, 1, 3, 10),
(82, 3, 11, 68, 83),
(12, 1, 1, 4, 12),
(13, 1, 1, 5, 13),
(14, 1, 1, 6, 14),
(15, 1, 1, 6, 15),
(16, 1, 1, 7, 16),
(17, 1, 1, 8, 17),
(84, 1, 1, 8, 85),
(19, 1, 1, 10, 19),
(20, 1, 1, 11, 20),
(21, 1, 1, 12, 21),
(22, 1, 1, 13, 22),
(23, 1, 1, 14, 23),
(24, 1, 1, 15, 24),
(25, 1, 1, 16, 25),
(26, 1, 1, 17, 26),
(374, 2, 6, 256, 366),
(28, 1, 1, 19, 28),
(29, 1, 1, 20, 29),
(30, 1, 1, 21, 30),
(31, 1, 1, 22, 31),
(32, 1, 1, 23, 32),
(33, 1, 1, 24, 33),
(34, 1, 16, 25, 34),
(35, 1, 2, 26, 35),
(36, 1, 2, 268, 36),
(37, 1, 2, 27, 37),
(38, 1, 2, 271, 38),
(39, 1, 2, 28, 39),
(40, 1, 2, 29, 40),
(41, 1, 2, 71, 41),
(42, 1, 2, 30, 42),
(43, 1, 2, 31, 43),
(44, 1, 2, 32, 44),
(45, 1, 2, 33, 45),
(46, 1, 2, 34, 46),
(47, 1, 2, 35, 47),
(48, 1, 2, 35, 48),
(49, 2, 5, 37, 49),
(50, 2, 5, 38, 50),
(51, 2, 5, 39, 51),
(52, 2, 5, 39, 52),
(98, 2, 5, 78, 98),
(54, 2, 5, 41, 54),
(55, 1, 16, 42, 55),
(56, 2, 5, 43, 56),
(57, 2, 5, 44, 57),
(58, 2, 5, 45, 58),
(364, 1, 1, 67, 356),
(61, 2, 6, 48, 61),
(248, 2, 8, 177, 249),
(63, 2, 6, 47, 63),
(247, 2, 5, 39, 248),
(65, 2, 6, 51, 65),
(66, 2, 6, 52, 66),
(67, 2, 6, 53, 67),
(68, 2, 6, 54, 68),
(69, 2, 6, 55, 69),
(70, 2, 6, 56, 70),
(99, 2, 5, 78, 99),
(72, 2, 7, 58, 72),
(73, 2, 7, 59, 73),
(74, 2, 8, 60, 74),
(75, 2, 8, 61, 75),
(76, 2, 6, 61, 76),
(77, 2, 6, 62, 77),
(78, 2, 6, 63, 78),
(380, 3, 11, 195, 372),
(85, 1, 1, 67, 82),
(81, 1, 1, 15, 81),
(83, 3, 12, 69, 84),
(86, 1, 16, 70, 86),
(87, 1, 1, 66, 87),
(88, 1, 2, 31, 88),
(89, 1, 2, 33, 89),
(90, 1, 16, 70, 90),
(91, 1, 1, 72, 91),
(92, 1, 16, 73, 92),
(93, 1, 16, 73, 93),
(94, 1, 16, 74, 94),
(95, 1, 16, 75, 95),
(96, 1, 1, 77, 97),
(97, 3, 11, 76, 96),
(100, 2, 5, 79, 100),
(101, 2, 5, 80, 101),
(102, 2, 5, 81, 102),
(103, 2, 5, 82, 103),
(104, 2, 5, 83, 104),
(105, 2, 5, 83, 105),
(106, 2, 5, 83, 106),
(107, 2, 5, 84, 107),
(108, 2, 5, 85, 108),
(109, 2, 5, 86, 109),
(110, 2, 5, 87, 110),
(111, 2, 5, 88, 111),
(112, 2, 5, 89, 112),
(113, 2, 5, 90, 113),
(114, 2, 5, 90, 114),
(115, 2, 5, 90, 115),
(249, 2, 6, 178, 250),
(117, 2, 5, 92, 117),
(118, 2, 5, 93, 118),
(119, 2, 5, 94, 119),
(120, 2, 5, 95, 120),
(121, 2, 5, 96, 121),
(122, 2, 5, 97, 122),
(123, 2, 5, 98, 123),
(409, 3, 11, 276, 400),
(125, 2, 6, 99, 125),
(126, 2, 6, 99, 126),
(127, 2, 6, 99, 127),
(128, 2, 6, 100, 128),
(129, 2, 6, 101, 129),
(246, 2, 7, 139, 247),
(245, 2, 8, 145, 246),
(244, 2, 8, 145, 245),
(133, 2, 6, 103, 134),
(134, 2, 6, 104, 135),
(135, 2, 6, 105, 136),
(136, 2, 6, 105, 137),
(137, 2, 6, 106, 138),
(138, 2, 6, 107, 139),
(139, 2, 6, 107, 140),
(140, 2, 6, 107, 141),
(141, 2, 6, 108, 142),
(142, 2, 6, 52, 143),
(143, 2, 6, 109, 144),
(240, 2, 7, 132, 241),
(145, 2, 6, 111, 146),
(242, 2, 6, 51, 243),
(147, 2, 6, 113, 148),
(148, 2, 6, 114, 149),
(149, 2, 6, 115, 150),
(150, 2, 6, 54, 151),
(151, 2, 6, 116, 152),
(152, 2, 6, 117, 153),
(153, 2, 6, 64, 154),
(379, 1, 1, 67, 371),
(377, 2, 7, 128, 369),
(156, 2, 6, 118, 157),
(157, 2, 6, 119, 158),
(158, 2, 6, 120, 159),
(159, 2, 6, 120, 160),
(160, 2, 6, 120, 161),
(161, 2, 6, 120, 162),
(162, 2, 6, 61, 163),
(163, 2, 6, 61, 164),
(164, 2, 6, 121, 165),
(165, 2, 6, 55, 166),
(166, 2, 6, 122, 167),
(167, 2, 6, 123, 168),
(168, 2, 6, 124, 169),
(169, 2, 7, 125, 170),
(170, 2, 7, 125, 171),
(171, 2, 7, 126, 172),
(172, 2, 7, 126, 173),
(173, 2, 7, 127, 174),
(174, 2, 7, 128, 175),
(175, 2, 7, 128, 176),
(378, 3, 14, 239, 370),
(177, 2, 7, 129, 178),
(178, 2, 7, 130, 179),
(179, 2, 7, 131, 180),
(180, 2, 7, 132, 181),
(406, 1, 16, 274, 397),
(182, 2, 7, 134, 183),
(183, 2, 7, 135, 184),
(184, 2, 7, 135, 185),
(185, 2, 7, 135, 186),
(186, 2, 7, 135, 187),
(375, 2, 5, 257, 367),
(188, 2, 7, 135, 189),
(189, 2, 7, 135, 190),
(190, 2, 7, 135, 191),
(191, 2, 7, 135, 192),
(192, 2, 7, 136, 193),
(193, 2, 7, 137, 194),
(241, 2, 7, 176, 242),
(195, 2, 7, 139, 196),
(196, 2, 8, 140, 197),
(197, 2, 8, 141, 198),
(383, 3, 11, 185, 375),
(199, 2, 8, 143, 200),
(200, 2, 8, 144, 201),
(201, 2, 8, 145, 202),
(243, 2, 8, 147, 244),
(203, 2, 8, 147, 204),
(204, 2, 8, 148, 205),
(205, 2, 8, 149, 206),
(206, 2, 8, 150, 207),
(207, 3, 11, 151, 208),
(208, 3, 11, 152, 209),
(209, 3, 11, 153, 210),
(210, 3, 11, 154, 211),
(211, 3, 11, 154, 212),
(212, 3, 11, 154, 213),
(213, 3, 11, 195, 214),
(214, 3, 11, 154, 215),
(215, 3, 11, 154, 216),
(216, 3, 11, 155, 217),
(217, 3, 11, 156, 218),
(218, 3, 11, 157, 219),
(219, 3, 11, 158, 220),
(220, 3, 11, 159, 221),
(221, 3, 11, 160, 222),
(222, 3, 13, 161, 223),
(223, 3, 13, 162, 224),
(224, 3, 13, 163, 225),
(225, 3, 13, 164, 226),
(226, 3, 13, 164, 227),
(227, 3, 13, 165, 228),
(228, 3, 13, 166, 229),
(229, 3, 13, 167, 230),
(230, 3, 14, 168, 231),
(231, 3, 14, 169, 232),
(232, 3, 14, 170, 233),
(233, 3, 14, 170, 234),
(234, 3, 14, 170, 235),
(235, 3, 14, 171, 236),
(236, 3, 14, 172, 237),
(237, 2, 8, 173, 238),
(238, 2, 6, 56, 239),
(239, 3, 14, 174, 240),
(250, 1, 1, 15, 251),
(251, 1, 2, 179, 252),
(252, 1, 16, 180, 253),
(253, 1, 2, 181, 254),
(254, 2, 7, 182, 255),
(255, 2, 7, 183, 256),
(256, 3, 11, 155, 257),
(257, 3, 11, 185, 258),
(258, 2, 7, 132, 259),
(259, 1, 1, 186, 260),
(260, 1, 16, 187, 261),
(261, 1, 16, 188, 262),
(262, 2, 6, 189, 263),
(263, 2, 8, 148, 264),
(264, 2, 6, 190, 265),
(265, 2, 5, 191, 266),
(266, 3, 14, 170, 267),
(267, 2, 6, 192, 268),
(268, 2, 5, 193, 269),
(269, 1, 1, 194, 270),
(270, 3, 11, 195, 271),
(271, 1, 16, 196, 272),
(272, 1, 2, 31, 273),
(273, 1, 16, 197, 274),
(274, 2, 6, 51, 275),
(373, 1, 1, 255, 365),
(276, 1, 1, 199, 277),
(313, 2, 7, 136, 312),
(278, 1, 2, 200, 279),
(279, 1, 1, 201, 280),
(280, 1, 1, 202, 281),
(281, 1, 2, 203, 282),
(282, 1, 1, 204, 283),
(326, 1, 1, 17, 276),
(284, 1, 1, 205, 285),
(285, 1, 16, 206, 286),
(286, 1, 16, 207, 287),
(287, 1, 1, 14, 288),
(288, 1, 2, 208, 289),
(289, 1, 1, 209, 290),
(290, 2, 7, 135, 291),
(291, 1, 2, 210, 292),
(312, 2, 7, 136, 311),
(293, 1, 1, 67, 294),
(294, 1, 1, 67, 295),
(295, 1, 2, 270, 296),
(296, 1, 2, 212, 297),
(297, 1, 1, 67, 298),
(325, 1, 1, 17, 27),
(299, 1, 16, 213, 300),
(329, 1, 1, 17, 301),
(301, 1, 1, 215, 302),
(302, 2, 7, 129, 303),
(304, 1, 1, 67, 304),
(305, 0, 0, 0, 0),
(306, 2, 5, 216, 305),
(376, 2, 7, 128, 368),
(308, 1, 1, 217, 307),
(309, 1, 16, 218, 308),
(310, 1, 1, 219, 309),
(311, 1, 1, 202, 310),
(314, 2, 5, 221, 313),
(315, 3, 11, 155, 348),
(316, 2, 7, 222, 315),
(317, 2, 6, 223, 316),
(318, 2, 5, 224, 317),
(319, 2, 6, 225, 318),
(320, 3, 13, 226, 319),
(321, 3, 13, 227, 320),
(322, 2, 7, 228, 321),
(323, 2, 5, 90, 322),
(324, 1, 2, 229, 323),
(330, 1, 16, 230, 324),
(331, 2, 5, 216, 325),
(332, 1, 1, 7, 326),
(333, 1, 1, 13, 327),
(354, 1, 1, 247, 347),
(335, 1, 1, 231, 328),
(336, 2, 7, 132, 329),
(337, 2, 7, 132, 330),
(338, 3, 11, 195, 331),
(339, 1, 1, 232, 332),
(340, 1, 1, 233, 333),
(341, 2, 7, 136, 334),
(342, 3, 11, 234, 335),
(343, 3, 11, 235, 336),
(344, 3, 11, 236, 337),
(345, 2, 5, 237, 338),
(346, 3, 14, 238, 339),
(347, 3, 14, 238, 340),
(348, 3, 14, 239, 341),
(349, 1, 1, 240, 342),
(350, 2, 5, 242, 343),
(351, 2, 8, 244, 344),
(352, 2, 5, 245, 345),
(353, 2, 5, 246, 346),
(355, 3, 11, 248, 314),
(356, 3, 11, 160, 349),
(357, 1, 1, 15, 350),
(359, 1, 1, 16, 351),
(360, 1, 1, 249, 352),
(361, 2, 6, 250, 353),
(362, 2, 5, 251, 354),
(401, 2, 5, 216, 392),
(365, 1, 16, 252, 357),
(366, 1, 1, 253, 358),
(367, 1, 1, 15, 359),
(368, 1, 1, 8, 360),
(369, 2, 7, 135, 361),
(370, 1, 16, 254, 362),
(371, 1, 2, 266, 363),
(372, 1, 2, 267, 364),
(381, 3, 11, 258, 373),
(382, 3, 11, 259, 374),
(385, 3, 11, 260, 376),
(386, 2, 7, 261, 377),
(387, 3, 11, 262, 378),
(388, 3, 11, 263, 379),
(389, 3, 11, 195, 380),
(390, 2, 6, 56, 381),
(391, 3, 11, 264, 382),
(392, 3, 11, 195, 383),
(393, 3, 13, 265, 384),
(394, 3, 11, 195, 385),
(395, 2, 7, 135, 386),
(396, 2, 7, 135, 387),
(397, 2, 7, 135, 388),
(398, 2, 7, 135, 389),
(399, 1, 2, 26, 390),
(400, 1, 2, 269, 391),
(402, 2, 7, 136, 393),
(403, 1, 1, 16, 394),
(404, 2, 5, 272, 395),
(405, 1, 1, 273, 396),
(407, 1, 1, 275, 398),
(408, 2, 6, 99, 399),
(410, 1, 1, 17, 401),
(411, 1, 1, 277, 402),
(412, 1, 2, 203, 403),
(413, 2, 6, 278, 404),
(414, 1, 1, 279, 405);

-- --------------------------------------------------------

--
-- Table structure for table `family`
--

CREATE TABLE `family` (
  `id` smallint(4) NOT NULL auto_increment,
  `number` char(10) NOT NULL default '',
  `name` char(80) NOT NULL default '',
  `tcdb` char(20) NOT NULL default '',
  `pfam` char(10) NOT NULL,
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=406 ;

--
-- Dumping data for table `family`
--

INSERT INTO `family` (`id`, `number`, `name`, `tcdb`, `pfam`) VALUES
(1, '1.1.03.01.', 'Light-harvesting complexes from bacteria', '', 'PF00556'),
(2, '1.1.03.02.', 'Light-harvesting complexes from chloroplasts', '5.B.4', 'PF00504'),
(3, '1.1.02.01.', 'Photosynthetic reaction centers from bacteria', '3.E.2', ''),
(4, '1.1.02.02.', 'Photosystem I', '5.B.4', 'PF00223'),
(5, '1.1.02.03.', 'Photosystem II', '5.B.4', 'PF00421'),
(6, '1.1.04.01.', 'Cytochrome bc1 and b6f complexes', '3.D.3', 'PF00033'),
(7, '1.1.04.02.', 'Formate dehydrogenase', '5.A.3', 'PF00033'),
(8, '1.1.04.03.', 'Respiratory nitrate reductase', '5.A.3', 'PF02665'),
(9, '1.1.04.04.', 'Fumarate reductase respiratory complex', '', 'PF01127'),
(10, '1.1.04.05.', 'Succinate dehydrogenase/fumarate reductase', '', 'PF02300'),
(12, '1.1.05.01.', 'Cytochrome c oxidases', '3.D.4', 'PF00115'),
(13, '1.1.06.01.', 'V-type and F-type ATPases', '3.A.2', 'PF00137'),
(14, '1.1.01.01.', 'Ion-translocating rhodopsin', '3.E.1', 'PF01036'),
(15, '1.1.01.02.', 'G-protein coupled receptors', '', 'PF00001'),
(16, '1.1.27.01.', 'Major intrinsic protein (MIP) family', '1.A.8', 'PF00230'),
(17, '1.1.22.01.', 'Voltage-gated ion channels', '1.A.1', 'PF07885'),
(85, '1.1.22.02.', 'Inward rectifier potassium channels', '1.A.2', 'PF01007'),
(19, '1.1.28.01.', 'Chloride transporter', '2.A.49', 'PF00654'),
(20, '1.1.24.01.', 'Small conductance mechanosensitive ion channel (MscS)', '1.A.23', 'PF05552'),
(21, '1.1.23.01.', 'Large conductance mechanosensitive ion channel (MscL)', '1.A.22', 'PF01741'),
(22, '1.1.19.01.', 'Ammonia transporter Amt', '1.A.11', 'PF00909'),
(23, '1.1.26.01.', 'Ligand-gated ion channel of neurotransmitter receptors', '1.A.9', 'PF02932'),
(24, '1.1.14.01.', 'Glycerol-3-phosphate transporter', '2.A.1.4', 'PF07690'),
(25, '1.1.15.01.', 'Hydrophobe/amphiphile efflux-1 family', '2.A.6.2', 'PF00873'),
(26, '1.1.09.01.', 'FecCD transport family', '3.A.1.13', 'PF01032'),
(27, '1.1.09.03.', 'Lipid/drug exporters', '3.A.1.106', 'PF00664'),
(28, '1.1.12.01.', 'Protein translocase', '3.A.5', 'PF00344'),
(29, '1.1.16.01.', 'Proton glutamate symport protein', '2.A.23', 'PF00375'),
(30, '1.1.13.01.', 'ADP/ATP carrier', '2.A.29', 'PF00153'),
(31, '1.1.08.01.', 'P-ATPase', '3.A.3', 'PF00122'),
(32, '1.1.07.01.', 'Methane monooxygenase', '', 'PF02461'),
(33, '1.1.29.01.', 'Sulfatase', '', 'PF00884'),
(34, '1.2.07.01.', 'Glycophorin A', '', 'PF01102'),
(35, '1.3.01.01.', 'OmpA family', '', 'PF01389'),
(36, '1.3.04.03.', 'Lipid A acylation', '', 'PF07017'),
(37, '1.3.07.01.', 'OM protease omptin, OMPT', '', 'PF01278'),
(38, '1.3.08.01.', 'OM adhesion protein OpcA', '', 'PF07239'),
(39, '1.3.11.01.', 'Autotransporters of N-terminal passenger domain', '1.B.12', 'PF03797'),
(40, '1.3.12.01.', 'OM phospholipase A, OmpLA', '', 'PF02253'),
(41, '1.3.13.01.', 'Nucleoside transporter Tsx', '1.B.10', 'PF03502'),
(42, '1.3.14.01.', 'Fatty acid transporter FadL family', '1.B.9', 'PF03349'),
(43, '1.3.16.01.', 'General Bacterial Porin (GBP)', '1.B.1', 'PF00267'),
(44, '1.3.18.01.', 'Malptoporin-like proteins', '1.B.3', 'PF02264'),
(45, '1.3.20.01.', 'Brucella-Rhizobium Porin (BRP)', '1.B.14', 'PF00593'),
(46, '1.3.24.01.', 'TolC-like proteins', '1.B.17', 'PF02321'),
(47, '1.3.25.01.', 'Alpha-Hemolysin (alphaHL) channel-forming toxin (n=14,S=14)', '1.C.3', 'PF07968'),
(48, '1.3.25.02.', 'Mycobacterial Porin (MBP) (n=16,S=16)', '1.B.24', 'PF09203'),
(49, '2.1.04.01.', 'Myeloperoxidase-like', '', 'PF03098'),
(50, '2.1.05.01.', 'Terpene synthases', '', 'PF00432'),
(51, '2.1.15.01.', 'ENTH domain', '', 'PF01417'),
(52, '2.1.15.02.', 'VHS domain', '', 'PF00790'),
(54, '1.2.17.01.', 'Cytochrome P450', '', 'PF00067'),
(55, '1.2.23.01.', 'Bcl-2 inhibitors of programmed cell death', '1.A.21', 'PF00452'),
(56, '2.1.18.01.', 'Annexins', '1.A.31', 'PF00191'),
(57, '2.1.21.01.', 'Influenza virus matrix protein M1', '', 'PF00598'),
(58, '2.1.17.01.', 'LEM domain', '', 'PF03020'),
(356, '1.1.18.06.', 'Nucleobase:Cation Symporter-2', '2.A.40', 'PF00860'),
(61, '2.2.14.01.', 'Discoidin domain', '', 'PF00754'),
(247, '2.3.13.02.', 'Phosducin', '', 'PF02114'),
(63, '2.2.11.01.', 'C2 domain', '', 'PF00168'),
(246, '2.4.09.03.', 'Sedlin', '', 'PF04628'),
(65, '2.2.20.01.', 'Pleckstrin-homology domain', '', 'PF00169'),
(66, '2.2.06.01.', 'Retinol binding protein-like (n=8,S=12)', '', 'PF08212'),
(67, '2.2.38.01.', 'Cloacin translocation domain', '', 'PF03515'),
(245, '2.4.09.02.', 'Srx domain of the signal recognition particle receptor alpha-subunit', '3.A.5', 'PF09201'),
(69, '2.2.39.01.', 'Snake venom toxins', 'C.1.74', 'PF00087'),
(70, '2.2.41.01.', 'Defensin', '1.C.85', 'PF00323'),
(72, '2.3.09.01.', 'Amidase signature (AS) enzymes', '', 'PF01425'),
(73, '2.3.03.01.', 'FMN-linked oxidoreductases', '', 'PF01180'),
(74, '2.4.07.01.', 'PX domain', '', 'PF00787'),
(75, '2.2.37.01.', 'Long-chain scorpion toxins', '8.B.1', 'PF00537'),
(76, '2.2.37.02.', 'Insect defensins', '1.C.47', 'PF01097'),
(77, '2.2.26.01.', 'FYVE, a phosphatidylinositol-3-phosphate binding domain', '', 'PF01363'),
(78, '2.2.27.01.', 'Protein kinase C1 domain', '', 'PF00130'),
(372, '3.1.14.03.', 'Basic amphiphilic peptides', '', ''),
(86, '1.2.09.01.', 'Calcium ATPase regulators', '1.A.50', 'PF04272'),
(81, '1.1.14.02.', 'LacY-like proton/sugar symporter', '2.A.1.5', 'PF01306'),
(82, '1.1.18.01.', 'Neurotransmitter: sodium symporter', '2.A.22', 'PF00209'),
(83, '3.1.05.01.', 'Magainin', '', ''),
(84, '3.3.01.01.', 'Gramicidin A', '1.D.1', ''),
(87, '1.1.17.01.', 'Sodium/Proton antiporter 1', '2.A.33', 'PF06965'),
(88, '1.3.16.02.', 'Rhodobacter PorCa Porin (RPP)', '1.B.7', ''),
(89, '1.3.20.02.', 'Outer Membrane Receptor (OMR)', '1.B.14', 'PF00593'),
(90, '1.2.09.02.', 'FXYD regulators', '1.A.27', 'PF02038'),
(91, '1.1.25.01.', 'CorA Metal Ion Transporters (MIT)', '1.A.35', 'PF01544'),
(92, '1.2.12.01.', 'Major coat protein, symmetry class I', '', 'PF05371'),
(93, '1.2.12.02.', 'Major coat protein, symmetry class II', '', ''),
(94, '1.2.13.01.', 'Pilin', '', 'PF07963'),
(95, '1.2.10.01.', 'Pulmonary surfactant-associated protein', '', 'PF08999'),
(96, '3.1.06.01.', 'Peptaibol', '1.D.5', ''),
(97, '1.1.20.01.', 'Small Multidrug Resistance (SMR)', '2.A.7.1', ''),
(98, '2.1.08.01.', 'Monodomain cytochrome c', '', 'PF00034'),
(99, '2.1.08.02.', 'Two-domain cytochrome c', '', 'PF00034'),
(100, '2.1.11.01.', 'Spectrin repeat', '', 'PF00435'),
(101, '2.1.12.01.', 'Outer surface protein C', '', 'PF01441'),
(102, '2.1.23.01.', 'Ectatomin subunits', '', 'PF06457'),
(103, '2.1.13.01.', 'Crustacean CHH/MIH/GIH neurohormone', '', 'PF01147'),
(104, '2.1.24.01.', 'Saposin', '1.C.35', 'PF03489'),
(401, '1.1.09.05.', 'Mitochondrial peptide exporter family (ABCB)', '3.A.1.212.', 'PF00664'),
(250, '2.2.01.01.', 'Peptidase S26', '', 'PF10502'),
(107, '2.1.25.01.', 'Bacteriocin AS-48', '1.C.28', 'PF09221'),
(108, '2.1.09.01.', 'Uteroglobin', '', 'PF09252'),
(109, '2.1.14.01.', 'Tetratricopeptide repeat', '', 'PF01733'),
(110, '2.1.02.01.', 'Lipoxygenases', '', 'PF00305'),
(111, '2.1.03.01.', 'Bacterial phospholipase C', '', 'PF00882'),
(112, '2.1.06.01.', 'Isoprenyl diphosphate synthases', '', 'PF00348'),
(113, '2.1.01.01.', 'Vertebrate secretory phospholipase A2', '', 'PF00068'),
(114, '2.1.01.02.', 'Insect secretory phospholipase A2', '', 'PF05826'),
(115, '2.1.01.03.', 'Prokaryotic phospholipase A2', '', 'PF09056'),
(253, '1.2.11.01.', 'Stannin', '', 'PF09049'),
(117, '2.1.10.01.', 'Glycolipid transfer protein', '', 'PF08718'),
(118, '2.1.26.01.', 'Colicin pore forming domain', '1.C.1', 'PF01024'),
(252, '1.3.23.01.', 'Autotransporter-2 (AT-2)', '1.B.40', 'PF03895'),
(120, '2.1.27.01.', 'delta-Endotoxin', '1.C.2', 'PF03945'),
(121, '2.1.28.01.', 'Heat-stable enterotoxin B', '', 'PF09075'),
(122, '2.1.20.01.', 'GLA-domain', '', 'PF00594'),
(123, '2.1.22.01.', 'Virus ectodomain', '', 'PF00517'),
(400, '3.1.25.01.', 'Amylin family', '1.C.49', 'PF00214'),
(125, '2.2.12.02.', 'ML domain', '', 'PF02221'),
(126, '2.2.12.03.', 'ADP ribosylation factor', '', 'PF00025'),
(240, '3.4.05.01.', 'Cyclosporin', '', ''),
(128, '2.2.13.01.', 'Gamma-adaptin C-terminal appendage domain-like', '', 'PF02883'),
(129, '2.2.05.01.', 'Plastocyanin/azurin-like', '', 'PF00127'),
(249, '2.4.03.01.', 'Transcriptional factor tubby, C-terminal domain', '', 'PF01167'),
(251, '1.1.14.03.', 'Drug/proton antiporter', '2.A.1.2', 'PF07690'),
(238, '2.4.13.01.', 'OSBP-related proteins', '', 'PF01237'),
(248, '2.1.15.03.', 'Phosphoinositide-binding clathrin adaptor, N-terminal domain', '', 'PF07651'),
(134, '2.2.32.01.', 'Anemone pore-forming cytolysin', '1.C.38', 'PF06369'),
(135, '2.2.22.01.', 'Hydrophobin', '', 'PF06766'),
(398, '1.1.31.01.', 'Vitamin uptake transporter', '2.A.88', 'PF09515'),
(397, '1.2.25.01.', 'Oligosaccharidetransferase', '', 'PF10215'),
(138, '2.2.21.01.', 'Histidine-rich actin-binding protein', '', 'PF06268'),
(139, '2.2.02.01.', 'Prokaryotic proteases', '', 'PF00089'),
(140, '2.2.02.02.', 'Eukaryotic proteases', '', 'PF00089'),
(141, '2.2.02.03.', 'Viral proteases', '', 'PF02907'),
(142, '2.2.03.01.', 'Eukaryotic aspartyl protease', '', 'PF00026'),
(143, '2.2.06.02.', 'Fatty acid binding protein-like (n=10)', '8.A.33', 'PF00061'),
(144, '2.2.07.01.', 'Polyisoprenoid-binding protein', '', 'PF04264'),
(241, '2.3.16.02.', 'Tandem RecA ATPase-like', '3.A.5', 'PF07517'),
(146, '2.2.04.01.', 'Retinal pigment epithelial membrane protein', '', 'PF03055'),
(243, '2.2.20.02.', 'Phosphotyrosine-binding domain', '', 'PF00640'),
(148, '2.2.24.01.', 'Vitelline membrane outer protein-I', '', 'PF03762'),
(149, '2.2.09.01.', 'Ganglioside GM2 activator', '', ''),
(150, '2.2.19.01.', 'Adsorption protein p2', '', 'PF09214'),
(151, '2.2.17.01.', 'Gonadodropin/Follitropin', '', 'PF00236'),
(152, '2.2.35.01.', 'Thiol-activated cytolysin', '1.C.12', 'PF01289'),
(153, '1.2.19.01.', 'Viral glycoprotein', '1.G.3', 'PF01589'),
(154, '2.2.36.01.', 'Cyclotide', '', 'PF03784'),
(371, '1.1.18.07.', 'HCO3- transporter', '2.A.31', 'PF00955'),
(369, '1.2.21.04.', 'Thi4 family', '', 'PF01946'),
(157, '2.2.28.01.', 'Gurmarin', '', ''),
(158, '2.2.29.01.', 'Agouti-related protein', '', 'PF05039'),
(159, '2.2.34.01.', 'Conotoxin', '', 'PF02950'),
(160, '2.2.34.02.', 'Spider toxins', '8.B.6', 'PF02819'),
(161, '2.2.34.03.', 'Insect toxins', '', 'PF08117'),
(162, '2.2.34.04.', 'Albumin 1', '', 'PF08027'),
(163, '2.2.37.03.', 'Short-chain scorpion toxins', '', 'PF00451'),
(164, '2.2.37.04.', 'Plant defensins', '1.C.45', 'PF00304'),
(165, '2.2.30.01.', 'Elafin-like', '', ''),
(166, '2.2.39.02.', 'Dendroaspin', '', 'PF00087'),
(167, '2.2.40.01.', 'Neurotoxin III', '', 'PF08098'),
(168, '2.2.31.01.', 'Fibronectin type II module', '', 'PF00040'),
(169, '2.2.10.01.', 'High potential iron protein', '', 'PF01355'),
(170, '2.3.01.01.', 'Beta-glycanases', '', 'PF02055'),
(171, '2.3.01.02.', 'Family 1 of glycosyl hydrolase', '', 'PF00232'),
(172, '2.3.02.01.', 'Mammalian PLC', '', 'PF00387'),
(173, '2.3.02.02.', 'Bacterial PLC', '', 'PF00388'),
(174, '2.3.04.01.', 'Tyrosine-dependent oxidoreductases', '', 'PF00106'),
(175, '1.2.21.01.', 'Pyridine nucleotide-disulphide oxidoreductase', '', 'PF07992'),
(176, '1.2.21.03.', 'Flavin containing amine oxidoreductase', '', 'PF01593'),
(370, '3.4.07.02.', 'Compstatin', '', ''),
(178, '2.3.14.01.', 'CRAL/TRIO domain', '', 'PF00650'),
(179, '2.3.15.01.', 'ETFP subunits', '', 'PF01012'),
(180, '2.4.10.01.', 'Synapsin domain', '', 'PF02078'),
(181, '2.3.16.01.', 'Shikimate kinase', '', 'PF01202'),
(399, '2.2.12.04.', 'RHO protein GDP dissociation inhibitor', '', 'PF02115'),
(183, '2.3.08.01.', 'Lysophospholipase', '', 'PF01734'),
(184, '2.3.06.01.', 'Acetylcholinesterase-like', '', 'PF00135'),
(185, '2.3.06.02.', 'Mycobacterial antigens', '', 'PF00756'),
(186, '2.3.06.03.', 'Gastric lipase', '', 'PF04083'),
(187, '2.3.06.04.', 'Thioesterases', '', 'PF02089'),
(367, '2.1.37.01.', 'PfEMP1 (Plasmodium falciparum erythrocyte membrane protein)', '', 'PF03011'),
(189, '2.3.06.06.', 'Fungal lipases', '', 'PF01764'),
(190, '2.3.06.07.', 'Bacterial lipase', '', 'PF01674'),
(191, '2.3.06.08.', 'Pancreatic lipase', '', 'PF00151'),
(192, '2.3.06.09.', 'Cutinase-like', '', 'PF01083'),
(193, '2.3.10.01.', 'Glycosyltransferase family 28', '', 'PF03033'),
(194, '2.3.11.01.', 'Ferrochelatase', '', 'PF00762'),
(242, '2.3.12.01.', 'Myotubularin-like phosphatases', '', 'PF02893'),
(196, '2.3.13.01.', 'Glutathione S-transferase', '', 'PF00462'),
(197, '2.4.01.01.', 'GMC oxidoreductases', '', 'PF00732'),
(198, '2.4.02.01.', 'Epoxide Hydrolase', '', 'PF07858'),
(375, '3.1.13.02.', 'Nonstructural polyprotein of Semiliki forest virus, anchor domain', '', ''),
(200, '2.2.25.01.', 'SH2 domain', '', ''),
(201, '2.4.05.01.', 'Sterol carrier protein', '', 'PF02036'),
(202, '2.4.09.01.', 'Synatpobrevin N-terminal domain', '', 'PF00957'),
(244, '2.4.06.02.', 'Phosphatidylinositol transfer protein (PITP)', '', 'PF02121'),
(204, '2.4.06.01.', 'STAR domain', '9.B.64', 'PF01852'),
(205, '2.4.04.01.', 'Neutral sphingomyelinases', '', 'PF03372'),
(206, '2.4.11.01.', 'Crambin-like', '1.C.44', 'PF00321'),
(207, '2.4.12.01.', 'Leucocin-like bacteriocin', '1.C.24', 'PF01721'),
(208, '3.1.07.01.', 'Moricin', '1.C.17', 'PF06451'),
(209, '3.1.08.01.', 'Tachykinin peptides', '', 'PF02202'),
(210, '3.1.09.01.', 'Antimicrobial peptide HP', '', ''),
(211, '3.1.01.01.', 'Neuropeptide Y', '', 'PF00159'),
(212, '3.1.01.02.', 'Glucagon', '', 'PF00123'),
(213, '3.1.01.03.', 'Motilin', '', 'PF04644'),
(214, '3.1.14.06.', 'Transportan', '', ''),
(215, '3.1.01.05.', 'Neurokinin-like', '', ''),
(216, '3.1.01.06.', 'Orexin', '', 'PF02072'),
(217, '3.1.10.01.', 'Poneratoxin', '', ''),
(218, '3.1.02.01.', 'Endothelin-like', '', 'PF00322'),
(219, '3.1.11.01.', 'Alpha-conotoxin', '', 'PF07365'),
(220, '3.1.03.01.', 'Major surface glycoprotein G', '', 'PF00802'),
(221, '3.1.04.01.', 'Synuclein', '1.C.77', 'PF01387'),
(222, '3.1.12.01.', 'Pleurocidin', '1.C.62', 'PF08107'),
(223, '3.2.02.01.', 'Lactoferricin B', '', 'PF00405'),
(224, '3.2.03.01.', 'Hepcidin', '', 'PF06446'),
(225, '3.2.04.01.', 'Cyclic trypsin inhibitor STFI-1', '', ''),
(226, '3.2.05.01.', 'Microcin J25', '9.A.52', ''),
(227, '3.2.05.02.', 'Subtilosin A', '1.C.84', 'PF11420'),
(228, '3.2.06.01.', 'PSP1-like', '', 'PF02425'),
(229, '3.2.07.01.', 'Tricyclic peptide RP71935', '', ''),
(230, '3.2.01.01.', 'Octreotide', '', ''),
(257, '3.1.10.02.', 'Mastoparan family', '1.C.32', 'PF08249'),
(232, '3.4.01.01.', 'Gramicidin S', '', ''),
(233, '3.4.02.01.', 'Actagardine', '', ''),
(234, '3.4.02.02.', 'Mersacidin', '', ''),
(235, '3.4.02.03.', 'Nisin', '1.C.20', 'PF02052'),
(236, '3.4.03.01.', 'Heat-stable enterotoxin', '', ''),
(237, '3.4.04.01.', 'Lipopeptides of Streptomyces', '', ''),
(239, '2.2.41.02.', 'Sea anemone sodium channel inhibitory toxin', '8.B.11', 'PF00706'),
(254, '1.3.15.01.', 'OmpG porin', '1.B.21', 'PF09381'),
(255, '2.3.17.01.', 'ClpP protease', '', 'PF00574'),
(256, '2.3.18.01.', 'Choline/carnitine  O-acyltransferases', '', 'PF00755'),
(258, '3.1.13.01.', 'Nonstructural protein 5a, anchor domain', '', 'PF01506'),
(259, '2.3.16.03.', 'G-proteins', '', 'PF00503'),
(260, '1.1.30.01.', 'Rhomboid proteases', '', 'PF01694'),
(261, '1.2.02.01.', 'T cell receptor transmembrane dimerization domain', '', 'PF11628'),
(262, '1.2.16.01.', 'OMA polysaccharide transporter', '1.B.18', 'PF02563'),
(263, '2.2.08.01.', 'Osmotin, thaumatin-like protein', '', 'PF00314'),
(264, '2.4.04.02.', 'Spider sphingomyelinases', '', ''),
(265, '2.2.15.01.', 'Methuselah ectodomain', '', 'PF06652'),
(266, '2.1.16.01.', 'Extracellular domain of amyloid beta A4 protein', '', ''),
(267, '3.4.02.04.', 'Cinnamycin', '', ''),
(268, '2.2.16.01.', 'Lipoproteins of Mycobacteria', '', 'PF07161'),
(269, '2.1.29.01.', 'Apolipoprotein', '', 'PF01442'),
(270, '1.1.33.01.', 'Disulfide bond oxidoreductase-B (DsbB)', '5.A.2', 'PF02600'),
(271, '3.1.14.01.', 'Apolipoprotein A-I peptide', '', ''),
(272, '1.2.08.01.', 'Cytochrome c of nitrite reductase', '', 'PF03264'),
(273, '1.3.16.03.', 'Porins O and P', '1.B.5', 'PF07396'),
(274, '1.2.04.01.', 'Integrin transmembrane domain', '', 'PF08725'),
(275, '2.2.20.03.', 'Third domain of FERM', '', 'PF09379'),
(276, '1.1.09.02.', 'Binding-protein-dependent transport system', '', 'PF00528'),
(277, '1.1.40.01.', 'MAPEG domain', '', 'PF01124'),
(312, '2.3.10.03.', 'Glycosyltransferase family 9', '', 'PF01075'),
(279, '1.3.17.01.', 'Outer membrane protein insertion porin (OmpIP)', '1.B.20', 'PF08479'),
(280, '1.1.41.01.', 'Magnesium ion transporter-E (MgtE)', '9.A.19', 'PF03448'),
(281, '1.1.42.01.', 'Acid-sensing ion channels', '1.A.6', 'PF00858'),
(282, '1.3.19.01.', 'Outer membrane porin (Opr)', '1.B.25', 'PF03573'),
(283, '1.1.43.01.', 'Bacterial zinc transporters', '2.A.4.1', 'PF01545'),
(365, '1.1.63.01.', 'Phosphotransferase Glucose-Glucoside (Glc) Family', '4.A.1', 'PF02378'),
(285, '1.1.44.01.', 'Site-2 protease', '', 'PF02163'),
(286, '1.2.14.01.', 'Influenza virus matrix protein 2', '1.A.19', 'PF00599'),
(287, '1.2.01.01.', 'Transmembrane domain of protein tyrosine kinase', '', ''),
(288, '1.1.26.02.', 'Prokaryotic pentameric ligand-gated ion channels', '1.A.9', 'PF02932'),
(289, '1.3.21.01.', 'Fimbrial usher porin', '1.B.11', 'PF00577'),
(290, '1.1.47.01.', 'Polysulfide reductase', '5.A.3', ''),
(291, '2.3.06.10.', 'Platelet-activating factor acetylhydrolase family', '', 'PF03403'),
(292, '1.3.22.01.', 'Voltage-dependent anion channel (VDAC) porin', '1.B.8', 'PF01459'),
(311, '2.3.10.02.', 'Glycosyltransferase family 70', '', ''),
(294, '1.1.18.02.', 'Nucleobase-cation symporter 1', '2.A.39', ''),
(295, '1.1.18.03.', 'Solute:sodium symporter', '2.A.21', 'PF00474'),
(296, '1.3.06.01.', 'Major OMP from thermophilic eubacteria', '', ''),
(297, '1.3.09.01.', 'Lipid A deacylase', '', 'PF09982'),
(298, '1.1.18.04.', 'Betaine/carnitine/choline transporters', '2.A.15', 'PF02028'),
(366, '1.2.20.01.', 'Peptidase family M1', '', 'PF01433'),
(300, '1.2.06.01.', 'BNip3 (BCL2/Adenovirus E1B-interacting protein 3)', '1.A.20.', 'PF06553'),
(301, '1.1.09.04.', 'Multidrug resistance exporter (MDR)', '3.A.1.201', 'PF00664'),
(302, '1.1.52.01.', 'Connexin', '1.A.24', 'PF00029'),
(303, '2.3.14.02.', 'SpoIIaa-like protein', '', 'PF11964'),
(304, '1.1.18.05.', 'Amino acid-Polyamine-Organocation (APC) family', '2.A.3', 'PF00324'),
(305, '1.2.18.01.', 'Transglycosylase of penicillin-binding proteins (Glycosyltransferase family 51)', '', 'PF00912'),
(368, '1.2.21.02.', 'FAD dependent oxidoreductase', '', 'PF01266'),
(307, '1.1.53.01.', 'Prokaryotic diacylglycerol kinase', '', 'PF01219'),
(308, '1.2.05.01.', 'SNARE complex', '', 'PF00835'),
(309, '1.1.55.01.', 'Pore-forming haemolysin E', '1.C.10', 'PF06109'),
(310, '1.1.42.02.', 'ATP-gated cation channel', '1.A.7', 'PF00864'),
(313, '2.1.38.01.', 'Corynebacterial porin B', '1.B.41', 'PF11565'),
(314, '3.1.10.03.', 'Lactococcin A family', '1.C.22', ''),
(315, '2.3.19.01.', 'Glycosylating toxin', '1.C.57', 'PF04488'),
(316, '2.2.42.01.', 'Pneumovirus matrix protein', '', 'PF03393'),
(317, '2.1.31.01.', 'Colicin M', '', ''),
(318, '2.2.43.01.', 'OxaA/YidC', '', ''),
(319, '3.2.08.01.', 'BRICHOS domain', '', ''),
(320, '3.2.09.01.', 'Ksi conotoxins', '8.B.4', ''),
(321, '2.3.20.01.', 'CheY-like', '', 'PF01058'),
(322, '2.1.01.04.', 'Plant phospholipase A2', '', ''),
(323, '1.3.10.01.', 'Oligogalactoronate-specific porin (KdgM)', '1.B.35.', 'PF06178'),
(324, '1.2.03.01.', 'CD4', '', 'PF12104'),
(325, '1.2.18.02.', 'Phage lysozyme', '', 'PF00959'),
(326, '1.1.27.02.', 'Formate/Nitrite transporter (FNT) family', '2.A.44.', 'PF01226'),
(327, '1.1.19.02.', 'Urea transporter', '1.A.28.', 'PF03253'),
(328, '1.1.10.01.', 'Glutamate-gated Ion Channel (GIC) family', '1.A.10.', 'PF00060'),
(329, '2.3.16.04.', 'Dynamin', '', 'PF00350'),
(330, '2.3.16.05.', 'ArsA ATPase', '', 'PF02374'),
(331, '3.1.14.02.', 'Lipopeptide detergents', '', ''),
(332, '1.1.57.01.', 'Vitamin K epoxide reductase', '', 'PF07884'),
(333, '1.1.58.01.', 'Signal transduction histidine kinase', '', ''),
(334, '2.3.10.04.', 'Glycosyltransferase family 2', '', ''),
(335, '3.1.15.01.', 'FATC domain', '', 'PF02260'),
(336, '3.1.15.01.', 'Pardaxin', '', 'PF07425'),
(337, '3.1.17.01.', 'Cathelicidin', '1.C.33', 'PF00666'),
(338, '2.1.32.01.', 'Carnocyclin A', '1.C.90', ''),
(339, '3.4.06.01.', 'Indolicidin', '', ''),
(340, '3.4.06.02.', 'Tritrpticin', '', ''),
(341, '3.4.07.01.', 'Trp-rich synthetic peptides', '', ''),
(342, '1.1.11.01.', 'Tellurite-resistance/Dicarboxylate transporter', '2.A.16', 'PF03595'),
(343, '2.1.33.01.', 'DrrA protein', '', ''),
(344, '2.4.14.01.', 'Bacterial conjugation TrbI-like', '3.A.7', 'PF03743'),
(345, '2.1.34.01.', 'DivIVA protein', '', 'PF05103'),
(346, '2.1.35.01.', 'PASCIN (protein kinase C and casein kinase substrate)', '', 'PF00611'),
(347, '1.1.59.01.', 'MerF Mercuric ion uptake family', '9.A.7', 'PF11431'),
(348, '3.1.10.03.', 'Melittin', '1.C.18', 'PF01372'),
(349, '3.1.12.02.', 'Dermaseptin', '1.C.52', 'PF12121'),
(350, '1.1.14.04.', 'Fucose-proton symporter', '2.A.1.7', 'PF07690'),
(351, '1.1.15.02.', 'Heavy metal efflux family', '2.A.6.1', 'PF00873'),
(352, '1.1.60.01.', 'Multi antimicrobial extrusion (MATE) family', '2.A.66.1', 'PF01554'),
(353, '2.2.44.01.', 'PLAT domain', '', 'PF01477'),
(354, '2.1.36.01.', 'Endoplasmic reticulum oxidoreductin', '', 'PF04137'),
(392, '1.2.18.03.', 'Transglycosylase SLT domain', '', 'PF01464'),
(357, '1.2.15.01.', 'TYROBP', '', ''),
(358, '1.1.62.01.', 'Prokaryotic riboflavin transporter', '2.A.87.', ''),
(359, '1.1.14.05.', 'Proton-dependent oligopeptide transporter (POT)', '2.A.17', 'PF00854'),
(360, '1.1.22.03.', 'Potassium transporter (Trk)', '2.A.38', 'PF02386'),
(361, '2.3.06.11.', 'Putative lysophospholipase', '', 'PF12146'),
(362, '1.2.24.01.', 'Fst toxin', '1.C.64', ''),
(363, '1.3.02.01.', 'Opacity porins', '', 'PF02462'),
(364, '1.3.03.01.', 'Outer membrane protein W (OmpW) family', '1.B.39', 'PF03922'),
(373, '3.1.20.01.', 'Delta lysin', '', 'PF05372'),
(374, '3.1.21.01.', 'Hepatitis C virus envelope glycoprotein E1', '', 'PF01539'),
(376, '3.1.19.01.', 'Membrane-binding domain of phosphotransferase IIA component', '', 'PF00358'),
(377, '2.3.09.01.', 'Cytidylyltransferase', '', 'PF01467'),
(378, '3.1.22.01.', 'Scorpion NDBP 5 family', '', ''),
(379, '3.1.23.01.', 'Antifreeze protein, type I', '', ''),
(380, '3.1.14.04.', 'Distinctin', '', ''),
(381, '2.2.41.03.', 'Theta-defensin', '', ''),
(382, '3.1.24.01.', 'Aurein', '', 'PF08256'),
(383, '3.1.14.05.', 'Anticoccidial peptide PW2', '', ''),
(384, '3.2.10.01.', 'Thanatin', '', ''),
(385, '3.1.14.07.', 'Penetratin', '', ''),
(386, '2.3.06.05.', 'Carboxylesterase/Thioesterase 1', '', 'PF02230'),
(387, '2.3.06.12.', 'Carboxylesterase', '', 'PF07859'),
(388, '2.3.06.13.', 'NDRG family', '', 'PF03096'),
(389, '2.3.06.14.', 'Secretory lipase', '', 'PF03583'),
(390, '1.3.01.02.', 'Enterobacterial Ail/Lom protein', '', 'PF06316'),
(391, '1.3.05.01.', 'Lipid A 3-O-deacylase (PagL)', '', 'PF09411'),
(393, '2.3.10.05.', 'Glycosyltransferase family 30', '', 'PF04413'),
(394, '1.1.15.03.', 'SecDF protein-export membrane protein', '3.A.5', 'PF02355'),
(395, '2.1.07.01.', 'Class III cytochrome C', '', 'PF02085'),
(396, '1.1.21.01.', 'Oligosaccharyltransferase', '', ''),
(402, '1.1.32.01.', 'Type IV leader peptidase', '', 'PF01478'),
(403, '1.3.19.02.', 'Alginate export porin', '1.B.13', ''),
(404, '2.2.18.01.', 'Adaptor complexes medium subunit', '', 'PF00928'),
(405, '1.1.34.01.', 'H+ or Na+ translocating NADH Dehydrogenas', '3.D.1', 'PF00361');

-- --------------------------------------------------------

--
-- Table structure for table `membrane`
--

CREATE TABLE `membrane` (
  `id` smallint(4) NOT NULL auto_increment,
  `name` char(50) NOT NULL default '',
  `abbreviation` char(25) NOT NULL default '',
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=27 ;

--
-- Dumping data for table `membrane`
--

INSERT INTO `membrane` (`id`, `name`, `abbreviation`) VALUES
(1, 'Archaebacterial membrane', 'Archaebac.'),
(2, 'Bacterial gram-negative inner membrane', 'Bact. gram-neg inner'),
(3, 'Bacterial gram-negative outer membrane', 'Bact. gram-neg outer'),
(4, 'Eukaryotic plasma membrane', 'Eukaryo. plasma'),
(5, 'Mitochondrial inner membrane', 'Mitochon. inner'),
(6, 'Endoplasmic reticulum membrane', 'Endoplasm. reticulum'),
(7, 'Thylakoid membrane', 'Thylakoid'),
(8, 'Bacterial gram-positive plasma membrane', 'Bact. gram-pos plas.'),
(9, 'Golgi membrane', 'Golgi'),
(10, 'Nuclear inner membrane', 'Nuclear inner'),
(11, 'Peroxisome membrane', 'Peroxisome'),
(12, 'Endosome membrane', 'Endosome'),
(13, 'Vacuole membrane', 'Vacuole'),
(14, 'Vesicle membrane', 'Vesicle'),
(15, 'Viral membrane', 'Viral'),
(16, 'Chloroplast inner membrane', 'Chloroplast inner'),
(17, 'Chloroplast outer membrane', 'Chloroplast outer'),
(19, 'Mitochondrial outer membrane', 'Mitochon. outer'),
(22, 'Bacterial gram-positive acid-fast cell wall', 'Bact. gram-pos cell wall'),
(23, 'Secreted', 'Secreted'),
(24, 'Lysosome membrane', 'Lysosome'),
(25, 'Nuclear outer membrane', 'Nuclear outer'),
(26, 'Synthetic', 'Synthetic');

-- --------------------------------------------------------

--
-- Table structure for table `protein`
--

CREATE TABLE `protein` (
  `id` smallint(4) NOT NULL auto_increment,
  `family_id` smallint(3) NOT NULL default '0',
  `species_id` smallint(3) NOT NULL default '0',
  `membrane_id` tinyint(2) NOT NULL default '0',
  `pdbid` varchar(5) NOT NULL default '',
  `name` varchar(80) NOT NULL default '',
  `resolution` varchar(5) NOT NULL default '',
  `topology` varchar(6) NOT NULL default '',
  `thickness` decimal(4,1) NOT NULL default '0.0',
  `thicknesserror` decimal(4,1) NOT NULL default '0.0',
  `tilt` smallint(3) NOT NULL default '0',
  `tilterror` smallint(3) NOT NULL default '0',
  `gibbs` decimal(5,1) NOT NULL default '0.0',
  `tau` varchar(4) NOT NULL default '',
  `numsubunits` tinyint(2) NOT NULL default '0',
  `numstrands` tinyint(2) NOT NULL default '0',
  `verification` text NOT NULL,
  `comments` text NOT NULL,
  `date_added` date NOT NULL default '0000-00-00',
  PRIMARY KEY  (`id`),
  KEY `species_id` (`species_id`),
  KEY `membrane_id` (`membrane_id`),
  KEY `family_id` (`family_id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=1375 ;

--
-- Dumping data for table `protein`
--

INSERT INTO `protein` (`id`, `family_id`, `species_id`, `membrane_id`, `pdbid`, `name`, `resolution`, `topology`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`, `tau`, `numsubunits`, `numstrands`, `verification`, `comments`, `date_added`) VALUES
(1, 35, 9, 3, '1qjp', 'Outer membrane protein A (OMPA)', '1.65', 'A in', 25.4, 1.5, 11, 1, -29.5, 'N.D.', 1, 8, 'Four interfacial Trp residues of OmpA are located at distances of 8-13 Å from the calculated bilayer center. This is close to 9-10 Å obtained by the parallax method (Kleinschmidt and Tamm 1999). Average tilt angle of TM beta-strands (39°) is slightly smaller than estimated by ATR FTIR (46°)(Ramakrishnan et al. 2005).', 'OmpA is required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. It also serves as a receptor for a number of T-even like phages and can act as a porin with low permeability that allows slow penetration of small solutes.', '2005-09-04'),
(2, 390, 9, 3, '1qj8', 'Outer membrane protein X (OMPX)', '1.90', 'A in', 23.6, 2.8, 12, 5, -30.7, 'N.D.', 1, 8, 'Locations of the hydrophobic boundaries are consistent with  mapping of detergent-embedded areas of OmpX by NMR (Fernandez et al. 2002).', '   OmpX from Escherichia coli promotes adhesion to and entry into mammalian cells. <br/ >   It also has a role in the resistance against attack by the human complement system.<br/ >', '2005-09-04'),
(3, 363, 24, 3, '1p4t', 'Outer membrane protein NspA', '2.55', 'A in', 24.9, 2.4, 22, 3, -42.9, '28', 1, 8, '', 'Pathogenic Neisseria spp. possess a repertoire of phase-variable Opacity proteins that mediate various pathogen--host cell interactions.', '2005-09-04'),
(1006, 286, 52, 15, '3lbw', 'M2 proton channel of Influenza A, closed state', '1.65', 'A out', 31.1, 1.7, 7, 10, -50.5, '', 4, 4, '', '', '0000-00-00'),
(1007, 37, 310, 3, '2x55', 'Plasminogen activator PLA (coagulase/fibrinolysin)', '1.85', 'A in', 25.6, 1.9, 4, 5, -43.9, '', 1, 10, '', '', '0000-00-00'),
(1008, 238, 36, 4, '1zhx', 'Oxysterol-binding protein homolog 4 (KES1)', '1.50', 'in', 1.2, 0.9, 90, 7, -5.0, '', 1, 0, '', '', '0000-00-00'),
(6, 38, 24, 3, '1k24', 'Outer membrane adhesin/invasin OpcA', '2.03', 'A in', 25.4, 1.3, 10, 11, -41.7, '19', 1, 10, '', 'Neisseria species specific OpcA proteins play an important role in meningococcal adhesion and invasion of both epithelial and endothelial cells.', '2005-09-04'),
(7, 39, 24, 3, '1uyn', 'Autotransporter  NalP', '2.60', 'X out', 25.3, 1.3, 8, 8, -47.6, 'N.D.', 1, 12, '', '', '2005-09-04'),
(8, 40, 9, 3, '1qd6', 'Outer membrane phospholipase A', '2.10', 'C in', 23.9, 1.0, 0, 0, -77.2, 'N.D.', 1, 12, 'Membrane boundary planes of monomeric form (1qd6C OPM entry) are consistent with detergent-covered region in crystals of monomeric phospholipase A (Snijder et al. 2003).', '', '2005-09-04'),
(9, 41, 9, 3, '1tly', 'Bacterial Nucleoside Transporter Ts', '3.00', 'A in', 23.4, 1.5, 8, 0, -48.1, '41', 1, 12, '', '', '2005-09-04'),
(10, 42, 9, 3, '1t16', 'Fatty Acid Transporter FadL', '2.60', 'A out', 25.4, 1.3, 6, 7, -58.0, '38', 1, 14, '', '', '2005-09-04'),
(11, 43, 9, 3, '1hxx', 'Porin OmpF', '2.20', 'A in', 25.1, 1.0, 0, 0, -139.8, 'N.D.', 3, 48, 'Results are consistent with experimental hydrophobic thickness of OmpF porin (Keeffe et al. 2000) and hydrophobic boundaries as determined by neutron diffraction in crystals with detergent (Pebay-Peyroula et al. 1995)', '', '2005-09-04'),
(12, 43, 16, 3, '1osm', 'Porin', '3.20', 'A in', 24.0, 1.1, 0, 0, -136.6, 'N.D.', 3, 48, '', '', '2005-09-04'),
(13, 43, 8, 3, '1e54', 'Anion-selective porin', '2.10', 'A in', 25.4, 0.5, 0, 0, -138.8, 'N.D.', 3, 48, '', '', '2005-09-04'),
(14, 88, 30, 3, '2por', 'Porin', '1.80', 'A in', 23.4, 0.6, 0, 0, -114.8, 'N.D.', 3, 48, '', '', '2005-09-04'),
(15, 88, 33, 3, '3prn', 'Porin', '1.90', 'A in', 23.2, 0.5, 0, 0, -127.6, 'N.D.', 3, 48, '', '', '2005-09-04'),
(16, 44, 9, 3, '1af6', 'Maltoporin', '2.40', 'A in', 25.1, 0.7, 0, 0, -117.9, '40', 3, 54, '', '', '2005-09-04'),
(17, 44, 278, 3, '2mpr', 'Maltoporin', '2.40', 'A in', 24.5, 1.0, 0, 0, -109.7, 'N.D.', 3, 54, '', '', '2005-09-04'),
(18, 44, 278, 3, '1a0s', 'Sucrose-specific porin', '2.40', 'P in', 23.8, 1.1, 0, 0, -103.5, 'N.D.', 3, 54, '', '', '2005-09-04'),
(19, 89, 9, 3, '1qfg', 'Ferric hydroxamate uptake receptor FhuA', '2.50', 'A in', 24.7, 1.0, 5, 1, -81.3, '19', 1, 22, 'Average tilt of TM beta-strands (38°) is slightly smaller than estimated by ATR FTIR spectroscopy (44°)(Ramakrishnan et al. 2005).', 'This receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin.', '2005-09-04'),
(20, 89, 9, 3, '1fep', 'Ferric enterobactin receptor FepA', '2.40', 'A in', 24.3, 1.1, 1, 0, -77.2, 'N.D.', 1, 22, 'Locations of hydrophobic boundaries are consistent with site-directed spin-labeling studies (Klug et al. 1997).', '', '2005-09-04'),
(21, 89, 9, 3, '1kmo', 'Outer membrane transporter FecA', '2.00', 'A in', 24.5, 1.2, 3, 0, -69.6, 'N.D.', 1, 22, '', '', '2005-09-04'),
(22, 45, 9, 3, '1nqe', 'Outer membrane cobalamin transporter BtuB', '2.00', 'A in', 23.4, 1.0, 5, 0, -68.8, '22', 1, 22, 'Locations of hydrophobic boundaries are consistent with site-directed spin-labeling studies (Fanucci et al. 2002).', 'Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein tonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins.', '2005-09-04'),
(23, 89, 28, 3, '2iah', 'Pyoverdine Outer Membrane Receptor FpvA', '2.70', 'A in', 24.0, 0.5, 8, 0, -79.7, '15', 1, 22, '', '', '2005-09-04'),
(24, 46, 9, 3, '1ek9', 'Outer membrane protein TolC', '2.10', 'A in', 24.6, 1.4, 0, 2, -56.1, 'N.D.', 3, 12, '', '', '2005-09-04'),
(25, 46, 46, 3, '1yc9', 'Multidrug Resistance (VceC) protein', '1.80', 'A in', 24.6, 1.0, 0, 0, -62.2, 'N.D.', 3, 12, '', '', '2005-09-04'),
(26, 46, 28, 3, '1wp1', 'Drug-Discharge Outer Membrane Protein, OprM', '2.56', 'A in', 24.7, 1.2, 0, 0, -64.0, 'N.D.', 3, 12, '', '', '2005-09-04'),
(27, 47, 39, 23, '7ahl', 'Alpha-hemolysin', '1.89', 'A out', 23.5, 0.9, 0, 1, -49.3, 'N.D.', 7, 14, 'Several Trp residues of alpha-hemolysin (7ahl) are situated in the lipid head group\r\narea according to our results, which is consistent with their accessibility to water-soluble iodide and doxyl probes (Raja et al. 1999) and with locations of lipid head groups determined crystallographically (Galdiero and Gouaux 2004).', '', '2005-09-04'),
(28, 48, 22, 22, '1uun', 'Porin MspA', '2.50', 'A out', 40.7, 2.1, 0, 0, -71.0, 'N.D.', 8, 16, '', '', '2005-09-04'),
(31, 19, 9, 2, '1ots', 'ClC chloride transporter', '2.50', 'A in', 29.7, 0.8, 0, 0, -115.3, 'N.D.', 2, 28, '', '', '2005-09-04'),
(1130, 2, 38, 7, '3pl9', 'Light-harvesting complex CP29', '2.8', 'A in', 29.8, 1.6, 2, 2, -66.6, '', 1, 3, '', '', '0000-00-00'),
(32, 19, 278, 2, '1kpl', 'ClC chloride transporter', '3.00', 'A in', 29.3, 0.8, 2, 1, -128.0, 'N.D.', 2, 28, '', '', '2005-09-04'),
(33, 32, 19, 2, '1yew', 'Particulate Methane Monooxygenase', '2.80', 'B in', 28.2, 0.7, 0, 0, -188.5, 'N.D.', 9, 42, '', '', '2005-09-04'),
(34, 20, 9, 2, '2oau', 'Mechanosensitive channel protein MscS, expanded state', '3.70', 'A out', 31.8, 0.8, 1, 1, -171.3, 'N.D.', 7, 14, '', 'This is an open or another expanded state of the mechanosensor (Bass et al. 2002, Akitake et al. 2005). MscS is inserted in the "monotopic" mode (it does not transverse the bilayer), due to the missing (disordered) N-terminal segment of alpha-helix in each of seven subunits.  Key voltage-sensitive arginines remain outside of the calculated hydrophobic slab, in the lipid head group region.', '2005-09-04'),
(35, 21, 21, 8, '2oar', 'Mechanosensitive channel MscL', '3.50', 'A in', 36.1, 2.2, 0, 0, -142.7, 'N.D.', 5, 10, 'Calculated membrane core boundaries of MscL seem to be consistent with spin-labeling and fluorescence studies (Perozo et al. 2001, Powl et al. 2003, 2005). However, calculated hydrophobic thickness is much larger than obtained in hydrophobic matching studies. ', '', '2005-09-04'),
(36, 16, 9, 2, '1rc2', 'Aquaporin Z', '2.5', 'A in', 29.7, 1.3, 0, 0, -118.7, 'N.D.', 4, 32, '', '', '2005-09-04'),
(37, 16, 9, 2, '1ldf', 'Glycerol uptake facilitator', '2.10', 'A in', 30.1, 0.9, 0, 0, -147.9, 'N.D.', 4, 32, '', '', '2005-09-04'),
(38, 22, 9, 2, '1u7g', 'Ammonia Channel', '1.40', 'A out', 29.8, 1.3, 0, 0, -148.7, 'N.D.', 3, 33, '', '', '2005-09-04'),
(185, 16, 6, 4, '2b6p', 'Aquaporin-0, open state', '2.4', 'A in', 31.1, 1.5, 0, 1, -130.0, '', 4, 32, '', '', '2005-09-25'),
(40, 81, 9, 2, '2cfp', 'Lactose Permease, structure at acidic pH', '3.30', 'A in', 31.1, 1.4, 2, 2, -85.4, '14', 1, 12, 'Results are consistent with chemical modification and spin-labeling studies of lactose permease (Voss et al. 1996, Frillingos et al. 1998, Zhao et al. 1999, Kwaw et al. 2001, Guan et al. 2002, Ermolova et al. 2003, Venkatesan et al. 2000a,b,c, Zhang et al. 2003). Average tilt of TM helices (20°) is smaller than estimated by ATR FTIR (30°)(Le Coutre et al. 1997). Hydrophobic thickness is ~2.5A smaller than was calculated for the lower resolution structure (1pv6).', '', '2005-09-04'),
(41, 24, 9, 2, '1pw4', 'Glycerol-3-Phosphate Transporter', '3.30', 'A in', 31.2, 1.4, 1, 7, -92.5, '35', 1, 12, '', '', '2005-09-04'),
(42, 26, 9, 2, '1l7v', 'ABC transporter BtuCD', '3.20', 'A in', 30.7, 1.1, 0, 1, -121.0, 'N.D.', 2, 22, '', 'Part of the ABC transporter complex btuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (btuD), two transmembrane proteins (btuC) and a solute-binding protein (btuF - not present in the crystal structure).', '2005-09-04'),
(43, 1, 32, 2, '1nkz', 'Light-harvesting complex LH2', '2.00', 'A in', 31.8, 0.6, 0, 0, -193.5, 'N.D.', 18, 18, '', '', '2005-09-04'),
(44, 1, 32, 2, '1ijd', 'Light-harvesting complex LH3', '3.00', 'A in', 29.8, 0.7, 0, 0, -174.6, 'N.D.', 18, 18, '', '', '2005-09-04'),
(45, 1, 35, 2, '1lgh', 'Light-harvesting complex', '2.40', 'A in', 29.7, 0.5, 0, 0, -163.4, 'N.D.', 16, 16, '', '', '2005-09-04'),
(46, 2, 38, 7, '1rwt', 'Light-Harvesting Complex II', '2.70', 'A in', 30.0, 0.7, 0, 0, -154.0, 'N.D.', 3, 9, '', '', '2005-09-04'),
(47, 3, 43, 2, '1eys', 'Photosynthetic reaction center', '2.20', 'L in', 31.6, 1.0, 2, 0, -116.0, '32', 3, 11, '', '', '2005-09-04'),
(48, 3, 31, 2, '1l9b', 'Photosynthetic reaction center', '2.40', 'L in', 31.6, 0.8, 3, 0, -127.3, '32', 3, 11, 'Hydrophobic thicknesses of photosynthetic reaction centers from Rhodopseudomonas sphaeroides are about 30 Ã… (Riegler and Mohwald 1986, Roth et al. 1991) or close to 35 Ã… (Pape et al. 1974).', '', '2005-09-04'),
(49, 3, 34, 2, '1dxr', 'Photosynthetic reaction center', '2.00', 'L in', 31.8, 0.7, 5, 0, -121.8, '25', 3, 11, 'Hydrophobic thicknesses of photosynthetic reaction centers from Rhodopseudomonas viridis are about 25-30 &Aring; (Roth et al. 1989).', '', '2005-09-04'),
(51, 12, 31, 2, '1m56', 'Bacterial cytochrome c oxidase', '2.30', 'A in', 29.6, 1.8, 3, 0, -173.7, 'N.D.', 4, 22, '', '', '2005-09-04'),
(52, 12, 27, 2, '1qle', 'Bacterial cytochrome c oxidase', '3.00', 'A in', 31.7, 1.3, 4, 0, -167.4, 'N.D.', 4, 22, '', '', '2005-09-04'),
(53, 12, 44, 2, '1ehk', 'Bacterial cytochrome c oxidase', '2.40', 'A in', 31.3, 1.2, 8, 0, -114.6, '15', 3, 15, '', '', '2005-09-04'),
(54, 12, 9, 2, '1fft', 'Ubiquinol Oxidase', '3.50', 'A in', 29.5, 0.6, 12, 0, -82.3, 'N.D.', 3, 19, '', '', '2005-09-04'),
(55, 7, 9, 2, '1kqf', 'Formate dehydrogenase', '1.60', 'B out', 33.7, 1.1, 0, 0, -141.9, 'N.D.', 6, 15, '', '', '2005-09-04'),
(56, 8, 9, 2, '1q16', 'Respiratory Nitrate Reductase', '1.90', 'C out', 30.1, 0.9, 0, 0, -126.9, 'N.D.', 2, 10, '', '', '2005-09-04'),
(57, 10, 9, 2, '1kf6', 'Fumarate reductase', '2.70', 'C in', 30.2, 1.2, 14, 2, -65.6, '23', 2, 6, '', 'The calculations are conducted for one half of the complex, since the larger dimer  was assumed to be physiologically not relevant (Iverson et al. 1999).', '2005-09-04'),
(58, 9, 47, 2, '2bs2', 'Fumarate reductase', '1.78', 'C in', 31.2, 1.2, 1, 0, -116.5, 'N.D.', 2, 10, '', '', '2005-09-04'),
(59, 10, 9, 2, '1nek', 'Succinate dehydrogenase', '2.60', 'C in', 32.0, 0.6, 0, 0, -183.5, 'N.D.', 6, 18, '', '', '2005-09-04'),
(60, 17, 41, 8, '1r3j', 'Potassium channel KcsA', '1.90', 'C in', 34.8, 1.2, 0, 0, -111.0, 'N.D.', 4, 12, 'Locations of hydrophobic boundary planes are consistent with spin-labeling (Perozo et al. 1998, Cross et al. 1999, Cross and Hubbell 2002) and hydrophobic matching (Williamson et al. 2002, 2003) studies of KcsA.  Average tilt of TM helices (31°) is consistent with ATR FTIR data (33°)(Le Coutre et al. 1998).', '2k1e and 2kb2 are models of a water-soluble analogue; 1jq1 and 1jq2 are NMR models of a shorter segment', '2005-09-04'),
(61, 17, 40, 8, '1s5h', 'Potassium channel KcsA', '2.20', 'C in', 33.7, 1.3, 0, 1, -111.9, 'N.D.', 4, 12, '', '', '2005-09-04'),
(62, 85, 17, 2, '1xl6', 'Potassium channel Kirbac3.1', '2.85', 'A in', 29.1, 1.5, 0, 0, -71.0, 'N.D.', 4, 12, '', '', '2005-09-04'),
(63, 85, 5, 2, '1p7b', 'Potassium channel Kirbac1.1, closed state', '3.70', 'A in', 33.1, 1.3, 0, 0, -111.9, 'N.D.', 4, 12, '', '', '2005-09-04'),
(64, 14, 2, 2, '1xio', 'Sensory Rhodopsin', '2.00', 'A out', 31.9, 1.5, 13, 4, -63.1, '38', 1, 7, '', '', '2005-09-04'),
(797, 276, 259, 1, '3d31', 'Molybdate transporter ModBC, open state', '3.00', 'C in', 29.8, 1.5, 1, 0, -91.6, '', 2, 12, '', '', '0000-00-00'),
(798, 290, 44, 2, '2vpz', 'Polysulfide reductase', '2.4', 'C out', 29.8, 1.5, 1, 0, -105.2, '', 2, 16, '', '', '0000-00-00'),
(802, 15, 6, 4, '3cap', 'Opsin, retinal-free state, dimer', '2.90', 'A out', 30.8, 1.1, 0, 0, -130.1, '', 2, 14, '', 'The dimer is unstable and possibly non-native. However it fits membrane planar  boundaries.', '0000-00-00'),
(796, 289, 9, 3, '2vqi', 'P pilus usher PapC translocation domain', '3.20', 'A in', 23.1, 1.0, 3, 0, -61.0, '', 1, 24, '', 'Hydrophobic thickness is probably underestimated. It probably will increase in a physiological dimer, with monomers associated in membrane through their polar sides.  ', '0000-00-00'),
(67, 13, 9, 2, '1a91', 'F1F0 ATP synthase subunit c', 'NMR', 'C out', 36.1, 6.7, 21, 3, -21.4, '35', 1, 2, '', '', '2005-09-04'),
(68, 13, 9, 2, '1c17', 'F1F0 ATP synthase', 'NMR', 'A out', 34.6, 1.2, 4, 0, -149.9, '25', 13, 28, '', '1qo1 is crystal structure (3.9A, CA only)', '2005-09-04'),
(69, 13, 15, 2, '1yce', 'F-type Sodium ATPase', '2.40', 'L out', 37.0, 0.5, 0, 0, -104.0, 'N.D.', 11, 22, 'Spatial positions of calculated hydrophobic boundaries are consistent with electron cryo-microsopy data (Vonck et al 2002, Murata et al. 2005). ', 'Hydrophobic boundaries expand when calculated with detergent parameters.', '2005-09-04'),
(70, 13, 10, 2, '2bl2', 'V-type Sodium ATPase', '2.10', 'A out', 35.6, 0.7, 0, 0, -189.6, 'N.D.', 10, 40, '', '', '2005-09-04'),
(72, 28, 20, 1, '1rh5', 'Preprotein translocase SecY', '3.20', 'A in', 29.0, 1.1, 10, 0, -93.4, '14', 3, 12, 'Calculated orientation of hetero-trimeric SecY complex is similar to that in the 2D crystal where this protein forms a dimer of trimers (Breyton et al. 2002). Models of this translocon with bacterial ribosome were generated by MD fitting to EM map (3kcr and 3kc4 PDB entries). ', '', '2005-09-04'),
(73, 17, 1, 1, '1ors', 'Potassium channel KvAP, sensor domain', '1.90', 'C in', 31.5, 2.2, 19, 1, -50.3, '20', 1, 5, '', '', '2005-09-04'),
(74, 17, 1, 1, '1orq', 'Potassium channel KvAP', '3.20', 'C in', 29.3, 1.6, 0, 0, -78.6, 'N.D.', 4, 12, '', 'Three N-terminal helices are misplaced in the crystal structure (Cuello et al. 2004, MacKinnon 2004). They have been excluded during the calculations. Hydrophobic boundaries expand and reach the "paddle" in calculations with detergent solvation parameters.', '2005-09-04'),
(75, 14, 12, 1, '1m0l', 'Bacteriorhodopsin, trimer', '1.47', 'A out', 31.8, 1.1, 0, 1, -121.1, 'N.D.', 3, 21, 'Results are consistent with solid state NMR studies of bacteriorhodopsin (Kamihira et al. 2005). Also, see comments for monomeric bacteriorhodopsin, 1py6.', '', '2005-09-04'),
(76, 14, 23, 1, '1h2s', 'Sensory rhodopsin II', '1.93', 'A out', 30.5, 1.1, 0, 0, -123.4, 'N.D.', 4, 18, 'Accessibilities of eight residues to paramagnetic quenchers (Wegener et al. 2000) are consistent with locations of the calculated membrane boundaries.', '', '2005-09-04'),
(77, 14, 12, 1, '1e12', 'Halorhodopsin', '1.80', 'A out', 31.8, 1.4, 0, 1, -126.7, 'N.D.', 3, 21, '', 'A light-driven chloride pump.', '2005-09-04'),
(78, 14, 13, 1, '1uaz', 'Archaerhodopsin-1', '3.40', 'A out', 31.8, 1.3, 9, 2, -65.3, '35', 1, 7, '', 'Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.', '2005-09-04'),
(79, 6, 7, 7, '1q90', 'Cytochrome b6f', '3.10', 'C in', 31.8, 1.0, 0, 1, -226.4, 'N.D.', 16, 26, '', '', '2005-09-04'),
(758, 90, 14, 6, '2jo1', 'Na,K-ATPase regulatory protein FXYD1 (phospholemman)', 'NMR', 'A out', 29.9, 2.3, 12, 11, -27.7, '', 1, 1, 'A slightly larger tilt angle (15 compare to 8+-3 degree) was obtained in solid-state NMR study (Franzin et al. 2007).', '', '0000-00-00'),
(81, 4, 42, 7, '1jb0', 'Photosystem I', '2.50', 'A in', 31.4, 0.4, 1, 0, -285.7, 'N.D.', 9, 32, '', 'Side-chains in subunit K were reconstructed.', '2005-09-04'),
(202, 96, 68, 23, '1amt', 'Alamethicin', '1.5', 'A out', 10.9, 2.9, 74, 13, -17.1, '', 1, 0, 'This is the calculated membrane binding mode of monomeric alamethicin. At a higher concentration, the peptide forms oligomers that insert to the membrane in a different orientation, depending on the transmembrane potential (Barranger-Mathys and Cafiso 1996, Bechinger et al. 2001, Bak et al. 2001). Transfer energy of the peptide (~ -18.5 kcal/mol per monomer) is overestimated compared to the experimental value (~ -6 kcal/mol per monomer, Lewis and Cafiso 1999), because a significant part of the transfer energy must be spent to fold an alpha-helix from the coil that exists in aqueous solution, prior to insertion of the helix into the membrane.      ', 'The peptide is inserted "monotopically" (it does not cross the bilayer). There are small energetic differences between the surface and transmembrane arrangements of the peptide, especially in the monomeric form. An H-bond between Gln residues in the dimer stabilizes the transmembrane orientation (the crystal structure is a trimer, but third molecule is shifted, which makes incorporation of the entire trimer in the membrane energetically less favorable).  ', '2005-09-25'),
(83, 12, 6, 5, '1v55', 'Mitochondrial cytochrome c oxidase', '1.90', 'A in', 27.8, 0.9, 0, 0, -209.1, 'N.D.', 20, 56, 'Calculated hydrophobic thickness is about 1.5 Ã… smaller than from experimental data (Montecucco et al. 1982).', 'Local thinning of the hydrophobic membrane-spanning area. The calculated thickness might be underestimated.', '2005-09-04'),
(970, 304, 9, 2, '3l1l', 'Arginine/agmatine transporter (AdiC),  substrate-bound', '3.00', 'A in', 28.8, 1.4, 2, 2, -132.0, '', 2, 24, '', '', '0000-00-00'),
(85, 6, 6, 5, '1l0l', 'Cytochrome bc1, mitochondrial', '2.30', 'C in', 30.0, 0.6, 0, 0, -186.6, 'N.D.', 12, 26, '', '', '2005-09-04'),
(86, 6, 36, 5, '3cx5', 'Cytochrome bc1, mitochondrial', '1.90', 'C in', 27.2, 0.6, 0, 0, -173.9, 'N.D.', 10, 24, '', '1kyo - structure with bound cyrochrome c', '2005-09-04'),
(87, 30, 6, 5, '1okc', 'Mitochondrial ADP/ATP carrier', '2.20', 'A out', 29.5, 1.7, 14, 1, -44.6, '13', 1, 6, '', '', '2005-09-04'),
(184, 16, 26, 4, '2b6o', 'Aquaporin-0', '1.9', 'A in', 31.8, 1.4, 0, 0, -143.3, '', 4, 32, '', 'Closed state of the channel. 3m9i includes annular lipids between tetramers.', '2005-09-25'),
(89, 16, 6, 4, '1j4n', 'Aquaporin-1', '2.20', 'A in', 31.8, 1.0, 0, 0, -129.2, 'N.D.', 4, 32, '', '', '2005-09-04'),
(90, 16, 6, 4, '1ymg', 'Aquaporin-0', '2.20', 'A in', 31.3, 1.2, 0, 0, -138.4, 'N.D.', 4, 32, '', '', '2005-09-04'),
(91, 16, 26, 4, '1sor', 'Aquaporin-0', '3.00', 'A in', 31.8, 0.6, 0, 0, -144.9, 'N.D.', 4, 32, '', '', '2005-09-04'),
(92, 23, 45, 4, '2bg9', 'Nicotinic acetylcholine receptor, closed state', '4.00', 'A out', 30.1, 1.1, -3, 0, -119.6, '31', 5, 20, 'The shallow location of Trp452 from the G subunit of the nicotinic acetylcholine receptor (1.4 A° below the calculated hydrophobic boundary) is consistent with fluorescence studies (Chattopadhyay and McNamee 1991).', '', '2005-09-04'),
(93, 34, 14, 4, '1afo', 'Glycophorin A', 'NMR', 'A out', 31.9, 2.8, 5, 6, -43.5, 'N.D.', 2, 2, '', 'Theoretical model of the dimer (1msr, deposited before the experimental study) is nearly identical to the experimental structure. ', '2005-09-04'),
(94, 15, 6, 4, '1gzm', 'Rhodopsin', '2.70', 'A out', 32.2, 1.5, 11, 1, -75.6, '18', 1, 7, 'Results are consitent with X-ray scattering  (Blaurock and Wilkins 1972),\r\nchemical modification (Barclay and Findlay 1984, Davison and Findlay 1986a,b) and electron microscopy (Krebs et al.  2003) studies. Hydrophobic boundaries of rhodopsin expand when calculated with detergent parameters (<a href="http://opm.phar.umich.edu/about.php?subject=experiments">Figure 4</a>), in agreement with results of Hubbell et al. (2003).', '', '2005-09-04'),
(96, 31, 25, 6, '1su4', 'Calcium ATPase, E1-2Ca state', '2.40', 'A in', 29.5, 2.2, 26, 0, -66.4, '10', 1, 10, 'Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998).', 'Similar conformational states are indicated as related PDB entries', '2005-09-04'),
(97, 31, 25, 6, '1wpg', 'Calcium ATPase, E2-Pi state', '2.30', 'A in', 30.6, 1.1, 20, 0, -70.4, '10', 1, 10, 'Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998).', 'Similar conformational states are indicated as related PDB entries', '2005-09-04'),
(98, 31, 25, 6, '1t5s', 'Calcium ATPase, E1-ATP state', '2.60', 'A in', 29.7, 1.6, 22, 1, -58.6, '5', 1, 10, 'Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998).', 'Related PDB entries represent the same conformational state.', '2005-09-04'),
(99, 31, 25, 6, '2zbd', 'Calcium ATPase, E1P-ADP state', '2.40', 'A in', 31.8, 1.4, 22, 2, -70.6, '8', 1, 10, 'Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998).', 'Similar conformational states are indicated as related PDB entries', '2005-09-04'),
(100, 33, 14, 6, '1p49', 'Steryl-sulfatase', '2.60', 'A out', 29.6, 1.1, 23, 0, -34.6, '18', 1, 2, '', '', '2005-09-04'),
(101, 84, 3, 23, '1grm', 'Gramicidin A, head-to-head dimer, right-handed', 'NMR', 'N/A', 23.2, 4.0, 7, 9, -28.1, 'N.D.', 2, 1, 'Results are consistent with the experimental hydrophobic thickness of gramicidin A dimer (Elliott et al. 1983, Harroun et al. 1999) and with its nearly perpendicular arrangement to the membrane, as determined by solid state NMR and IR spectroscopy (Nabedryk et al. 1982, Andronesi et al. 2004, Andersen et al. 2005).  However, ATR FTIR spectroscopy gives a large dynamically averaged tilt angle (Kota et al. 2004).', '', '2005-09-04'),
(145, 70, 14, 23, '1dfn', 'Neutrophil defensin 3', '1.90', 'out', 1.4, 1.3, 87, 15, -3.9, '', 2, 0, '', '', '2005-09-25'),
(144, 154, 50, 23, '1bh4', 'Circulin A', 'NMR', 'out', 3.9, 1.2, 60, 18, -6.6, '', 1, 0, '', '', '2005-09-25'),
(143, 76, 51, 23, '1myn', 'Drosomycin', 'NMR', 'out', 4.6, 1.2, 10, 17, -6.0, '', 1, 0, '', '', '2005-09-25'),
(142, 67, 9, 23, '1jch', 'Colicin E3', '3.02', 'out', 2.8, 0.3, 89, 5, -8.8, '', 4, 0, 'This is a nuclease type colicin that interacts with lipid bilayers (Mosbahi et al. 2006). ', 'Inactivates ribosomes by hydrolyzing 16S RNA in 30S ribosomes at a specific site. Related PDB entries: 1JCH (A/C:1-551), 1E44 (B:456-551), 1UJW (B:314-448). \r\n', '2005-09-25'),
(141, 66, 9, 3, '1qwd', 'Outer membrane lipoprotein Blc', '1.75', 'in', 3.2, 2.0, 80, 15, -4.6, '', 1, 0, 'Cys19 (Lys19) residue may be palmitoylated (UniProt).', 'First 21 residues in the protein are non-native ("cloning artifact").', '2005-09-25'),
(140, 52, 51, 12, '1dvp', 'Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)', '2.00', 'in', 3.0, 0.0, 89, 0, -6.6, '', 2, 0, 'The dimer probably dissociates or slightly change conformation after interaction with membrane because each monomeric unit tends to interact with the bilayer independently. A symmetric binding mode (Mao et al. (2000) and Diraviyam et al. (2003) has a higher energy. Monomeric FYVE domain has a partially different orientation with respect to the membrane (Blatner et al. 2004).', 'Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Each monomeric unit in the dimer includes a VHS and a FYVE domain. Additional membrane-anchoring elements: inositol lipids that are specifically bound to FYVE domains.', '2005-09-25'),
(139, 58, 14, 10, '1jei', 'Inner nuclear membrane protein emerin', 'NMR', 'in', 2.4, 1.3, 88, 17, -3.0, '', 1, 0, '', 'Nuclear transmembrane protein; associated with the inner nuclear membrane and the nuclear matrix.  Includes low-complexity regions and a potential TM helix 223-243,\r\nin addition to this N-terminal domain. Disordered segment 47-53 has been excluded during calculations.', '2005-09-25'),
(138, 57, 52, 15, '1aa7', 'Influenza virus matrix protein M1', '2.08', 'in', 2.6, 0.8, 89, 4, -5.6, '', 2, 0, '', 'This protein forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the ribonucleocapsids.', '2005-09-25'),
(137, 56, 55, 4, '1a8a', 'Annexin V', '1.90', 'in', 2.1, 1.1, 89, 10, -8.9, '', 3, 0, 'Residues that penetrate the membrane core in the calculated orientation of the trimer are L29, T72, A101, W185 and A260. Substitutions of T72 and W185 by Ala decrease membrane binding affinity (Campos et al. 1998). Also, substitutions of S144, S228, and S303 by Lys reduce binding affinity (these residues are located just beyond the calculated hydrophobic boundary, and their side-chains are directed toward the bilayer). ', 'This protein undergoes major conformational changes upon association with membranes.', '2005-09-25'),
(136, 55, 14, 19, '1g5m', 'Apoptosis regulator Bcl-2', 'NMR', 'out', 4.2, 1.4, 33, 11, -6.6, '', 1, 0, 'This structure includes residues 3-207.  Missing C-terminal segment includes potential TM helix 212-233. The protein undergoes major conformational changes upon association with membranes. ', 'Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif (residues 10-30), has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity. Structure without BH4 motif is 1ysw (residues 45-207). 1gjh is a different isoform.  \r\n', '2005-09-25'),
(135, 75, 49, 23, '2sn3', 'Neurotoxin 3', '1.20', 'out', 4.0, 1.3, 74, 17, -5.5, '', 1, 0, '', 'Binds to sodium channels and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission.', '2005-09-25'),
(134, 69, 54, 23, '1kxi', 'Cardiotoxin-A5', '2.19', 'out', 6.3, 1.1, 69, 15, -10.5, '', 1, 0, '', 'Low cytotoxin activity. Displays poor hemolytic activity but is proficient at inducing aggregation and fusion of sphingomyelin vesicles. The calculated orientation is approximately consistent with computational results of Dubovskii et al. (2002). ', '2005-09-25'),
(133, 73, 14, 5, '1d3h', 'Dihydroorotate dehydrogenase', '1.80', 'in', 3.4, 0.8, 55, 6, -10.1, '', 1, 0, '', 'In bacteria, this enzyme is located on the inner side of the cytosolic membrane. In some yeasts, it is a cytosolic protein, while in other eukaryotes it is found in the mitochondria.', '2005-09-25'),
(132, 61, 14, 4, '1czs', 'C2 domain of coagulation factor V', '1.90', 'out', 3.4, 1.6, 13, 15, -6.2, '', 1, 0, 'W26, W27, L79, and S80 penetrate the bilayer core in the calculated orientation. W26 and W27 are important for membrane binding according to mutagenesis studies (Kim et al. 2000). Residues are numbered as in PDB file.', '', '2005-09-25'),
(131, 83, 56, 23, '2mag', 'Magainin 2', 'NMR', 'out', 10.1, 0.9, 81, 14, -13.7, '', 1, 0, 'The alpha-helix of magainin is parallel to the membrane surface, with its nonpolar side (F5, L6, F16, I20) buried in the hydrophobic region of the membrane (Matsuzaki et al. 1994, Marassi et al. 2000). The transfer energy is strongly overestimated (~ -8 kcal/mol in the experiment, Wieprecht et al. 1999), because part of the transfer energy must be spent to fold an alpha-helix from a coil in aqueous solution, prior to insertion of the helix into membrane.     ', 'Antimicrobial peptide that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. This peptide forms oligomeric ion channels in membranes. It also forms a dimer (1dum). Side-chain conformers of this NMR model were optimized.', '2005-09-25'),
(130, 72, 55, 6, '1mt5', 'Fatty acid amide hydrolase', '2.80', 'in', 11.1, 0.2, 89, 0, -21.9, '', 2, 0, 'Consistent with membrane-association mode proposed by Bracey et al. (2002). The protein has TM helix 9-29 (Patricelli et al. 1998), in agreement with this orientation.', '', '2005-09-25'),
(129, 176, 14, 19, '1s3e', 'Monoamine oxidase B, monomer', '1.60', 'out', 7.3, 0.6, 37, 1, -14.2, '', 2, 0, '', 'Monomer, homo- or heterodimer. Enzymatically active as monomer. Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAO-B preferentially degrades benzylamine and phenylethylamine.', '2005-09-25'),
(128, 50, 48, 8, '2sqc', 'Squalene-hopene cyclase', '2.00', 'in', 7.4, 0.5, 90, 1, -27.8, '', 2, 0, 'Bacterial cell membrane; peripheral membrane protein. Crystallization with detergent (OCTYLTETRAOXYETHYLENE).', 'Catalyzes the cyclization of squalene into hopene.', '2005-09-25'),
(127, 49, 53, 6, '1cx2', 'Prostaglandin H2 synthase-2 (cyclooxygenase)', '3.00', 'out', 9.7, 0.4, 89, 3, -37.4, '', 2, 0, 'Crystallization with detergent (N-OCTYL-beta-D-GLUCOPYRANOSIDE).', 'May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity.', '2005-09-25'),
(150, 51, 55, 4, '1h0a', 'Epsin-1 (ENTH domain)', '1.70', 'in', 3.2, 1.1, 39, 19, -5.3, '', 1, 0, 'N-terminal helix (residues L6 and M10) penetrates the hydrophobic core of lipid bilayers in the presence of inositol lipids (Stahelin et al. 2003), which is consistent with the calculated orientation (L6, M10, I13 and V14 are buried in the hydrophobic interior of the membrane). Maximal membrane binding affinity is -10.5 kcal/mol (Stahelin et al. 2003), which is higher than the calculated transfer energy due to specific binding of phosphoinositides. ', 'Binds to membranes enriched in phosphatidylinositol-4,5-biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.\r\nAdditional membrane-anchoring elements: inositol lipids that are specifically bound to the protein. N-terminal domain of epsin-4 (1xgw) was also identified as membrane-associated though its N-terminus in calculations. ', '2005-09-25'),
(153, 63, 14, 4, '1rlw', 'Cytosolic phospholipase A2, group IVA', '2.40', 'in', 6.4, 1.9, 57, 17, -7.8, '', 1, 0, 'Side-chains of residues A34, F35, G36, M38, L39, Y96, V97 and M98 penetrate into  the hydrophobic core of the membrane in the calculated orientation (Y96 is in the interfacial region). Membrane depth parameters of spin-labeled cysteines were positive only in these positions (Frazier et al. 2002, Malmberg et al. 2003), cosistently with mutagenenesis/binding studies of Bittova et al. (1999). Depth parameters were close to zero for residues K32 and N95, which are located just beyond the calculated hydrophobic boundaries. Two calcium ions are located at the distances of 5.8 and 7.2 A beyond the hydrophobic boundary, i.e. 0.8 and 2.2 A, respectively, beyond the level of bulk lipid phosphates. This is consistent with positioning of these ions approximately at the level of lipid phosphates in X-ray reflectivity and EPR studies (Malkova et al. 2005, Malmberg and Falke 2005). Maximal membrane binding affinity is about -11 kcal/mol (Bittova et al. 1999, Stahelin and Cho 2001) or -6.4 kcal/mol (Nalefski et al. 2001).', 'Orientation of this C2 domain changes little when it associates with catalytic domain (see 1cjy).', '2005-09-25'),
(154, 63, 55, 4, '1dsy', 'Protein kinase C alpha, complex with phosphatidyl serine', '2.60', 'in', 0.9, 1.5, 18, 16, -3.0, '', 1, 0, 'Side-chains of P188, N189, and T250 penetrate the hydrocarbon core. Residues in positions 188 and 250 were not spin-labeled. Residues N189, R249 and R252 were shown to be the closest to the membrane (positive depth parameters after substitutions of the corresponding residues by spin-labeled cysteines) (Kohout et al. 2003, Table 3). Two calcium ions are located at the distances of 5.3 and 5.9 A beyond the hydrophobic boundary, i.e. 0.3 and 0.9 A, respectively, beyond the level of bulk lipid phosphates. This is consistent with EPR studies (Malmberg and Falke 2005). Maximal membrane binding affinity is -6.7 kcal/mol (Kohout et al. 2003), -10.8 kcal/mol (Stahelin and Cho 2001), or -12.8 kcal/mol (Stahelin et al. 2003). This is higher than the calculated transfer energy (-0.6 kcal/mol without the ligand) due to specific binding of the phosphatidyl serine. ', '', '2005-09-25'),
(155, 63, 55, 4, '1rsy', 'Synaptotagmin-1, C2A domain (Calcium free)', '1.90', 'in', 2.5, 1.6, 24, 17, -4.1, '', 1, 0, 'Side-chains of residues in positions M173, G174, and F234 penetrate into the hydrophobic core of the membrane in the calculated orientation. Experimental membrane depth parameters are positive in positions 174 and 234 (only) but negative in position 173 (Table 2 in Frazier et al. 2003). However, residue M173 was identified as most important for membrane binding by Gerber et al. (2002).', 'N-terminal residues originating from expression vector (9F-17F) have been removed during calculations. ', '2005-09-25'),
(156, 63, 55, 4, '1byn', 'Synaptotagmin-1, C2A domain (Calcium bound)', 'NMR', 'in', 3.8, 1.6, 32, 19, -4.7, '', 1, 0, 'Side-chains of residues in positions M173, G174, and F234 penetrate into the hydrophobic core of the membrane in the calculated orientation. Experimental membrane depth parameters are positive in positions 174 and 234 (only) but negative in position 173 (Frazier et al. 2003). However, residue M173 has been identified as most important for membrane binding by Gerber et al. (2002). \r\nThree calcium ions are located at the distances of 6.1, 6.3 and 3.3 A beyond the hydrophobic boundary, i.e. 1.1, 1.3 and -1.7 A, respectively, from the level of bulk lipid phosphates. This is consistent with EPR studies (Malmberg and Falke 2005). Maximal membrane binding affinity: -6.5 kcal/mol (Nalefski et al. 2001).', '', '2005-09-25'),
(157, 63, 55, 4, '1uov', 'Synaptotagmin-1, C2B domain (Calcium bound)', '1.65', 'in', 1.7, 1.8, 36, 13, -3.7, '', 1, 0, 'Side-chains of residues V304, G305, I367 and G368 penetrate into the hydrophobic core of the membrane in the calculated orientation. Experimental membrane depth parameters are close to zero (although negative) for spin-labeled cysteines in positions 305 and 367 (Rufener et al. 2005).', '', '2005-09-25'),
(158, 65, 55, 4, '1mai', 'PH domain of phospholipase C delta 1', '1.90', 'in', 15.0, 1.8, 22, 14, -17.8, '', 1, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Spatial positions of the protein calculated with and without the bound lipid are almost identical. Transfer energy was calculated without contribution from the bound lipid. Experimental membrane binding affinity is -6.2 kcal/mol in the presence of PIP2 and less than -4 kcal/mol without PIP2 (Wang et al. 1999).', 'This orientation is in agreement with results of computational modeling based on electrostatic interactions (Singh and Murray 2003). However, PH domain penetrates by ~15A deeper into the membrane according to our results: nonpolar residues are inserted in the membrane hydrocarbon core, not in the head group region.', '2005-09-25'),
(159, 74, 14, 12, '1h6h', 'PX domain of NADH oxidase (p40phox),  ligand-bound', '1.70', 'in', 3.9, 2.0, 55, 14, -6.0, '', 1, 0, 'Residues embedded in the hydrophobic interior of the membrane are F35, Y94 and V95. This is consistent with the important role of F35, Y94 and V95 in interactions with lipid bilayers (Stahelin et al. 2003). This orientation was calculated including atoms of the bound ligand (inositol lipid). Orientation of apo-protein is slightly different (V97 of apo-protein also penetrates the membrane core). Maximal membrane binding affinity is -12.6 kcal/mol (Stahelin et al. 2003), which is higher than calculated transfer energy of the apo-protein (-4.5 kcal/mol) due to strong specific binding of phosphoinositide.', 'Subcellular localization of PX domains - see Cho and Stahelin (2005).', '2005-09-25'),
(160, 77, 36, 13, '1vfy', 'FYVE domain of Vps27 protein', '1.15', 'in', 3.7, 1.8, 24, 19, -4.2, '', 1, 0, 'This FYVE domain strongly associates with lipid bilayers in the presence of PtdIns(3)P lipids (Blatner et al. 2004).  L185 and L186 penetrate the hydrophobic slab according to our results. This is consistent with binding and mutagenesis studies: mutations of L185 and L186 reduced the monolayer penetration, while mutations of K181 and K182 had only a slight effect (Stahelin et al. 2002).  Membrane binding affinity of an isolated FYVE domain is -10.5 kcal/mol (Blatner et al. 2004), which is higher than the calculated transfer energy due to specific binding of PtdIns(3)P.', 'This orientation is in agreement with results of computational modeling of FYVE domains based on the electrostatic interactions (Diraviyam et al. 2003). However, FYVE domain penetrates by ~10A deeper into the membrane according to our results: nonpolar residues are inserted in the membrane hydrocarbon core, not in the head group region.', '2005-09-25'),
(161, 78, 53, 4, '1ptr', 'C1 domain of protein kinase C delta', '2.20', 'in', 2.1, 1.7, 29, 16, -5.4, '', 1, 0, 'The protein penetrates deeper into the membrane core when bound to the acetyl phorbol ligand, according to the calculations (this model). M239, S240, P241, F243, L250, W252, G253, L254 and V255 are buried in the membrane core in the ligand-bound state are, consistent with the important role of L250, W252 and L254 in protein-lipid interactions (Wang et al. 2001). ', 'Protein kinase C delta is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC also serves as the receptor for phorbol esters,\r\na class of tumor promoters (13-acetylphorbol in the PDB structure).  ', '2005-09-25'),
(162, 86, 14, 6, '1zll', 'Phospholamban', 'NMR', 'A in', 30.5, 1.4, 0, 2, -76.0, '', 5, 5, 'Average tilt (21°) of TM helices is slightly smaller than estimated by ATR FTIR (28±6°)(Arkin et al. 1995).', 'This is structure of full-length peptide. All models of the pentamer (experimental: 1xnu, 1zll, and 2hyn and theoretical: 1k9n,1pln, 1psl, and 1kch) represent essentially the same structure of transmembrane alpha-bundle, with CA atom rmsd of 1-2 A (1psl was apparently the first model deposited to the PDB).  Experimental models of monomeric helix: 1n7l (in detergent),1plp (TFE), 1fjp and 1fjk; 1n7l (detergent, rabbit), 2kb7 (solution + solid state NMR).', '2005-09-25'),
(164, 87, 9, 2, '1zcd', 'Sodium/proton antiporter 1 (NhaA)', '3.4', 'A in', 28.4, 1.4, 2, 2, -78.6, '', 1, 14, 'Accessibilities of two residues to paramagnetic quenchers (Hilger et al. 2005) are consistent with locations of the calculated membrane boundaries.', 'This protein forms a non-physiological head-to-head dimer.', '2005-09-25'),
(165, 17, 55, 4, '2a79', 'Potassium channel Kv1.2.', '2.9', 'B in', 29.8, 1.5, 0, 0, -147.0, '', 4, 28, '', '', '2005-09-25'),
(166, 82, 58, 2, '2a65', 'Leucine transporter LeuT, substrate-bound', '1.65', 'A in', 29.8, 0.5, 0, 0, -157.9, '', 2, 28, '', '', '2005-09-25'),
(167, 10, 57, 5, '1zoy', 'Succinate dehydrogenase (mitochondrial respiratory complex II)', '2.4', 'C in', 29.8, 1.1, 3, 6, -52.6, '', 2, 6, '', '', '2005-09-25'),
(168, 12, 27, 2, '1ar1', 'Bacterial cytochrome c oxidase', '2.7', 'A in', 31.9, 1.5, 7, 0, -108.4, '', 2, 14, '', '', '2005-09-25'),
(169, 14, 23, 1, '1h68', 'Sensory rhodopsin II, monomer', '2.1', 'A out', 30.3, 1.5, 15, 2, -60.0, '', 1, 7, '', '', '2005-09-25'),
(170, 14, 12, 1, '1py6', 'Bacteriorhodopsin, monomer', '1.8', 'A out', 29.6, 2.2, 24, 8, -59.7, '', 1, 7, 'Results are consistent with studies of hydrophobic thickness (Piknova et al. 1993, Dumas et al. 1999) and site-directed spin labeling of bacteriorhodopsin (Altenbach et al. 1990, 1994, Greenhalgh et al. 1991) under conditions when the protein is monomeric.', 'Monomeric forms of bacteiorhodopsin are indicated as related PDB entries.', '2005-09-25'),
(171, 16, 14, 4, '1h6i', 'Aquaporin-1', '3.54', 'A in', 30.8, 1.1, 0, 0, -135.6, '', 4, 32, '', 'Hydrophobic thickness is underestimated, perhaps due to a relatively poor quality of this EM-based structure.  Some loops are turned "inside out", as can see from comparison with the higher resolution structure of bovine homologue (1j4n).\r\n ', '2005-09-25'),
(172, 37, 9, 3, '1i78', 'Outer membrane protease OmpT', '2.6', 'A in', 26.5, 1.6, 5, 6, -46.9, '', 1, 10, '', 'This aspartic peptidase is distinct from trypsin-like proteases becase it cleaves polypeptides between two basically-charged amino acids. The enzyme is sensitive to the serine protease inhibitor diisopropylfluoro-phosphate, to divalent cations such as Cu2+, Zn2+ and Fe2+, and its activity decreases at lower temperatures. OmpT is not a a serine protease with Ser(99) and His(212) as active site residues, but rather a aspartic endopeptidase whose activity is also strongly dependent on Asp(83) and Asp(85). Both acids may function in binding of the water molecule and/or oxyanion stabilisation.', '2005-09-25'),
(173, 6, 6, 5, '1pp9', 'Cytochrome bc1, mitochondrial', '2.1', 'C in', 29.8, 0.3, 6, 0, -179.3, '', 10, 26, '', '', '2005-09-25'),
(174, 22, 59, 1, '2b2f', 'Ammonium transporter Amt-1', '1.72', 'A out', 28.9, 0.7, 0, 0, -152.5, '', 3, 33, '', '', '2005-09-25'),
(175, 14, 13, 1, '1vgo', 'Archaerhodopsin-2', '2.5', 'A out', 30.7, 1.3, 18, 2, -73.1, '', 1, 7, '', 'Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.', '2005-09-25'),
(176, 89, 28, 3, '1xkw', 'Fe(III)-pyochelin receptor FptA', '2.0', 'A in', 24.8, 1.0, 5, 4, -84.3, '', 1, 22, '', '', '2005-09-25'),
(177, 43, 9, 3, '1pho', 'Phosphoporin (PhoE)', '3.0', 'A in', 24.1, 1.2, 0, 0, -134.1, '', 3, 48, '', '', '2005-09-25'),
(178, 31, 25, 6, '2agv', 'Calcium ATPase, E2 state (Ca-free)', '2.4', 'A in', 29.7, 2.2, 20, 2, -61.5, '', 1, 10, 'Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998).', 'Similar conformational states are indicated as related PDB entries', '2005-09-25'),
(1033, 13, 312, 8, '2x2v', 'F1F0 ATP synthase', '2.50', 'A out', 35.3, 1.2, 0, 0, -137.7, '', 13, 26, '', '', '0000-00-00'),
(1034, 348, 83, 23, '2mlt', 'Melittin', '2.00', 'out', 15.0, 1.0, 65, 11, -12.0, '', 1, 0, '', '', '0000-00-00'),
(1035, 349, 314, 23, '2k9b', 'Dermatistinctin K', 'NMR', 'out', 4.6, 1.0, 90, 10, -7.0, '', 1, 0, '', '', '0000-00-00'),
(180, 17, 1, 1, '2a0l', 'Potassium channel KvAP', '3.9', 'A out', 29.5, 1.1, 0, 0, -100.0, '', 4, 12, '', 'Three N-terminal helices are misplaced in the crystal structure (Cuello et al. 2004, MacKinnon 2004). They have been excluded during the calculations. The "paddle" penetrate the bilayer core, but key arginines remain in the lipid head group area.', '2005-09-25'),
(186, 16, 60, 1, '2f2b', 'Aquaporin Aqpm', '1.7', 'A in', 29.0, 0.8, 0, 0, -129.9, '', 4, 32, '', '', '2005-09-25'),
(187, 13, 61, 8, '1wu0', 'F1F0 ATP synthase subunit c', 'NMR', 'A out', 31.9, 2.7, 44, 1, -23.2, '', 1, 2, '', '', '2005-09-25'),
(188, 86, 14, 6, '1jdm', 'Sarcolipin', 'NMR', 'A in', 29.5, 2.8, 3, 18, -27.3, '', 1, 1, 'Consistent with the solid-state NMR determined orientation (Mascioni et al. 2002).', 'Sarcolipin and phospholamban are weakly homologous. The original model of sarcolipin in micelles (1jdm) has been optimized. This is full-length peptide.', '2005-09-25'),
(189, 91, 62, 2, '2bbj', 'CorA magnesium transporter', '3.9', 'A in', 29.9, 1.0, 0, 0, -80.8, '', 5, 10, '', 'This lower resolution model is kept as a representative because it has a better defined structure of loops at the extracellular side (these loops define positition of the hydrophobic boundary) ', '2005-09-25'),
(190, 176, 55, 19, '1o5w', 'Monoamine oxidase A', '3.2', 'A out', 31.4, 3.4, 20, 3, -23.1, '', 2, 2, 'Membrane binding mode is similar to that proposed by Ma et al. (2004). Crystallization with detergent (DIMETHYLDECYLPHOSPHINE OXIDE/FOSCHOLINE-12).', 'Monomer, homo- or heterodimer. Enzymatically active as monomer. Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAO-A preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.', '2005-09-25'),
(191, 92, 63, 23, '1ifi', 'Capsid protein G8P', '3.3', 'A out', 36.8, 0.2, 0, 0, -69.8, '', 15, 15, '', '', '2005-09-25'),
(192, 92, 64, 23, '1ifk', 'Capsid protein G8P', '5.0', 'A out', 31.8, 0.7, 0, 0, -83.5, '', 15, 15, '', '', '2005-09-25'),
(193, 93, 65, 23, '1ifp', 'Capsid protein G8P', '3.1', 'A out', 34.2, 0.1, 6, 6, -57.6, '', 12, 12, '', '', '2005-09-25'),
(194, 93, 66, 23, '1hgz', 'Capsid protein G8P', '2.4', 'A out', 29.2, 2.3, 8, 7, -46.5, '', 15, 15, '', '', '2005-09-25'),
(195, 94, 67, 23, '2pil', 'Fimbrial protein, type IV pilin, monomer', '2.6', 'A in', 30.7, 4.1, 22, 10, -24.4, '', 1, 1, '', 'The monomeric unit of the pilin probably spans the lipid bilayer, prior to its assembly into pilus (Craig et al. 2006).\r\n ', '2005-09-25'),
(197, 16, 38, 4, '1z98', 'Aquaporin Sopip2, closed state', '2.1', 'A in', 28.1, 2.2, 0, 0, -117.2, '', 4, 32, '', '', '2005-09-25'),
(196, 95, 57, 23, '1spf', 'Pulmonary surfactant-associated protein C', 'NMR', 'A in', 31.7, 3.3, 21, 0, -32.0, '', 1, 1, 'This peptide forms a hydrophopbic alpha-helix, with a transmembrane orientation (Vandenbussche et al. 1992).', 'Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. This is full-length peptide.', '2005-09-25'),
(198, 16, 38, 4, '2b5f', 'Aquaporin Sopip2, open state', '3.9', 'A in', 29.4, 1.1, 2, 2, -113.0, '', 4, 32, '', '', '2005-09-25'),
(199, 10, 11, 5, '1yq3', 'Succinate dehydrogenase (mitochondrial respiratory complex II)', '2.2', 'C in', 29.6, 1.8, 4, 6, -56.7, '', 2, 6, '', '', '2005-09-25'),
(200, 9, 47, 2, '2bs3', 'Fumarate reductase', '2.2', 'C in', 31.2, 1.4, 2, 1, -117.8, '', 2, 10, '', '', '2005-09-25'),
(203, 96, 69, 23, '1ee7', 'Chrysospermin C', 'NMR', 'A in', 9.8, 2.3, 82, 12, -12.2, '', 1, 0, 'Studied in detergent (DPC).', 'The peptide was inserted "monotopically" (it does not cross the bilayer). There are small energetic differences between the surface and transmembrane arrangements of the peptide. The shown arrangement has the lowest transfer energy.', '2005-09-25'),
(794, 15, 255, 4, '2z73', 'Squid rhodopsin dimer', '2.50', 'A out', 32.9, 1.0, 0, 1, -143.3, '', 2, 14, '', '', '0000-00-00'),
(795, 16, 256, 4, '3c02', 'Aquaglyceroporin', '2.05', 'A in', 30.4, 1.3, 0, 0, -137.4, '', 4, 32, '', '', '0000-00-00'),
(205, 30, 6, 5, '1ym6', 'Mitochondrial ADP/ATP carrier', 'NMR', 'A out', 31.7, 1.5, 12, 1, -44.8, '', 2, 7, '', '', '2005-09-25'),
(206, 364, 9, 3, '2f1v', 'Outer membrane protein W', '2.7', 'A in', 25.4, 1.4, 10, 3, -38.3, '', 1, 8, '', 'This protein may form the receptor for S4 colicins in Escherichia coli.', '2005-09-25'),
(207, 16, 55, 4, '2d57', 'Aquaporin-4', '3.2', 'A in', 29.8, 1.1, 0, 0, -126.2, '', 4, 32, '', '', '2005-09-25'),
(208, 17, 70, 8, '2ahy', 'NaK potassium channel, closed state', '2.4', 'A in', 29.5, 0.7, 0, 1, -105.7, '', 4, 12, '', '', '2005-09-25'),
(210, 98, 42, 7, '1c6s', 'Cytochrome c6', 'NMR', 'out', 0.4, 1.7, 89, 16, -1.3, '', 1, 0, '', 'Functions as an electron carrier between membrane-bound cytochrome b6f and photosystem I in oxygenic photosynthesis.  Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(211, 98, 86, 7, '1f1f', 'Cytochrome c6', '2.7', 'out', 4.8, 1.6, 80, 15, -3.5, '', 1, 0, '', 'Functions as an electron carrier between membrane-bound cytochrome b6f and photosystem I in oxygenic photosynthesis. Membrane-binding site participates in protein-protein interaction.', '2006-03-17');
INSERT INTO `protein` (`id`, `family_id`, `species_id`, `membrane_id`, `pdbid`, `name`, `resolution`, `topology`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`, `tau`, `numsubunits`, `numstrands`, `verification`, `comments`, `date_added`) VALUES
(212, 98, 116, 7, '1ls9', 'Cytochrome c6', '1.3', 'out', 4.1, 1.0, 70, 14, -2.9, '', 1, 0, '', 'Functions as an electron carrier between membrane-bound cytochrome b6f and photosystem I in oxygenic photosynthesis. Predicted membrane-binding site is also involved in protein-protein association.', '2006-03-17'),
(213, 98, 178, 2, '1a8c', 'Cytochrome c552', 'NMR', 'out', 2.7, 1.0, 80, 11, -4.7, '', 1, 0, '', 'Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase. Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(214, 98, 144, 5, '1hrc', 'Mitochondrial cytochrome c', '1.9', 'out', 2.1, 1.0, 80, 16, -2.6, '', 1, 0, 'Calculated orientation is similar for all water-soluble cytochromes c. It is the same as an orientation of the closely related cytochrome c2 in the photosynthetic reaction center from Rhodobacter sphaeroides (PDB entry 1l9b). Calculated orientation corresponds to the binding mode proposed by Rytomaa and Kinnunen (1995), but differs from the binding mode proposed by Brown and Wuthrich (1977). Also, calculated orientation is in agreement with the following data: (a) membrane-binding side includes K86, K87, and K72 residues (Kostrewa et al. 2000); (b) cytochrome c inserts into lipid bilayer up to the level of initial methylenes (Domanov et al. 2005); and (c) heme is accessible to lipid phosphates (Pinheiro and Watts 1994). Experimental membrane binding affinity varies from -3.3 to -5.3 kcal/mol (0.1 M KCl) depending on the type of anionic lipid (Rietveld et al. 1983, Sankaram and Marsh  1993).  Note that more remotely related cytochromes c from mitochondrial bc1 complexes (subunits D from 1kb9, 1pp9, etc.) have an additional C-terminal TM helix and adopt an opposite orientation with respect to the membrane. These cytochromes have a distinctly differnt arrangement of positively charged residues, which follows the negatively charged membrane surface. ', 'Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. ', '2006-03-17'),
(215, 98, 34, 2, '1co6', 'Cytochrome c2', '1.6', 'out', 1.4, 0.7, 78, 10, -3.3, '', 1, 0, '', 'Cytochrome c2 is found mainly in purple, nonsulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some nonphotosynthetic bacteria. Predicted membrane-binding site is also involved in protein-protein association.', '2006-03-17'),
(216, 98, 203, 2, '1kx7', 'Mono-heme c-type cytochrome ScyA', 'NMR', 'out', 1.8, 1.1, 72, 12, -3.2, '', 1, 0, '', 'Predicted membrane-binding site is also involved in protein-protein association.', '2006-03-17'),
(217, 98, 192, 2, '1cor', 'Cytochrome c551', 'NMR', 'out', 2.6, 1.1, 73, 12, -6.1, '', 1, 0, '', 'Electron donor for cytochrome cd1 in nitrite and nitrate respiration. Predicted membrane-binding site is also involved in protein-protein association.', '2006-03-17'),
(218, 98, 28, 2, '451c', 'Cytochrome c551', '1.6', 'out', 1.4, 0.9, 85, 10, -5.4, '', 1, 0, '', 'Electron donor for cytochrome cd1 in nitrite and nitrate respiration. Predicted membrane-binding site is also involved in protein-protein association.', '2006-03-17'),
(219, 99, 192, 2, '1m70', 'Cytochrome c4', '1.2', 'out', 5.4, 0.8, 67, 14, -5.6, '', 1, 0, '', 'Diheme, high potential cytochrome c believed to be an intermediate electron donor to terminal oxidation systems. Predicted membrane-binding site is also involved in protein-protein association.', '2006-03-17'),
(220, 100, 51, 4, '2spc', 'Spectrin alpha chain', '1.8', 'in', 4.3, 0.8, 87, 11, -6.2, '', 2, 0, 'Subcellular location: near the inner surface of the plasma membrane of nearly all cells. Interacts with lipid bilayers (Maksymiw et al. 1987).', 'Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Native spectrin molecule is a tetramer composed of two antiparallel heterodimers joined head to head so that each end of the native molecule includes the C-terminus of the alpha subunit and the N-terminus of the beta subunit.', '2006-03-17'),
(221, 101, 94, 3, '1g5z', 'Outer surface protein C', '2.5', 'out', 3.6, 0.6, 2, 8, -7.0, '', 2, 0, '', 'Members of this family are lipoproteins that are probably involved in evasion of the host immune system by pathogens.', '2006-03-17'),
(222, 102, 138, 23, '1eci', 'Ectatomin', 'NMR', 'out', 5.3, 1.8, 58, 15, -5.2, '', 2, 0, '', 'Pore-forming protein that forms nonselective cation channels both in cell and artificial membranes (Pluzhnikov et al. 1999). Ectatomin is an heterodimer of an A and a B chain linked by a disulfide bond. The pore is formed by two heterodimers (?).', '2006-03-17'),
(223, 103, 170, 23, '1j0t', 'Molt-inhibiting hormone', 'NMR', 'out', 4.1, 0.4, 66, 6, -7.0, '', 1, 0, 'No experimental data about interactions with lipid bilayers.', 'Predicted membrane-binding site participates in protein-protein interactions.', '2006-03-17'),
(224, 104, 14, 24, '1n69', 'Saposin B, complex with phosphatidylethanolamine', '2.2', 'out', 1.2, 1.0, 58, 6, -2.4, '', 6, 0, 'It was suggested that a more "open" conformation of saposin B interacts with lipid bilayers (Ahn et al. 2003).  Saposin B extracts phospholipids from the lipid surface; the binding is optimal at low pH values (Ciaffoni et al. 2006).   ', 'Saposins A, B, C, and D are small lysosomal glycoproteins released by proteolysis from a single precursor polypeptide, prosaposin. Saposin B is an activator protein that can extract lipids from membranes. This protein undergoes conformational changes upon association with membranes. See also closed monomeric (3bqp,3bqq) and open dimeric (2z9a) forms of saposin D.', '2006-03-17'),
(225, 104, 57, 23, '1nkl', 'NK-lysin', 'NMR', 'out', 2.8, 1.5, 37, 12, -5.4, '', 1, 0, '', 'Antimicrobial protein that undergoes conformational changes upon association with membranes. May be an effector molecule of cytotoxic activity. High activity against E. coli and B. megaterium.', '2006-03-17'),
(227, 107, 143, 23, '1o82', 'Bacteriocin AS-48', '1.4', 'out', 4.4, 1.1, 81, 13, -7.0, '', 1, 0, '', 'This protein undergoes conformational changes and forms channels in membranes.', '2006-03-17'),
(228, 56, 57, 14, '1hm6', 'Annexin I', '1.8', 'in', 2.1, 0.9, 88, 7, -5.6, '', 1, 0, '', 'Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.', '2006-03-17'),
(229, 56, 14, 4, '1w7b', 'Annexin II', '1.5', 'in', 2.4, 1.2, 87, 18, -3.8, '', 1, 0, '', 'Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity.', '2006-03-17'),
(230, 56, 14, 4, '1axn', 'Annexin III', '1.7', 'in', 2.7, 0.8, 77, 11, -5.7, '', 1, 0, '', 'Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate.', '2006-03-17'),
(231, 56, 6, 4, '1i4a', 'Annexin IV', '2.0', 'in', 2.5, 1.1, 89, 3, -7.7, '', 3, 0, '', 'May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A).', '2006-03-17'),
(232, 56, 14, 4, '1hvf', 'Annexin V', '2.0', 'in', 2.3, 1.5, 79, 10, -5.4, '', 1, 0, '', 'An anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. This protein undergoes major conformational changes upon association with membranes.', '2006-03-17'),
(233, 56, 11, 4, '1yii', 'Annexin V', '1.4', 'in', 3.1, 0.7, 79, 7, -5.1, '', 1, 0, '', 'This protein undergoes major conformational changes upon association with membranes.', '2006-03-17'),
(234, 56, 14, 4, '1m9i', 'Annexin VI', '2.65', 'in', 2.8, 0.3, 82, 0, -8.5, '', 1, 0, '', '', '2006-03-17'),
(235, 56, 14, 4, '1w3w', 'Annexin VIII', '1.9', 'in', 4.1, 1.0, 79, 9, -6.2, '', 1, 0, '', 'This annexin is normally expressed in endothelial cells of the placenta and the lung. It may have a role in the signal transduction pathway in the \r\nacute promyelocytic leukemia cells. The structure of the K16A mutant of annexin A8 reveals the conformation of an intact medium-length annexin N terminus, including two highly accessible functional\r\nregulation sites, a calpain cleavage site and a potential phosphorylation site. The regulation would take place by releasing the N terminus from restrictive interactions within the hydrophilic channel between the annexin structural\r\nmodules, releasing their full flexibility (Rety et al. 2005).', '2006-03-17'),
(236, 56, 161, 4, '1dm5', 'Annexin XII', '1.9', 'in', 2.7, 1.0, 90, 7, -10.2, '', 3, 0, 'Residues E142, S144 and G145 of annexin B12 are positioned just beyond the calculated hydrophobic boundary (subunit C of the trimer) and their side-chains are directed toward the membrane, which is consistent with spin-labeling studies (Isas et al. 2004).', 'This protein undergoes major conformational changes upon association with membranes. ', '2006-03-17'),
(237, 56, 112, 4, '1dk5', 'Annexin 24', '2.8', 'in', 3.5, 1.3, 76, 18, -4.4, '', 1, 0, 'Characterization of this plant annexin using biophysical methods revealed calcium-dependent binding to phospholipid vesicles with preference for phosphatidylcholine over phosphatidylserine and magnesium-dependent phosphodiesterase activity in vitro (Hofmann et al. 2000).  W107 penetrates the hydrocarbon core in the calculated orientation.  Two other aromatic residues (W35 and Y192) occupy the interfacial region.  This is consistent with fluorescence data (Hofmann et al. 2000).', '', '2006-03-17'),
(238, 56, 149, 4, '1n00', 'Annexin GH1', '2.1', 'in', 1.5, 2.0, 70, 17, -3.7, '', 1, 0, 'W32 penetrates the bilayer interior, while W104 occupies interfacial region of membrane, consistent with the membrane-interaction mode discussed by Hofmann et al. (2003). ', 'This protein may undergo conformational changes upon association with membranes.', '2006-03-17'),
(239, 49, 26, 6, '1q4g', 'Prostaglandin H2 synthase-1', '2.0', 'out', 8.9, 0.4, 90, 1, -43.4, '', 2, 0, 'Residues I74, W75, W77, L78, F88, F91, L92, W98, L99 and F102 are involved in hydrophobic interactions with the membrane (Spencer et al. 1999) in agreement with the set of membrane core embedded residues in the calculated position of the dimer (I74, W75, W77, L78, T81, L82, F88, F91, L92, W98, L99, F102, V103, T106, F107, I108). Protein was crystallized with N-OCTYL-beta-D-GLUCOPYRANOSIDE. Calculated boundaries correspond to oxygens of several crystallized detergent molecules.  Two other molecules of detergent occupy binding pocket. Results of our calculations are also  consitent with MD simulations of the protein (Nina et al. 2000).', 'May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells. Structure with longer polypeptide chain: 1u67 (1-600, 3.1A resolution).', '2006-03-17'),
(240, 108, 146, 23, '1puo', 'Major allergen I', '1.8', 'out', 3.7, 0.8, 58, 6, -7.8, '', 1, 0, 'No experimental data about interactions with lipid bilayers.', 'Possible transporter of hydrophobic substances. Major allergen produced by the domestic cat. This protein is sticky and easily adheres to walls, carpet, clothing, furniture and bedding.', '2006-03-17'),
(241, 50, 14, 6, '1w6k', 'Lanosterol synthase', '2.1', 'in', 7.6, 1.0, 77, 4, -17.8, '', 1, 0, 'Consistent with orientation proposed by Thoma et al. (2004). This is an integral monotopic protein.', 'Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, first step of cholesterol biosynthesis.', '2006-03-17'),
(242, 54, 25, 6, '1nr6', 'Cytochrome P450 2C5', '2.1', 'in', 10.6, 1.0, 54, 18, -9.1, '', 1, 0, 'Crystallization with detergent (CYMAL-5). This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This protein differs from other forms of cytochrome P450 in that it catalyzes the 21-hydroxylation of progesterone, resulting in the formation of deoxycorticosterone.', '2006-03-17'),
(243, 54, 25, 6, '1suo', 'Cytochrome P450 2B4, closed state', '1.9', 'in', 4.6, 1.3, 57, 4, -14.2, '', 1, 0, 'Membrane-bound. Endoplasmic reticulum. Crystallization with detergent (CYMAL-5). This cytochrome presumably forms TMH 1-21, consistent with calculated orientation.', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin.', '2006-03-17'),
(244, 54, 14, 6, '1pq2', 'Cytochrome P450 2C8', '2.7', 'in', 3.8, 1.8, 65, 9, -8.6, '', 1, 0, 'Crystallization with detergent (CYMAL-6). This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti-cancer drug paclitaxel (taxol).', '2006-03-17'),
(245, 54, 14, 6, '1og5', 'Cytochrome P450 2C9', '2.5', 'in', 7.6, 1.0, 79, 6, -13.7, '', 1, 0, 'Crystallization with detergent (CYMAL-5). This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.', '2006-03-17'),
(246, 54, 14, 6, '1tqn', 'Cytochrome P450 3A4', '2.0', 'in', 8.7, 1.0, 67, 11, -18.5, '', 1, 0, 'Crystallization with detergent (CYMAL-6/CHAPS). This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', '2j0c and 2j0d have the same calculated positions in the membrane as 1tqn, although conformations of some loops in 2j0c are different. ', '2006-03-17'),
(247, 54, 14, 6, '1z10', 'Cytochrome P450 2A6', '1.9', 'in', 5.0, 1.7, 44, 18, -9.5, '', 1, 0, 'Crystallization with detergent (ANAPOE-X-405). This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', 'Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. 2p85 is a nearly identical structure of P450 2a13.', '2006-03-17'),
(248, 109, 36, 13, '1qqe', 'Vesicular transport protein sec17', '2.9', 'in', 5.2, 6.1, 17, 15, -6.2, '', 1, 0, 'This is known peripheral membrane protein (UniProt). A related protein SNAP-25 (SNP25_HUMAN) has several S-palmitoyl cysteines (85,88,90,92) after two first N-terminal coils of the superhelix.', 'SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. Interacts with SEC18.', '2006-03-17'),
(249, 109, 221, 4, '1hxi', 'Nucleoside transporter 2 (water-soluble domain)', '1.6', 'in', 3.7, 1.0, 71, 5, -8.1, '', 1, 0, 'No direct experimental data about interactions of this domain with lipid bilayers. ', 'It has a large TM domain which belongs to TCDB 2.A.57. This is PFAM family PF01733.', '2006-03-17'),
(900, 319, 287, 23, '2jni', 'Arenicin-2', 'NMR', 'out', 2.1, 1.1, 82, 15, -5.2, '', 1, 0, '', '', '0000-00-00'),
(250, 109, 14, 19, '1nzn', 'Mitochondria fission protein Fis1', '2.0', 'out', 6.1, 1.4, 72, 8, -9.3, '', 1, 0, 'Additional membrane-anchoring elements: C-terminal segment 123-147 (missing in the crystal structure) presumably forms a TM helix, which is geometrically possible in this membrane-association mode. The C-terminal TM helix was unfolded in aqueous solution, even in the presence of bicelles (Suzuki et al. 2003) ', 'Function - see Koch et al. (2005).', '2006-03-17'),
(251, 110, 25, 4, '2p0m', 'Arachidonate 15-Lipoxygenase', '2.4', 'in', 8.6, 0.1, 87, 5, -14.3, '', 1, 0, 'Results are consistent with the membrane-anchoring role of Y15, F70, L71, W181 and L195 (Walther et al. 2004). The following residues are buried in the membrane in the calculated position of the protein: L71, I194, L195, L291, Y292, and F412 (Y15 and F70 are close to the calculated hydrophobic boundary, and W181 is missing in the crystal structure). Membrane binding affinity is -4.6 kcal/mol (Walther et al. 2004).', 'Alpha-helical lipoxygenases, alpha-helical phospholipase C, and alpha/beta pancreatic lipases have a common C2 domain. ', '2006-03-17'),
(1310, 96, 142, 23, '1r9u', 'Zervamicin IIb, transmembrane orientation', 'NMR', 'out', 23.2, 5.4, 38, 7, -15.0, '', 1, 1, '', '', '0000-00-00'),
(1311, 184, 14, 23, '1jmy', 'Bile-salt activated lipase, different conformation', '2.6', 'out', 5.0, 1.4, 85, 9, -5.3, '', 1, 0, '', '', '0000-00-00'),
(1312, 339, 215, 26, '1hr1', 'Indolicidin, with P->A substitution', 'NMR', 'out', 5.4, 4.0, 84, 9, -8.3, '', 1, 0, '', '', '0000-00-00'),
(1313, 176, 14, 19, '2xfn', 'Monoamine oxidase B, dimer', '1.6', 'out', 30.0, 3.2, 14, 0, -14.5, '', 2, 2, '', '', '0000-00-00'),
(1314, 28, 20, 1, '3bo0', 'Preproteiin translocase SecY', '9.6', 'A in', 29.6, 1.2, 6, 2, -78.0, '', 3, 12, '', '', '0000-00-00'),
(1315, 15, 6, 4, '2x72', 'Metarhodopsin II, dimer', '3.0', 'A out', 30.0, 0.6, 0, 0, -132.0, '', 2, 14, '', '', '0000-00-00'),
(1316, 262, 9, 3, '2w8h', 'Outer membrane lipoprotein Wza, water-soluble part', '2.76', 'in', 1.6, 0.2, 1, 0, -22.1, '', 8, 0, '', '', '0000-00-00'),
(253, 111, 119, 23, '1ca1', 'Alpha-toxin (PHLC1_CLOPE), open state', '1.9', 'out', 2.9, 1.0, 89, 4, -9.3, '', 1, 0, 'Results are consistent with the important role of Y331 and F334 for asociation with lipid bilayers (Jepson et al. 2001).', 'Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca(2+) dependent manner and toxicity is conferred by this C-terminal domain, which also contributes to the sphingomyelinase activity.', '2006-03-17'),
(254, 112, 9, 2, '1rqj', 'Farnesyl diphosphate synthase (Geranyltranstransferase)', '1.9', 'in', 3.3, 0.7, 87, 3, -7.7, '', 1, 0, 'No experimental data about interactions with lipid bilayers.', '', '2006-03-17'),
(255, 113, 54, 23, '1poa', 'Snake phospholipase A2, group I', '1.5', 'out', 4.8, 1.0, 89, 7, -10.7, '', 1, 0, 'Residues penetrating the bilayer core are W19, W61 and F64 (Y3 and W18 are mostly outsite the calculated boundaries). This is consistent with the important role of W19, W61, and F64 (Sumandea et al. 1999) or W61, F64 and Y110 (Stahelin and Cho 2001) in protein-membrane asociation. Y110 is in the interfacial region (just beyond the hydrophobic core) in the calculated orientation of the phospholipase. Maximal membrane binding affinity is -11.4 kcal/mol (Stahelin and Cho 2001).', '', '2006-03-17'),
(256, 113, 181, 23, '1m8t', 'Snake phospholipase A2, group I, acidic 2', '2.1', 'out', 4.4, 0.8, 88, 6, -6.6, '', 1, 0, '', 'Displays edema-inducing and moderate anticoagulant activities.', '2006-03-17'),
(257, 113, 129, 23, '1pp2', 'Snake phospholipase A2, group II', '2.5', 'out', 3.7, 1.3, 80, 7, -12.9, '', 1, 0, '', '', '2006-03-17'),
(258, 113, 78, 23, '1bk9', 'Snake phospholipase A2, group II, acidic', '2.0', 'out', 7.3, 0.3, 87, 3, -11.4, '', 1, 0, '', '', '2006-03-17'),
(260, 113, 78, 23, '1jia', 'Snake phospholipase A2, group II, B', '2.1', 'out', 3.3, 0.5, 78, 4, -11.2, '', 1, 0, 'Obtained orientation is in agreement with mutagenesis and binding study of a homologous phosholipase (Wijewickrama et al. 2006). Residues interacting with the membrane acyl chain region are V20, F24, A119, P121, and I124, according to the calculations. Residues important for membrane binding are Y120, P121, I124, and L125 (others were not tested; Y120 and L125 occupy the interfacial region in the calculated position) (Wijewickrama et al. 2006). Structures of membrane-associated loops in these homologous proteins may differ. ', '', '2006-03-17'),
(261, 113, 78, 23, '1bjj', 'Snake phospholipase A2, group II, neutral', '2.8', 'out', 2.6, 0.7, 86, 5, -8.4, '', 1, 0, '', 'Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Acts presynaptically. First case of a non-basic phospholipase showing potent neurotoxicity.', '2006-03-17'),
(262, 113, 75, 23, '1vap', 'Snake phospholipase A2, group II', '1.6', 'out', 5.1, 0.6, 88, 5, -10.3, '', 1, 0, 'The following residues are buried in the membrane core: F3, M18, V19, W30, M61, I63, and W109. According to flourescence data (Lathrop et al. 2001), W20, W30, and W109 interact with lipids (value of Fmax for W30+ mutant in Table 1 from Lathrop et al. indicates that W30 contributes to the protein-lipid interactions).  W20 occupies interfacial region in the calculated orientation of phospholipase (residue numbering corresponds to UniProt and PDB). Maximal membrane binding affinity is -10.6 kcal/mol (Stahelin and Cho 2001) or -5.2 kcal/mol (Tatulian 2002).', 'This orientation is similar to one suggested by Diraviyam and Murray (2006). However, phospholipase penetrates by ~10 A deeper in the membrane according to our results (nonpolar residues are inserted in the hydrocarbon core, not in the head group region).', '2006-03-17'),
(263, 113, 77, 23, '1s8i', 'Myotoxin', '1.6', 'out', 4.9, 0.7, 83, 5, -10.6, '', 1, 0, '', 'Group II subfamily. Myotoxic protein that presumably lacks PA2 enzymatic activity. Induces necrosis of muscle cells. Three crystal forms of the myotoxin (1s8i, 1s8g and 1s8h) reveal that the presence of a ligand in the active site (naturally presumed to be a fatty acid) induces the exposure of a hydrophobic surface\r\n(the hydrophobic knuckle) toward the C terminus (Ambrosio et al. 2004).', '2006-03-17'),
(264, 113, 179, 23, '1ae7', 'Snake phospholipase A2, group I', '2.0', 'out', 4.7, 0.6, 84, 9, -6.2, '', 1, 0, '', 'Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Acts presynaptically. Is directly toxic to skeletal muscle upon local application in vivo (dystrophic effect).', '2006-03-17'),
(265, 113, 225, 23, '1vip', 'Snake phospholipase A2, group II,  RVV-VD', '2.2', 'out', 4.4, 0.8, 85, 11, -9.5, '', 1, 0, '', 'This protein has anticoagulant activity.', '2006-03-17'),
(266, 113, 224, 23, '1jlt', 'Snake phospholipase A2, group II', '1.4', 'out', 2.8, 1.0, 89, 7, -8.7, '', 1, 0, '', '', '2006-03-17'),
(267, 113, 137, 23, '1oz6', 'Snake phospholipase A2, group II', '2.6', 'out', 5.6, 1.0, 84, 13, -9.6, '', 1, 0, '', '', '2006-03-17'),
(268, 113, 101, 23, '1u4j', 'Snake phospholipase A2, group I, isoform 2', '2.1', 'out', 2.2, 0.6, 83, 4, -8.5, '', 1, 0, '', '', '2006-03-17'),
(269, 113, 101, 23, '1g2x', 'Snake phospholipase A2, group I,  KPA2', '2.5', 'out', 3.8, 1.5, 84, 10, -5.4, '', 1, 0, '', 'The protein shows anticoagulant and neurotoxic activities.', '2006-03-17'),
(270, 113, 101, 23, '1tc8', 'Snake phospholipase A2, group I, isoform 1', '2.7', 'out', 3.1, 1.4, 89, 11, -5.0, '', 1, 0, '', '', '2006-03-17'),
(271, 113, 76, 23, '1mc2', 'Myotoxin', '0.8', 'out', 2.4, 0.1, 80, 2, -9.4, '', 1, 0, '', 'Myotoxic protein that presumably lacks PA2 enzymatic activity. The lack of catalytic activity appears to be related to the presence of Phe102, which prevents the access of substrate to the active site. The substitution of tryptophan for leucine at residue 10 interferes with dimer formation and may be responsible for the additional loss of hemolytic activity. The ultrahigh resolution of the experimental diffraction data permits alternative conformations to be modeled for disordered residues (Liu et al. 2003). ', '2006-03-17'),
(272, 113, 96, 23, '1umv', 'Snake phospholipase A2, group II, hypotensive', '1.7', 'out', 5.1, 0.7, 87, 4, -8.6, '', 1, 0, '', '', '2006-03-17'),
(273, 113, 95, 23, '1god', 'Myotoxin', '2.8', 'out', 3.0, 0.8, 80, 8, -7.4, '', 1, 0, '', 'Group II subfamily. Myotoxic protein that lacks enzymatic activity. Does not bind calcium as one of the calcium binding ligands is lost (Asp->Lys in position 48).', '2006-03-17'),
(274, 113, 98, 23, '1gmz', 'Snake phospholipase A2-3, group II', '2.4', 'out', 3.8, 1.5, 88, 10, -6.7, '', 1, 0, '', 'Has moderate PLA2 activity but a strong myotoxic activity. Also has anticoagulant activity.', '2006-03-17'),
(275, 113, 173, 23, '1ozy', 'Snake phospholipase A2, group I', '2.7', 'out', 2.6, 1.0, 85, 5, -9.0, '', 1, 0, '', '', '2006-03-17'),
(276, 113, 97, 23, '1xxs', 'Myotoxin II', '1.8', 'out', 4.5, 1.2, 76, 10, -5.3, '', 1, 0, '', 'Displays myotoxin and edema-inducing activities. Lacks PA2 enzymatic activity as well as of hemorrhagic, anticoagulant and coagulant activities. Homodimer in aqueous solution. Does not bind calcium as one of the calcium binding ligands is lost (Asp->Lys in position 48). Two stearic acid molecules were located in the substrate-binding cleft of each monomer in positions, which favor the interaction of their carboxyl groups with active site residues. The way of binding of stearic acids to this Lys49-PLA(2)s is analogous to phospholipids and transition state analogues to catalytically active PLA(2)s. Two additional stearic acid molecules were located at the dimer interface region, defining a hitherto unidentified acyl-binding site on the protein surface. The strictly conserved Lys122 for Lys49-PLA(2)s may play a fundamental role for stabilization of ligand-protein complex (Watanabe et al. 2005). ', '2006-03-17'),
(277, 113, 130, 23, '1zwp', 'Snake phospholipase A2, group II,  VRV-PL-VIIIa', '1.1', 'out', 4.9, 1.0, 76, 7, -12.5, '', 1, 0, '', 'This toxin shows neurotoxic symptoms and damages vital organs such as lung, liver and kidney. Displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle.', '2006-03-17'),
(278, 113, 14, 23, '1n28', 'Phospholipase A2, group IIA', '1.5', 'out', 3.6, 0.6, 88, 4, -7.0, '', 1, 0, 'The orientation and a set of membrane-embedded residues (V3, L19, F23, F63, and Y111) are consistent with site-directed spin-labeling studies (V3, K10, L19, F23, and F63 - based on exposure to NiEDDA; membrane depth parameters were not evaluated) (Canaan et al. 2002). Maximal membrane binding affinity is -6.4 kcal/mol (Bezzine et al. 2002).', 'Participates in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This orientation is similar to one predicted by Diraviyam and Murray (2006). However, phospholipase penetrates by ~10A deeper in the membrane according to our results and MD simulations (Zhou and Schulten, 1996): nonpolar residues are inserted in the hydrocarbon core, not in the head group region.', '2006-03-17'),
(279, 113, 6, 23, '1g4i', 'Phospholipase A2, group IB', '0.9', 'out', 1.9, 0.5, 87, 4, -7.4, '', 1, 0, '', 'A cluster of 2-methyl-2,4-pentanediol molecules is present at the entrance of the hydrophobic channel that leads to the catalytic site and mimics the fatty-acid chains of a substrate analogue (Steiner et al. 2001). Some mutants form a molten globule-like state at pH<4. ', '2006-03-17'),
(280, 113, 57, 23, '4p2p', 'Phospholipase A2, group IB', '2.4', 'out', 3.3, 0.8, 89, 7, -8.6, '', 1, 0, 'Published fluorescence quenching data show penetration of Trp3 into the acyl chain region of the lipid bilayer (Tatulian et al. 2005), consistent with the calculations.  ', 'Structure of this phospholipase has been also determined in micelles where first \r\nthree residues of the N-terminal alpha-helix (Ala1, Leu2 and Trp3) are disordered (van den Berg et al. 1995). K56 (PDB numbering) is N6-palmitoylated (UniProt).  ', '2006-03-17'),
(281, 113, 14, 23, '1le6', 'Phospholipase A2, group X', '1.9', 'out', 7.4, 0.9, 78, 6, -13.2, '', 1, 0, 'Calculated transfer energy is larger than a maximal experimental value (-6.1 kcal/mol, Bezzine et al. 2002). Perhaps the experimental data reflects the membrane-binding affinity of a premicellar protein-lipid aggregate (Pan et al. 2002); hence, the large exposed hydrophobic surface of the membrane-dissociated protein might be partially covered by lipid.    ', 'Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers uncharged phosphatidylethanolamine and phosphatidylcholine liposomes to those of charged phosphatidylserine (a unique feature of this phospholipase). ', '2006-03-17'),
(282, 114, 83, 23, '1poc', 'Phospholipase A2', '2.0', 'out', 4.0, 1.6, 60, 6, -9.5, '', 1, 0, 'Calculated orientation is similar to that determined by spin-labeling studies (Lin et al. 1998). Membrane-embedded residues in the calculated orientation: I1, I2, Y3, P4, G5, K14, I78, F82, M86, and L90. Spin-labeled residues with small exposure factors to Crox: I2, K14, and I78 (others were not tested except F82 that has a slightly higher exposure factor) (Lin et al. 1998). These residues penetrate the aliphatic core, not the interfacial region of membrane, according to the calculations (consistent with position of the crystallized lipid).  Protein-membrane binding involves significant hydrophobic, rather than electrostatic component  (Bollinger et al. 2004). Maximal membrane binding affinity is -8.2 kcal/mol (Bollinger et al. 2004). Carbonyl groups of bound (substrate) lipid are situated ~2A above the calculated hydrocarbon membrane boundary plane.', '', '2006-03-17'),
(283, 115, 213, 23, '1kp4', 'Prokaryotic phospholipase A2', '1.6', 'out', 2.4, 1.3, 42, 13, -5.6, '', 1, 0, '', '', '2006-03-17'),
(285, 117, 6, 4, '1tfj', 'Glycolipid transfer protein', '1.6', 'in', 3.9, 1.0, 90, 5, -8.3, '', 1, 0, '', 'Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids and glyceroglycolipids between membranes but does not catalyze the transfer of phospholipids. It is possible that it is involved in the intracellular translocation of glucosylceramides.', '2006-03-17'),
(286, 118, 9, 23, '1col', 'Colicin A channel-forming domain', '2.4', 'out', 1.8, 1.0, 43, 11, -3.2, '', 1, 0, '', 'The protein undergoes major conformational changes in membrane. The membrane-penetrating hydrophobic alpha-hairpin is oriented towards the bilayer (this is a possible initial bound state).', '2006-03-17'),
(996, 287, 14, 4, '2ks1', 'Receptor tyrosine kinase erbB-2, complex with EGF receptor', 'NMR', 'A out', 32.0, 2.5, 15, 5, -50.6, '', 2, 2, '', '', '0000-00-00'),
(289, 120, 91, 23, '1ji6', 'Cry3Bb1', '2.4', 'out', 3.8, 1.6, 64, 6, -4.2, '', 2, 0, '', 'This protein undergoes major conformational transitions and oligomerization upon association with membranes.', '2006-03-17'),
(290, 120, 91, 23, '1i5p', 'Cry2Aa', '2.2', 'out', 3.4, 1.2, 16, 12, -7.0, '', 1, 0, '', 'This endotoxin has two alternative membrane association modes in the monomeric state: (1) as in Cry 3A (through the alpha-helical domain), and (2) through the hydrophobic beta-sheet at the opposite side of the protein, as shown in the picture. This protein undergoes major conformational transitions and oligomerization upon association with membranes.', '2006-03-17'),
(1299, 117, 6, 1, '1wbe', 'Glycolipid transfer protein, different conformation', '1.36', 'in', 4.2, 2.1, 88, 6, -7.1, '', 1, 0, '', '', '0000-00-00'),
(1300, 336, 307, 23, '1xc0', 'Pardaxin, different conformation', 'NMR', 'out', 20.8, 5.4, 42, 2, -9.6, '', 1, 1, '', '', '0000-00-00'),
(292, 121, 9, 23, '1ehs', 'Heat-stable enterotoxin II', 'NMR', 'out', 1.4, 1.1, 64, 11, -6.0, '', 1, 0, 'Interacts with lipid bilayers (Chao and Dreyfus 1999).', 'Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells.', '2006-03-17'),
(293, 122, 14, 4, '1dan', 'Coagulation factor VIIa', '2.0', 'out', 4.2, 6.0, 25, 26, -4.9, '', 4, 0, 'The elongated complex must be approximately perpendicular to the membrane based on a fluorescence study by McCallum et al. (1996). ', 'Heterodimer of a light chain and a heavy chain linked by a disulfide bond. Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis.', '2006-03-17'),
(294, 122, 6, 4, '1nl2', 'Prothrombin', '2.3', 'out', 3.9, 3.0, 18, 24, -5.8, '', 1, 0, 'Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. ', '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. Only protein complexes with GLA domain are indicated as related PDB entries.', '2006-03-17'),
(295, 122, 57, 4, '1pfx', 'Coagulation factor IX', '3.0', 'out', 1.9, 6.0, 84, 10, -3.9, '', 2, 0, 'Orientation of the complex should be more perpendicular to the membrane based on a fluorescence study by Mutucumarana et al. (1992).', 'Heterodimer of a light chain and a heavy chain; disulfide-linked. Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. Activated by factor XIa, which excises the activation peptide.', '2006-03-17'),
(296, 122, 14, 4, '1lqv', 'Coagulation factor XIV  (protein C) in complex with its receptor', '1.6', 'out', 3.4, 3.9, 53, 14, -5.6, '', 2, 0, 'The receptor is located above the membrane surface (Yegneswaran et al. 1997); it presumably has a TM helix 211-231.', 'Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids.', '2006-03-17'),
(297, 123, 159, 15, '1df4', 'Envelope glycoprotein gp41', '1.4', 'out', 6.3, 0.9, 0, 10, -6.7, '', 3, 0, '', 'Fragments of transmembrane glycoprotein.', '2006-03-17'),
(298, 123, 204, 15, '1svf', 'Paramyxovirus sv5 fusion protein core', '1.4', 'out', 8.4, 0.9, 0, 11, -10.7, '', 6, 0, '', 'Single-pass type I membrane protein.', '2006-03-17'),
(1331, 143, 55, 4, '1opb', 'Retinol-binding protein 2', '1.9', 'in', 1.9, 1.4, 25, 7, -3.6, '', 1, 0, '', '', '0000-00-00'),
(1332, 66, 55, 23, '1epb', 'Epididymal-specific lipocalin-5', '2.20', 'out', 6.4, 1.1, 74, 4, -3.8, '', 1, 0, '', '', '0000-00-00'),
(1333, 66, 14, 23, '1lf7', 'Complement component C8 gamma chain', '1.20', 'out', 1.9, 2.2, 43, 12, -2.6, '', 1, 0, '', '', '0000-00-00'),
(1334, 143, 144, 4, '1yiv', 'Myelin P2 protein', '2.1', 'in', 4.3, 0.6, 48, 6, -2.6, '', 1, 0, '', '', '0000-00-00'),
(1335, 143, 14, 6, '3o22', 'Prostaglandin-H2 D-isomerase', '1.4', 'in', 0.7, 1.2, 78, 13, -2.4, '', 1, 0, '', '', '0000-00-00'),
(302, 125, 6, 23, '1nep', 'Epididymal secretory protein E1', '1.7', 'out', 8.0, 1.4, 73, 14, -4.6, '', 1, 0, '', 'This is a cholesterol-binding protein, may be involved in the regulation of the lipid composition of sperm membranes during the maturation in the epididymis', '2006-03-17'),
(303, 399, 14, 4, '1ds6', 'Rho GDP-dissociation inhibitor 2, complex with G-protein RAC2', '2.3', 'in', 2.8, 1.0, 82, 6, -5.5, '', 2, 0, 'The inhibitor is bound to RAC2 protein (Ras-related C3 botulinum toxin substrate 2). RAC2 has S-geranylgeranyl cysteine 189. The  geranylgeranyl residue can be  buried in the membrane if the C-terminus of RAC2 is extended or unfolded (the C-terminal residues are missing in the crystal structure). The interaction with membrane is weak, since this is the inactive (GDP-bound) state. RAC2 is membrane-associated when activated.', 'Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. ', '2006-03-17'),
(305, 128, 14, 9, '1p4u', 'ADP-ribosylation factor binding protein Gga3 domain', '2.2', 'in', 6.5, 1.1, 71, 11, -6.5, '', 1, 0, 'No direct experimental data about interactions of this specific domain with lipid bilayers.  The predicted membrane binding site may be also involved in protein-protein interactions. ', 'Membrane-associated. Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif. The GAE domain binds accessory proteins regulating GGAs function.', '2006-03-17'),
(306, 129, 27, 2, '1sfd', 'Amicyanin', '0.9', 'out', 3.5, 0.8, 49, 10, -4.0, '', 1, 0, '', 'Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or\r\n                         to pseudoazurin.Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(307, 129, 216, 2, '1id2', 'Amicyanin', '2.1', 'out', 4.2, 1.3, 52, 8, -4.9, '', 1, 0, '', 'Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.', '2006-03-17'),
(308, 129, 186, 7, '9pcy', 'Plastocyanin', 'NMR', 'out', 1.8, 1.6, 18, 19, -1.9, '', 1, 0, '', 'Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. Loosely bound to the inner thylakoid membrane surface in chloroplasts.', '2006-03-17'),
(309, 129, 7, 7, '2plt', 'Plastocyanin', '1.5', 'out', 1.3, 1.5, 21, 18, -2.0, '', 1, 0, '', 'Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.', '2006-03-17'),
(310, 129, 214, 7, '1bxv', 'Plastocyanin', '1.8', 'out', 2.0, 1.6, 36, 19, -2.6, '', 1, 0, '', 'Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.', '2006-03-17'),
(311, 129, 190, 7, '1b3i', 'Plastocyanin', 'NMR', 'out', 2.8, 1.4, 43, 18, -4.4, '', 1, 0, '', 'Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.', '2006-03-17'),
(312, 129, 171, 2, '1pmy', 'Pseudoazurin', '1.5', 'out', 1.6, 1.4, 45, 13, -4.3, '', 1, 0, '', '', '2006-03-17'),
(313, 129, 38, 7, '1f56', 'Plantacyanin', '2.0', 'out', 1.4, 1.5, 11, 15, -2.0, '', 1, 0, '', '', '2006-03-17'),
(314, 129, 80, 2, '1rkr', 'Azurin I', '2.4', 'out', 1.0, 1.0, 43, 7, -4.3, '', 1, 0, '', 'Transfers electrons from cytochrome c551 to cytochrome oxidase.', '2006-03-17'),
(315, 129, 172, 2, '1cuo', 'Azurin iso-2', '1.6', 'out', 1.4, 1.6, 69, 15, -4.3, '', 1, 0, '', 'This methylothroph organism uses azurin in the oxidation of methylamine. Iso-2 is probably the acceptor of electrons from methylamine dehydrogenase.', '2006-03-17'),
(317, 63, 196, 4, '1gmi', 'Protein kinase C epsilon', '1.7', 'in', 2.9, 1.2, 46, 15, -5.9, '', 1, 0, 'Residue I89 and partially V29 and P31 penetrate the bilayer core. According to muatgenesis studies, the most important residue for membrane binding is I89 (Corbalan-Garcia et al. 2003). The binding is also affected by replacing Y91 and in the triple mutant W23A/R26A/R32A.  These residues are in the membrane interfacial region in the calculated orientation.', '', '2006-03-17'),
(318, 63, 55, 4, '3hn8', 'Synaptotagmin-3', '3.5', 'in', 4.0, 3.1, 74, 19, -4.0, '', 1, 0, '', '', '2006-03-17'),
(319, 63, 14, 4, '1ugk', 'Synaptotagmin-4', 'NMR', 'in', 2.5, 1.7, 34, 11, -3.5, '', 1, 0, '', '', '2006-03-17'),
(320, 63, 55, 4, '1a25', 'Protein kinase C beta', '2.7', 'in', 3.1, 1.0, 44, 18, -2.8, '', 1, 0, 'Maximal membrane binding affinity: -4.1 kcal/mol (Johnston and Cornell 1999) or -7.5 kcal/mol (Nalefski et al. 2001).', '', '2006-03-17'),
(321, 63, 55, 4, '2bwq', 'Rab3 interacting molecule 2 (RIM2), C2A domain', '1.4', 'in', 1.5, 1.6, 41, 19, -1.8, '1', 1, 0, '', 'This C2 domain does not bind calcium (Dai et al. 2005).', '2006-03-17'),
(323, 191, 144, 23, '1hpl', 'Pancreatic lipase', '2.3', 'out', 3.8, 0.3, 80, 5, -8.1, '', 1, 0, '', 'Alpha-helical lipoxygenases, alpha-helical phospholipase C, and alpha/beta pancreatic lipases have an additional common beta-sandwich domain.', '2006-03-17'),
(324, 111, 117, 23, '1olp', 'Alpha-toxin', '2.5', 'out', 2.8, 1.8, 62, 11, -6.1, '', 1, 0, 'Calculated orientation is in agreement with membrane binding mode proposed by Clark et al. (2003).', 'Alpha-helical lipoxygenases, alpha-helical phospholipase C, and alpha/beta pancreatic lipases have a common C2 domain.', '2006-03-17'),
(325, 61, 6, 4, '1sdd', 'C2 domains of coagulation factor Va', '2.8', 'out', 3.7, 2.0, 35, 8, -8.7, '', 2, 0, 'Residues Y1956, L1957, W2063 and W2064 are involved in hydrophobic interactions with the membrane (Peng et al. 2004, 2005) in agreement with the set of calculated membrane core embedded residues Y1956, L1957, W2063 and W2064. Maximal membrane binding affinity is -9 kcal/mol (Koppaka and Lentz 1996) or -13 kcal/mol (Peng et al. 2004).', 'Coagulation factor V is a cofactor that participates with factor Xa to activate prothrombin to thrombin. Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). Factor Va is composed of a heavy chain and a light chain, noncovalently bound. The interaction between the two chains is calcium-dependent. ', '2006-03-17'),
(326, 61, 14, 4, '1d7p', 'C2 domain of coagulation factor VIII', '1.5', 'out', 4.8, 2.0, 28, 10, -8.8, '', 1, 0, 'Residues M2199, F2200, L2251 and L2252 are involved in hydrophobic interactions with the membrane (Gilbert et al. 2002) in agreement with the set of calculated membrane core embedded residues M2199, F2200, L2251 and L2252. Maximal membrane binding affinity is -11.2 kcal/mol (Gilbert et al. 2002).', 'Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa. C2 domain is responsible for phospholipid-binding.', '2006-03-17'),
(329, 134, 72, 23, '1iaz', 'Equinatoxin II', '1.9', 'out', 3.0, 1.2, 44, 9, -5.1, '', 1, 0, 'W112 has been identified as buried in the hydrophobic core of phospholipid micelles or bicelles (Hong et al. 2002, Anderluh et al. 2005), which is consistent with the set of calculated buried residues P81, V82 and W112.  Maximal membrane binding affinity is -11 kcal/mol (Hong et al. 2002), which is much higher than calculated transfer energy probably due to strong specific binding of  sphingomyelin (Anderluh et al. 2005). This protein undergoes major conformational changes and oligomerization upon asociation with membranes. ', 'The protein has a cavity that may be involved in specific lipid binding.', '2006-03-17'),
(330, 134, 208, 23, '1gwy', 'Sticholysin II', '1.7', 'out', 3.4, 1.9, 35, 15, -5.0, '', 1, 0, 'St I and St II bind to biological and model membranes containing sphingomyelin, forming oligomeric pores that lead to leakage of internal contents (Alvarez et al. 2003)', 'This protein undergoes major conformational transitions and oligomerization upon association with membranes.', '2006-03-17'),
(331, 135, 219, 23, '1r2m', 'Hydrophobin II', '1.0', 'out', 4.1, 1.0, 16, 15, -6.6, '', 1, 0, 'A self-assembling protein that also strongly associates with surfactants. No direct experimental data about interactions with lipid bilayers.', '', '2006-03-17'),
(1309, 110, 189, 4, '3fg3', '8R-Lipoxygenase, central and C-terminal domains', '1.90', 'in', 5.0, 0.6, 86, 5, -9.3, '', 1, 0, '', '', '0000-00-00'),
(1301, 54, 299, 6, '3k1o', 'Sterol 14-alpha-demethylase (CYP51), different conformation', '2.89', 'in', 10.3, 0.9, 65, 5, -9.2, '', 1, 0, '', '', '0000-00-00'),
(1302, 361, 14, 4, '3jwe', 'Monoglyceride lipase MGLL, different closed conformation  ', '2.7', 'in', 6.2, 0.5, 88, 3, -5.8, '', 1, 0, '', '', '0000-00-00'),
(1303, 93, 327, 23, '2xkm', 'Capsid protein G8P, monomer', 'NMR', 'out', 29.2, 4.6, 34, 1, -23.0, '', 1, 1, '', '', '0000-00-00'),
(1304, 86, 14, 6, '2kb7', 'Phospholamban, monomer', 'NMR', 'P in', 32.0, 2.2, 15, 2, -34.6, '', 1, 1, '', '', '0000-00-00'),
(1305, 274, 14, 4, '2k1a', 'Integrin alphaIIb transmembrane helix', 'NMR', 'A out', 34.4, 2.6, 17, 6, -36.9, '', 1, 1, '', '', '0000-00-00'),
(1306, 274, 14, 4, '2rmz', 'Integrin beta3 transmembrane helix', 'NMR', 'A out', 30.0, 3.6, 49, 2, -36.0, '', 1, 1, '', '', '0000-00-00'),
(1307, 154, 215, 26, '2jue', 'Kalata B1, all-D analogue', 'NMR', 'out', 3.7, 1.0, 82, 17, -5.5, '', 1, 0, '', '', '0000-00-00'),
(1308, 110, 189, 4, '1u5u', '8R-Lipoxygenase, N-terminal domain', '2.0', 'in', 3.1, 0.3, 72, 3, -10.4, '', 1, 0, '', '', '0000-00-00'),
(334, 138, 134, 4, '1hce', 'Hisactophilin-1', 'NMR', 'in', 3.5, 1.1, 60, 15, -1.6, '', 1, 0, 'Contains N-myristoyl Gly 1 residue in vivo (it is replaced by Met in the PDB entry). Membrane-binding affinity of the myristoylated protein at pH 6: -8.1 kcal/mol (2.5 kcal/mol comes from electrostatic interactions of seven charged histidines with membrane, and 5.6 kcal/mol comes from transfer of a myristoyl group) (Hanakan et al. 1996).', 'May act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments.', '2006-03-17'),
(335, 139, 39, 23, '1qtf', 'Exfoliative toxin B', '2.4', 'out', 2.8, 1.9, 81, 11, -5.8, '', 1, 0, 'No experimental data about membrane-protein association.', 'Has serine protease-like properties and binds to the skin protein profilaggrin. Predicted membrane-association site may interact with another protein.', '2006-03-17'),
(336, 139, 14, 5, '1lcy', 'Mitochondrial serine protease HtrA2', '2.0', 'out', 7.4, 1.8, 67, 14, -5.1, '', 1, 0, 'No experimental data about membrane-protein association. Predicted membrane-association site may interact with another protein.', 'Serine protease that shows proteolytic activity against a nonspecific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs). Includes PDZ domain.', '2006-03-17'),
(1317, 274, 14, 4, '2knc', 'Integrin alphaIIb-beta3 transmembrane complex', 'NMR', 'A out', 34.8, 1.4, 13, 5, -46.2, '', 2, 2, '', '', '0000-00-00'),
(1318, 300, 14, 19, '2ka2', 'BNip3 transmembrane domain dimer', 'NMR', 'A in', 30.8, 1.8, 4, 2, -29.2, '', 2, 2, '', '', '0000-00-00'),
(1319, 190, 191, 23, '2es4', 'Lipase, complex with foldase', '1.85', 'out', 8.5, 0.0, 65, 2, -7.2, '', 2, 0, '', '', '0000-00-00'),
(1320, 31, 309, 2, '3rfu', 'Copper efflux ATPase', '3.20', 'A in', 30.0, 0.4, 16, 1, -72.1, '', 1, 8, '', '', '0000-00-00'),
(1321, 398, 164, 8, '3rlb', 'Thiamine transporter protein', '2.0', 'A in', 30.8, 1.8, 9, 1, -60.4, '', 1, 6, '', '', '0000-00-00'),
(1322, 397, 36, 6, '1rkl', 'Dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 4 (OST4)', 'NMR', 'A out', 24.8, 3.2, 22, 8, -18.4, '', 1, 1, '', '', '0000-00-00'),
(1323, 397, 14, 6, '2lat', 'Dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 4 (OST4)', 'NMR', 'A out', 31.6, 3.4, 5, 8, -21.6, '', 1, 1, '', '', '0000-00-00'),
(1324, 17, 41, 8, '3pjs', 'Potassium channel KcsA, full length, open', '3.8', 'K in', 31.6, 1.2, 1, 1, -87.3, '', 4, 8, '', '', '0000-00-00'),
(1325, 14, 360, 4, '3am6', 'Proton-pumping rhodopsin-2 from algae', '3.2', 'A out', 31.2, 1.6, 10, 1, -65.4, '', 1, 7, '', '', '0000-00-00'),
(1326, 330, 36, 6, '3sja', 'ATPase Get3, complex with Get1 cytosolic domain', '3.0', 'in', 6.4, 1.6, 89, 45, -8.1, '', 2, 0, '', '', '0000-00-00'),
(1336, 143, 364, 4, '2flj', 'Fatty acid-binding protein', 'NMR', 'in', 1.2, 1.5, 62, 10, -3.6, '', 1, 0, '', '', '0000-00-00'),
(1337, 143, 14, 4, '2rcq', 'Retinol-binding protein 2', '1.2', 'in', 2.9, 1.7, 55, 6, -5.5, '', 1, 0, '', '', '0000-00-00');
INSERT INTO `protein` (`id`, `family_id`, `species_id`, `membrane_id`, `pdbid`, `name`, `resolution`, `topology`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`, `tau`, `numsubunits`, `numstrands`, `verification`, `comments`, `date_added`) VALUES
(994, 36, 9, 3, '3gp6', 'Lipid A acylase PagP', '1.90', 'A in', 24.7, 1.5, 40, 1, -32.5, '', 1, 8, '', '', '0000-00-00'),
(995, 23, 14, 4, '2ksr', 'Nicotinic acetylcholine receptor, beta2 subunit', 'NMR', 'A out', 29.1, 2.2, 16, 1, -47.0, '', 1, 4, '', '', '0000-00-00'),
(993, 21, 39, 8, '3hzq', 'Mechanosensitive channel MscL', '3.82', 'A in', 20.8, 1.2, 1, 0, -56.9, '', 4, 8, '', '', '0000-00-00'),
(343, 142, 157, 13, '1qdm', 'Phytepsin', '2.3', 'out', 9.9, 1.1, 88, 10, -10.4, '', 1, 0, 'No direct experimental data about interactions with lipid biayers.', '', '2006-03-17'),
(344, 142, 14, 24, '1lyb', 'Cathepsin D', '2.5', 'out', 7.0, 0.6, 87, 5, -11.2, '', 2, 0, '', 'Lysosomal membrane-associated protease.\r\n                        Consists of a light chain and a heavy chain.', '2006-03-17'),
(345, 142, 188, 13, '1qs8', 'Plasmepsin IV', '2.5', 'out', 9.1, 1.5, 75, 5, -8.9, '', 1, 0, '', 'Plasmepsins II and V have been identified as membrane-associated proteins.', '2006-03-17'),
(346, 65, 14, 4, '1dyn', 'Dynamin-1', '2.2', 'in', 4.1, 1.2, 88, 15, -9.7, '', 2, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(347, 65, 14, 4, '1pls', 'Pleckstrin', 'NMR', 'in', 3.6, 2.0, 61, 19, -3.8, '', 1, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(348, 65, 53, 4, '1foe', 'T-lymphoma invasion and metastasis-inducing protein 1, with G-protein RAC2', '2.8', 'in', 4.5, 1.1, 64, 7, -6.7, '', 2, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(349, 65, 14, 4, '1fao', 'Dual adaptor of phosphotyrosine and 3-phosphoinositides', '1.8', 'in', 2.4, 2.0, 59, 19, -3.9, '', 1, 0, '', '', '2006-03-17'),
(350, 65, 14, 4, '1eaz', 'PH domain of TAPP1', '1.4', 'in', 1.7, 1.6, 87, 14, -3.0, '', 1, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(351, 65, 14, 4, '1unq', 'Rac-alpha serine/threonine kinase', '0.9', 'in', 2.7, 2.0, 67, 18, -3.9, '', 1, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(352, 65, 14, 4, '1p6s', 'Rac-beta serine/threonine protein kinase', 'NMR', 'in', 3.8, 1.8, 83, 11, -5.7, '', 1, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(353, 65, 53, 4, '1v5u', 'SET binding factor 1', 'NMR', 'in', 4.2, 1.5, 59, 10, -5.3, '', 1, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(354, 65, 14, 4, '1nty', 'Triple functional domain protein', '1.7', 'in', 3.2, 2.0, 59, 16, -3.9, '', 1, 0, '', '', '2006-03-17'),
(355, 65, 14, 4, '1upr', 'Phosphoinositol 3-phosphate binding protein 1', '1.4', 'in', 3.0, 1.4, 62, 19, -3.6, '', 1, 0, '', 'An additional membrane-anchoring element: inositol lipid that is specifically bound to the protein.', '2006-03-17'),
(356, 65, 6, 4, '2bcj', 'PH domain of GPCR kinase 2', '3.1', 'in', 5.7, 1.5, 85, 5, -10.4, '', 3, 0, 'Consistent with membrane-association mode of the complex proposed by Tesmer et al. (2005) and with locations of two important hydrophobic anchors missing in the crystal structure: an inositol lipid bound to PH domain and prenylated Cys 67(68) in gamma subunit of G-protein. ', 'Key membrane-interacting beta-turn in PH domain was modelled using different crystal structure of this kinase (1ym7). ', '2006-03-17'),
(357, 66, 6, 23, '1kt6', 'Retinol binding protein', '1.1', 'out', 4.3, 1.7, 74, 12, -4.7, '', 1, 0, '', '', '2006-03-17'),
(358, 66, 57, 23, '1aqb', 'Retinol binding protein', '1.6', 'out', 4.1, 1.1, 75, 14, -4.4, '', 1, 0, '', '', '2006-03-17'),
(359, 66, 14, 23, '1rbp', 'Retinol binding protein', '2.0', 'out', 3.5, 0.8, 70, 6, -5.8, '', 1, 0, '', '', '2006-03-17'),
(360, 143, 14, 4, '1hmt', 'Muscle fatty acid binding protein', '1.4', 'in', 4.3, 1.6, 49, 12, -5.0, '', 1, 0, '', '', '2006-03-17'),
(361, 143, 6, 4, '1bwy', 'Muscle fatty acid binding protein', 'NMR', 'in', 4.8, 1.3, 71, 12, -6.6, '', 1, 0, '', '', '2006-03-17'),
(362, 143, 55, 4, '1icm', 'Intestinal fatty acid binding protein', '1.5', 'in', 3.5, 1.5, 51, 18, -4.3, '', 1, 0, 'This protein interacts with lipid bilayers (Storch and Thumser, 2000). ', '', '2006-03-17'),
(363, 143, 14, 4, '1kzw', 'Intestinal fatty acid binding protein', 'NMR', 'in', 2.9, 1.3, 61, 12, -4.1, '', 1, 0, '', '', '2006-03-17'),
(364, 143, 14, 4, '1fdq', 'Brain fatty acid binding protein', '2.1', 'in', 3.1, 1.4, 51, 15, -4.9, '', 1, 0, '', '', '2006-03-17'),
(365, 143, 14, 4, '1b56', 'Epidermal fatty acid binding protein', '2.0', 'in', 2.5, 2.0, 56, 18, -3.5, '', 1, 0, '', '', '2006-03-17'),
(366, 143, 53, 4, '1a18', 'Adipocyte lipid-binding protein', '2.4', 'in', 3.7, 0.8, 47, 7, -7.4, '', 1, 0, '', '', '2006-03-17'),
(367, 143, 14, 4, '1tow', 'Adipocyte lipid-binding protein', '2.0', 'in', 2.5, 1.7, 51, 18, -4.5, '', 1, 0, '', '', '2006-03-17'),
(368, 143, 136, 4, '1o8v', 'Fatty acid-binding protein homolog 1', '1.6', 'in', 2.9, 1.0, 48, 15, -5.8, '', 1, 0, '', '', '2006-03-17'),
(369, 143, 200, 4, '1ftp', 'Fatty acid-binding protein', '2.2', 'in', 4.5, 1.0, 53, 11, -5.2, '', 1, 0, '', '', '2006-03-17'),
(370, 143, 14, 25, '1cbs', 'Cellular retinoic acid-binding protein 2', '1.8', 'in', 7.1, 1.9, 41, 13, -5.9, '', 1, 0, '', '', '2006-03-17'),
(371, 143, 6, 4, '1cbr', 'Cellular retinoic acid-binding protein 1', '2.9', 'in', 6.5, 1.1, 45, 11, -5.4, '', 1, 0, '', '', '2006-03-17'),
(372, 143, 55, 4, '1crb', 'Cellular retinol-binding protein II', '2.1', 'in', 2.4, 1.7, 52, 19, -5.3, '', 1, 0, '', '', '2006-03-17'),
(373, 143, 131, 4, '1kqw', 'Cellular retinol-binding protein II', '1.3', 'in', 3.1, 1.3, 45, 13, -4.9, '', 1, 0, '', '', '2006-03-17'),
(374, 143, 14, 4, '1ggl', 'Cellular retinol-binding protein III', '2.3', 'in', 3.3, 1.9, 53, 16, -4.9, '', 1, 0, '', '', '2006-03-17'),
(375, 143, 14, 4, '1lpj', 'Retinoid-binding protein 7', '2.0', 'in', 2.6, 1.1, 44, 13, -6.0, '', 1, 0, '', '', '2006-03-17'),
(376, 143, 6, 4, '1pmp', 'Myelin P2 protein', '2.7', 'in', 2.7, 1.3, 61, 13, -6.1, '', 1, 0, '', '', '2006-03-17'),
(377, 143, 201, 4, '1vyf', 'Fatty acid-binding protein Sm14', '1.8', 'in', 5.1, 1.2, 42, 18, -5.2, '', 1, 0, '', '', '2006-03-17'),
(378, 144, 44, 2, '1wub', 'Polyisoprenoid-binding protein', '1.6', 'out', 2.9, 1.9, 42, 13, -4.4, '', 1, 0, 'No experimental data about association with lipid bilayers.', 'This protein has two alternative binding modes with close transfer energies - through hydophobic spots situated at opposite edges of the beta-barrel.', '2006-03-17'),
(379, 240, 228, 23, '1cwa', 'Cyclosporin', '2.1', 'out', 10.2, 2.5, 82, 53, -7.2, '', 1, 0, 'This conformation of cyclosporine was taken from a complex with cyclophilin (1cwa) where all its hydrophobic side chains are exposed to the outside medium and the structure of the polypeptide backbone is non-regular.  The peptide adopts a competely different conformation (beta-hairpin) with partially buried nonpolar side-chains in organic solvents and probably in water (Wuthrich et al. 1991). Therefore, the calculated transfer energy is strongly overestimated and may be irrelevant (experimental value is -7.4 kcal/mol, Schote et al. 2002).', '', '2006-03-17'),
(380, 146, 214, 2, '2biw', 'Lignostilbene-alpha,beta-dioxygenase (retinal-forming oxygenase)', '2.3', 'in', 6.1, 0.9, 39, 9, -12.9, '', 1, 0, 'The protein was crystallized in the presence of detergent (octylpolyoxyethylene), although it is soluble without detergent (Kloer et al. 2005). Consistent with membrane association mode proposed by Kloer et al. (2005).', 'Synonym: lignostilbene-alpha,beta-dioxygenase.', '2006-03-17'),
(382, 148, 11, 23, '1vmo', 'Vitelline membrane outer protein-I', '2.2', 'out', 3.0, 2.0, 51, 12, -5.3, '', 1, 0, '', 'A component of the outer membrane of the vitelline layer of the egg. Seems to be able to\r\n                         synthesize N-acetylchito-oligosaccharides (n=14-15) from hexasaccharides of N-acetylglucosamine in a manner similar\r\n                         to the transferase activity of lysozyme', '2006-03-17'),
(383, 149, 14, 24, '1tjj', 'Ganglioside GM2 activator', '2.0', 'out', 4.2, 0.3, 57, 4, -8.3, '', 1, 0, 'GM2 activator interacts with lipid bilayers (Giehl et al. 1999). Calculated orientation is in agreement with membrane binding mode proposed by Wright et al. (2003).', 'Extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.', '2006-03-17'),
(384, 149, 53, 24, '2agc', 'Ganglioside GM2 activator', '2.5', 'out', 3.2, 1.0, 54, 12, -5.3, '', 1, 0, 'GM2 activator interacts with lipid bilayers (Giehl et al. 1999). Calculated orientation is in agreement with membrane binding mode proposed by Wright et al. (2003).', 'Extracts single GM2 molecules from membranes and presents them in\r\n                         soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.', '2006-03-17'),
(385, 150, 92, 15, '1n7v', 'Adsorption protein p2', '2.2', 'out', 8.7, 0.4, 81, 1, -8.6, '', 1, 0, 'No direct experimental data about interactions with lipid bilayers.  Predicted membrane-binding site can be involved in protein-protein association.', 'The life cycle of the phage begins when the phage adsorbs to its receptor on the surface of the                                                                                                                                              host via the adsorption protein P2 and injects its DNA into the host cytoplasm. The prolin-rich fin of P2 is probably responsible for the initial interaction of the virus with its host (Xu et al. 2003). ', '2006-03-17'),
(386, 151, 14, 4, '1xwd', 'Follicle-stimulating hormone-receptor complex', '2.9', 'out', 3.1, 1.5, 63, 7, -7.2, '', 3, 0, 'This orientation may actually reflect association of the complex with 7-alpha-helical transmembrane domain.', 'Subunit C: N-terminal domain of follicle-stimulating hormone receptor (from GPCR family A).  Subunit A:  alpha chain of follicle-stimulating hormone (FSH-alpha). Subunit B: follitropin beta chain (FSH-beta). This is heterodimer of the common alpha chain and the unique beta chain that confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin. Compare with 1fl7.', '2006-03-17'),
(387, 152, 119, 23, '1pfo', 'Perfringolysin', '2.2', 'out', 4.4, 2.0, 38, 12, -6.7, '', 1, 0, 'W466 is embedded in the bilayer core, while W464 and W467 may be structurally important but do not interact strongly with membrane.  This is consistent with studies of Sekino-Suzuki et al. (1996) and Nakamura et al. (1998). The elongated protein is approximately perpendicular to the membrane based on FRET data (Ramachandran et al. 2005).', 'Sulfhydryl-activated toxin. Binds cholesterol (residue 459). Undergoes major conformational transitions and oligomerization upon association with membranes. Forms oligomers in the host membrane.', '2006-03-17'),
(388, 153, 133, 15, '1ok8', 'Major envelope glycoprotein E, ectodomain', '2.0', 'out', 5.2, 0.9, 0, 6, -9.5, '', 3, 0, 'Corresponds to host-cell membrane association mode proposed by Modis et al. (2004). Crystallized with detergent (N-UNDECYL-beta-D-MALTOPYRANOSIDE/ N-NONYL-beta-D-GLUCOPYRANOSIDE).', 'Calculated orientation reflects association with host-cell membrane rather than with viral membrane.  TM helices at the opposite side of the trimer (not present in the crystal structure) are anchored in viral membrane.', '2006-03-17'),
(389, 154, 180, 23, '1pt4', 'Kalata B2, segment 71-98 (repeat 1)', 'NMR', 'out', 4.6, 1.2, 83, 14, -9.2, '', 1, 0, '', 'Probably participates in a plant defense mechanism. Has hemolytic activity.', '2006-03-17'),
(390, 154, 180, 23, '1nb1', 'Kalata B1, segment 93-120', 'NMR', 'out', 5.3, 1.4, 81, 18, -5.5, '', 1, 0, 'Residues buried in the membrane core: W19-V21 and L27-V29 (based on locations of NH hydrogens). This is consistent with burial of loops W19-V21 and L27-V29 in DPC micelles (Shenkarev et al. 2006). Maximal membrane binding affinity is -6.4 kcal/mol (Kamimori et al. 2005).', 'Probably participates in a plant defense mechanism. Has antibiotic activity. ', '2006-03-17'),
(1109, 357, 14, 4, '2l34', 'TYRO protein tyrosine kinase-binding protein', 'NMR', 'A out', 31.8, 3.0, 14, 10, -36.0, '', 2, 2, '', '', '0000-00-00'),
(1108, 356, 9, 2, '3qe7', 'Uracil transporter UraA', '2.78', 'A in', 27.7, 1.2, 16, 0, -79.3, '', 1, 14, '', '', '0000-00-00'),
(393, 154, 223, 23, '1df6', 'Cycloviolacin O1', 'NMR', 'out', 4.1, 1.2, 63, 19, -5.9, '', 1, 0, '', '', '2006-03-17'),
(394, 154, 222, 23, '1vb8', 'Cycloviolacin O1', 'NMR', 'out', 6.9, 1.0, 88, 17, -9.7, '', 1, 0, '', '', '2006-03-17'),
(395, 154, 182, 23, '1r1f', 'Palicourein', 'NMR', 'out', 4.8, 1.4, 70, 19, -5.0, '', 1, 0, '', 'Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus.', '2006-03-17'),
(396, 157, 151, 23, '1c4e', 'Gurmarin', 'NMR', 'out', 5.2, 1.3, 17, 17, -4.8, '', 1, 0, 'No experimental data about interactions with lipid bilayers. ', 'Suppresses strongly the sweet taste responses in the rat with high specificity to sucrose, glucose, glycine, and saccharin. Tyr-13, Tyr-14, Trp-28, and Trp-29 are probably involved in interactions with receptor (Ota et al. 1998). Other sweetness-inhibiting substances (gymnemic acid, ziziphin); sweet proteins (monellin, thaumatin and mabinlin); and taste-modifying proteins (miraculin and curculin) were studied. Structures of monellin and thaumatin are in the PDB.', '2006-03-17'),
(397, 158, 14, 23, '1mr0', 'Agouti-related protein', 'NMR', 'out', 3.1, 2.0, 37, 18, -5.6, '', 1, 0, 'No experimental data about interactions with lipid bilayers. ', 'Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(398, 159, 125, 23, '1fyg', 'Omega conotoxin SO3', 'NMR', 'out', 2.9, 1.1, 76, 18, -3.5, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(399, 159, 121, 23, '1g1z', 'Delta conotoxin EVIA', 'NMR', 'out', 6.5, 1.9, 72, 18, -8.7, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(400, 159, 126, 23, '1f3k', 'Omega conotoxin TxVII', 'NMR', 'out', 2.8, 1.4, 57, 18, -4.5, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(401, 159, 126, 23, '1fu3', 'Delta conotoxin TxVIA', 'NMR', 'out', 6.5, 1.8, 25, 18, -8.3, '', 1, 0, '', '', '2006-03-17'),
(402, 159, 123, 23, '1rmk', 'Mu-O conotoxin MrVIB', 'NMR', 'out', 10.1, 1.3, 62, 19, -10.7, '', 1, 0, 'MrVIA and MrVIB are hydrophobic peptides that aggregate in aqueous solution but were solubilized in 50% acetonitrile/water (Daly et al. 2004).', '', '2006-03-17'),
(403, 160, 74, 23, '1agg', 'omega-Agatoxin', 'NMR', 'out', 2.5, 1.4, 57, 17, -5.0, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(404, 160, 152, 23, '1kqi', 'ACTX-HI:OB4219', 'NMR', 'out', 5.2, 1.2, 72, 15, -8.2, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(405, 160, 153, 23, '1vtx', 'Atracotoxin-hvI', 'NMR', 'out', 8.3, 1.0, 89, 10, -9.4, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(406, 160, 87, 23, '1qdp', 'Robustoxin', 'NMR', 'out', 1.8, 1.9, 86, 18, -5.0, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(407, 160, 291, 23, '1qk6', 'Huwentoxin-1', 'NMR', 'out', 2.7, 1.5, 88, 11, -5.1, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(408, 160, 183, 23, '1v7f', 'Phrixotoxin 1', 'NMR', 'out', 4.1, 1.2, 90, 16, -6.8, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(409, 160, 293, 23, '1d1h', 'Hanatoxin 1', 'NMR', 'out', 3.4, 1.7, 68, 15, -4.2, '', 1, 0, 'Results are consistent with the location of hanatoxin in the interfacial region of of the membrane and Trp30 facing towards the center of the lipid bilayer (Phillips et al. 2005). Fluorescence quenching shows  penetration of the protein into the acyl chain region of the lipid bilayer.', 'Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(410, 160, 293, 23, '1s6x', 'Voltage sensor toxin VSTx1', 'NMR', 'out', 4.4, 1.4, 79, 13, -6.3, '', 1, 0, 'Results are consistent with fluorescence and other data of Jung et al. (2005, 2006). Maximal membrane binding affinity is -6.8 kcal/mol (Jung et al. 2005).', 'Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(411, 161, 79, 23, '1lmr', 'Toxin Ado1', 'NMR', 'out', 3.1, 1.6, 60, 19, -4.7, '', 1, 0, '', '', '2006-03-17'),
(412, 162, 148, 23, '1ju8', 'Leginsulin', 'NMR', 'out', 11.3, 1.6, 21, 17, -8.6, '', 1, 0, '', '', '2006-03-17'),
(413, 162, 187, 23, '1p8b', 'Albumin 1 subunit B (Pab1)', 'NMR', 'out', 11.1, 0.9, 40, 13, -8.2, '', 1, 0, '', '', '2006-03-17'),
(414, 75, 49, 23, '1jza', 'Neurotoxin 2', '2.2', 'out', 4.0, 1.7, 68, 15, -5.6, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction. Binds to sodium channels and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission.', '2006-03-17'),
(415, 75, 114, 23, '1cn2', 'Toxin 2', 'NMR', 'out', 2.9, 1.6, 81, 16, -5.1, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction. Binds to sodium channels and shift the voltage of activation toward more negative potentials.', '2006-03-17'),
(416, 75, 105, 23, '1djt', 'Alpha-like neurotoxin BmK-I', '1.2', 'out', 3.8, 0.9, 90, 15, -6.9, '', 2, 0, '', 'Membrane-binding site participates in protein-protein interaction. Binds to sodium channels and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals and insects. BmK-I is 6-fold more toxic than BmK-II.', '2006-03-17'),
(417, 75, 106, 23, '1dq7', 'Neurotoxin', '2.2', 'out', 5.9, 1.8, 88, 18, -8.1, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(418, 75, 217, 23, '1npi', 'Toxin VII', '1.1', 'out', 4.6, 1.5, 52, 16, -6.7, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction. Binds voltage-independently to sodium channels and shift the voltage of activation toward more negative potentials. This toxin is active against both mammals and insects.', '2006-03-17'),
(419, 75, 105, 23, '1kv0', 'Tx10 alpha-like toxin', '1.4', 'out', 1.9, 1.1, 83, 11, -4.6, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(420, 75, 165, 23, '1fh3', 'LQH III alpha-like toxin', 'NMR', 'out', 3.6, 1.5, 83, 16, -5.2, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(421, 163, 165, 23, '2crd', 'Charybdotoxin', 'NMR', 'out', 1.1, 1.5, 86, 15, -3.2, '', 1, 0, 'Experimental membrane bindig affinity is -2.0 kcal/mol (0.2 M KCl) to -3.6 kcal/mol (0.1 M KCl), and up to -8 kcal/mol at lower non-physiological ionic strength (Ben-Tal et al. 1997).', 'Membrane-binding site participates in association with potassium channel (see structure of the complex, 2a9h).', '2006-03-17'),
(422, 163, 104, 23, '1sis', 'Toxin I5a', 'NMR', 'out', 3.1, 1.4, 74, 16, -4.4, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(423, 76, 85, 23, '1ozz', 'Defensin ARD1', 'NMR', 'out', 4.9, 1.7, 31, 17, -7.1, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(424, 76, 199, 23, '1l4v', 'Sapecin', 'NMR', 'out', 5.4, 1.5, 84, 18, -5.1, '', 1, 0, 'The following residues are buried from water in the membrane, according to NMR study: L5, G8, G10-H13, A15-A18, C20-L22, and G27-Y29 (Takeuchi et al. 2004). The following residues are buried in the hydrophobic slab according to the calculations: L6-H19 and L21-L22 (based on locations of NH hydrogens), whereas G27-Y29 segment occupies interfacial region near the calculated hydrophobic boundary.', 'Sapesin of Sarcophaga peregrina (1l4v) and defensin A of Phormia terranovae (1ica) differ only by a single A34G substitution.', '2006-03-17'),
(425, 164, 195, 23, '1ayj', 'Antifungal protein 1', 'NMR', 'out', 11.0, 1.9, 39, 19, -7.4, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(426, 164, 187, 23, '1jkz', 'Defensin 1', 'NMR', 'out', 3.5, 1.6, 8, 19, -5.4, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(427, 191, 14, 23, '1lpb', 'Pancreatic lipase, complex with colipase from Pig', '2.4', 'out', 9.2, 0.4, 89, 2, -24.2, '', 2, 0, '', '', '2006-03-17'),
(428, 191, 57, 23, '1eth', 'Pancreatic lipase, complex with colipase', '2.8', 'out', 13.6, 0.2, 90, 3, -13.3, '', 2, 0, 'Maximal membrane binding affinity of this lipase without colipase is -11 kcal/mol (Tsujita and Brockman 1987), which is less than corresponding calculated transfer energy(-16.1 kcal/mol).  Without colipase, this lipase penetrates into the membrane deeper and in a slightly differnt orientation.', '', '2006-03-17'),
(429, 165, 14, 23, '1fle', 'Elafin, complex with elastase from Pig', '1.9', 'out', 4.4, 2.0, 52, 11, -6.3, '', 2, 0, 'No direct experimental data. The calculated orientation is in agreement with probable formation of membrane-anchoring helix by N-terminal segment of elafin, which is missing in this crystal structure (Efremov et al. 2001). ', 'Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis.', '2006-03-17'),
(430, 165, 176, 23, '1udk', 'Nawaprin', 'NMR', 'out', 6.3, 1.0, 81, 8, -7.3, '', 1, 0, '', '', '2006-03-17'),
(431, 69, 231, 23, '1tgx', 'Cytotoxin 1 ( Cardiotoxin gamma)', '1.5', 'out', 6.7, 1.0, 59, 12, -10.0, '', 1, 0, 'Maximal membrane-binding affinity is -9.6 kcal/mol (Batenburg et al. 1985). Fluorescence quenching shows  penetration of the protein into the hydrocarbon interior of the lipid bilayer. The study was probably done for D57N mutant, the toxin from Naja mossambica mossambica (NMR model 2cxx). ', 'Shows cytolytic activity (By similarity).', '2006-03-17'),
(432, 69, 174, 23, '1cdt', 'Cardiotoxin V4II', '2.5', 'out', 4.2, 1.0, 46, 14, -6.9, '', 2, 0, '', 'Shows cytolytic activity.', '2006-03-17'),
(434, 69, 54, 23, '1ug4', 'Cardiotoxin VI', '1.6', 'out', 6.4, 0.9, 62, 4, -12.2, '', 1, 0, '', 'Shows cytolytic activity (By similarity).', '2006-03-17'),
(1369, 402, 366, 1, '3s0x', 'Peptidase A24B, FlaK domain protein', '3.6', 'A out', 31.8, 1.6, 40, 2, -67.7, '', 1, 6, '', '', '0000-00-00'),
(1370, 15, 14, 4, '3sn6', 'Beta-2 adrenergic receptor, Gs protein complex', '3.2', 'R out', 30.2, 1.7, 11, 2, -67.8, '', 1, 7, '', 'Includes Galpha and Ggamma (bovine), Gbeta (rat) and an atibody fragment (subunit N). Lysozyme domain was removed.', '0000-00-00'),
(1371, 403, 28, 3, '3rbh', 'Alginate export protein', '2.30', 'A in', 23.4, 1.2, 4, 0, -72.0, '', 1, 18, '', '', '0000-00-00'),
(1372, 404, 55, 14, '2xa7', 'Subunit mu of AP-2 clatrin adaptor complex, open conformation', '3.1', 'in', 3.1, 2.2, 84, 14, -5.9, '', 4, 0, '', '', '0000-00-00'),
(436, 69, 175, 23, '1ffj', 'Cardiotoxin II (cytotoxin II)', 'NMR', 'out', 7.9, 0.8, 56, 5, -13.7, '', 1, 0, 'Interaction of the protein with DPC micelles was confined mainly to the tips of three loops, 4-12, 22-39 and 46-50 (Dubovskii et al. 2001).  This is generally consisten with the set of calculated membrane-embedded residues: L6-F10, F25-K36, and S46-V49 (based on locations of NH hydrogens). However, chemical shifts of many residues (primarily Lys and Arg) in the membrane interfacial region have also been affected by the binding. Independent Monte Carlo simulations of the protein led to similar results (Efremov et al. 2002, Dubovskii et al. 2005).', 'Shows cytolytic activity (By similarity).', '2006-03-17'),
(437, 69, 54, 23, '1h0j', 'Cardiotoxin III (cytotoxin 3)', '1.9', 'out', 7.1, 0.9, 59, 7, -11.3, '', 1, 0, 'The protein was crystallized with detergent. It binds to membrane in a tilted orientation, in agreement with FTIR data for lipid monolayers (Huang et al. 2003).  Also consistent with results of simulations (Efremov et al. 2004). ', 'Shows cytolytic activity (By similarity), and inhibits protein kinases C. Can cause leakage in vesicles.', '2006-03-17'),
(438, 69, 181, 23, '1txa', 'Toxin B', 'NMR', 'out', 2.6, 1.5, 51, 16, -5.6, '', 1, 0, '', 'Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (only alpha-7 alpha-8 alpha-9) nicotinic acetylcholine receptors (By similarity).', '2006-03-17'),
(439, 166, 132, 23, '1drs', 'Dendroaspin (mambin)', 'NMR', 'out', 3.3, 1.5, 87, 12, -6.5, '', 1, 0, '', 'Inhibits ADP-induced platelet aggregation and inhibits the binding of purified platelet fibrinogen receptor GPIIb-IIIa to immobilized fibrinogen.', '2006-03-17'),
(440, 70, 14, 23, '1ijv', 'Beta-defensin 1', '1.2', 'out', 3.5, 1.9, 74, 17, -5.4, '', 1, 0, '', '', '2006-03-17'),
(441, 70, 14, 23, '1kj6', 'Beta-defensin 3', 'NMR', 'out', 2.7, 1.3, 18, 18, -5.1, '', 1, 0, '', '', '2006-03-17'),
(442, 70, 53, 23, '1e4t', 'Beta-defensin 7', 'NMR', 'out', 3.6, 1.4, 13, 19, -5.2, '', 1, 0, '', '', '2006-03-17'),
(443, 70, 53, 23, '1e4r', 'Beta-defensin 8', 'NMR', 'out', 2.8, 1.1, 74, 19, -5.5, '', 1, 0, '', '', '2006-03-17'),
(444, 70, 6, 23, '1bnb', 'Beta-defensin 12', 'NMR', 'out', 6.0, 1.6, 88, 15, -10.8, '', 1, 0, '', '', '2006-03-17'),
(445, 70, 84, 23, '1ut3', 'Spheniscin-2', 'NMR', 'out', 3.6, 1.6, 44, 17, -6.2, '', 1, 0, '', 'Defensin of King penguin. Has antifungal activity and antibacterial activity against Gram-positive and Gram-negative bacteria. Involved in the process of food preservation in the stomach during the incubation fast. May also be present during infection.', '2006-03-17'),
(446, 70, 25, 23, '1ews', 'Alpha-defensin corticostatin-related peptide RK-1', 'NMR', 'out', 4.7, 1.1, 18, 17, -4.4, '', 1, 0, '', '', '2006-03-17'),
(447, 239, 81, 23, '1bds', 'Antihypertensive protein BDS-1', 'NMR', 'out', 5.6, 0.8, 83, 9, -9.6, '', 1, 0, '', 'Blocks specifically the Kv3.4 potassium channel. Reduces blood pressure.', '2006-03-17'),
(448, 239, 207, 23, '1shi', 'Sea anemone neurotoxin-1', 'NMR', 'out', 8.0, 1.0, 87, 17, -5.9, '', 1, 0, '', '', '2006-03-17'),
(449, 239, 81, 23, '1atx', 'Sea anemone toxin IA', 'NMR', 'out', 4.5, 1.7, 63, 12, -6.1, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(450, 239, 82, 23, '1ahl', 'Anthopleurin-A', 'NMR', 'out', 3.7, 1.2, 86, 11, -7.3, '', 1, 0, '', '', '2006-03-17'),
(451, 239, 82, 23, '1apf', 'Anthopleurin-B', 'NMR', 'out', 6.4, 1.3, 78, 19, -7.1, '', 1, 0, '', '', '2006-03-17'),
(452, 167, 81, 23, '1ans', 'Neurotoxin III', 'NMR', 'out', 3.3, 1.4, 50, 15, -4.7, '', 1, 0, '', 'Binds specifically to the sodium channel.', '2006-03-17'),
(453, 168, 6, 23, '1h8p', 'Collagen-binding type II domain of seminal plasma protein PDC-109', '1.8', 'out', 10.5, 0.9, 87, 7, -16.6, '-12.', 2, 0, 'Penetrates up to the level of C-14 into the hydrophobic interior of the membrane (Ramakrishnan et al. 2001). Membrane binding can be modulated by cholesterol ( Swamy et al. 2002). Consistent with orientation proposed by Wah et al. (2002). ', 'Major component of seminal plasma. Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins.  The dimer has translational rather than C2 symmetry.', '2006-03-17'),
(454, 169, 139, 2, '1hpi', 'High potential iron protein', '1.8', 'out', 2.7, 1.0, 89, 12, -4.4, '', 1, 0, 'May act as a membrane-associated electron shuttle between cytochrome bc1 complex and photosynthetic reaction center in purple bacteria (Lieutaud et al. 2003).', '', '2006-03-17'),
(455, 73, 9, 2, '1f76', 'Dihydroorotate dehydrogenase', '2.5', 'in', 3.7, 0.8, 24, 8, -8.7, '', 1, 0, '', 'In bacteria, DHOdease is located on the inner side of the cytosolic membrane. In some yeasts, it is a cytosolic protein, while in other eukaryotes it is found in the mitochondria.', '2006-03-17'),
(456, 73, 55, 5, '1uum', 'Dihydroorotate dehydrogenase', '2.3', 'in', 6.9, 0.4, 50, 6, -6.3, '', 1, 0, '', 'In bacteria, DHOdease is located on the inner side of the cytosolic membrane. In some yeasts, it is a cytosolic protein, while in other eukaryotes it is found in the mitochondria.', '2006-03-17'),
(457, 73, 38, 11, '1gox', 'Glycolate oxidase', '2.0', 'out', 4.1, 0.0, 90, 0, -18.5, '', 4, 0, '', '', '2006-03-17'),
(458, 170, 14, 24, '1ogs', 'Glucosylceramidase', '2.0', 'out', 4.2, 1.1, 89, 4, -9.0, '', 1, 0, '', 'Lysosomal enzyme glucosylceramidase facilitates the hydrolysis of glucosylceramide to ceramide and glucose. Peripheral membrane protein. Its catalytic activity is regulated by saposin C.', '2006-03-17'),
(459, 171, 29, 1, '1vff', 'Beta-glycosidase', '2.5', 'in', 3.9, 1.6, 39, 10, -9.7, '', 1, 0, 'Crystallization with detergent (TRITON X-100). The calculated orientation is in agreement with membrane-binding mode proposed by Akiba et al. (2004).', '', '2006-03-17'),
(460, 172, 55, 4, '1djx', 'Phospholipase C-delta isoform 1', '2.3', 'in', 4.1, 0.9, 68, 5, -7.2, '', 1, 0, 'Maximal membrane binding afiinity of an isolated C2 domain of this protein is -12 kcal/mol (Ananthanarayanan et al. 2002), due to specific protein-lipid binding and electrostatics.', 'Mediates production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). This protein contains TIM barrel (catalytic) domain, C2 domain, PH domain (1mai), and two EF-hand domains. This structure represents monomer. In crystal, the protein forms a loosely packed dimer with a continuous planar nonpolar surface coming from the monomers. Thus, the dimer might actually exist in the membrane-associated state, even though it was identified as unstable by PQS.', '2006-03-17'),
(461, 173, 70, 23, '2ptd', 'Phosphatidylinositol-specific phospholipase C', '2.0', 'out', 4.3, 1.1, 64, 12, -8.3, '', 1, 0, 'Membrane embedded residues are P42, I43, W47, T240, A241 and W242. This is consistent with the important role of I43, W47 and W242 for association with the membrane (Feng et al. 2003). Rescue mutation G238W (Feng et al. 2003) is also consistent with the calculated protein orientation. Maximal membrane binding affinity is -5.6 kcal/mol (Feng et al. 2003).', 'Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors.', '2006-03-17'),
(462, 173, 168, 23, '2plc', 'Phosphatidylinositol-specific phospholipase C', '2.0', 'out', 7.5, 1.0, 80, 13, -8.7, '', 1, 0, '', '', '2006-03-17'),
(463, 175, 6, 5, '1e6e', 'Adrenodoxin reductase of mitochondrial p450 systems, complex with adrenodoxin', '2.3', 'in', 2.3, 1.0, 11, 2, -4.1, '', 2, 0, 'This is known membrane-associated protein.', 'Serves as the first electron transfer protein in all the mitochondrial p450 systems. ', '2006-03-17'),
(465, 176, 177, 5, '1sez', 'Protoporphyrinogen oxidase', '2.9', 'in', 2.2, 1.0, 50, 3, -7.0, '', 1, 0, '', '', '2006-03-17'),
(1042, 13, 36, 5, '2xok', 'F1C10 ATP synthase', '3.01', 'K in', 35.3, 1.3, 0, 0, -58.9, '', 10, 20, '', '', '0000-00-00'),
(1044, 16, 59, 1, '3ne2', 'Aquaporin AqpM', '3.00', 'A in', 31.2, 1.3, 0, 0, -143.5, '', 4, 24, '', '', '0000-00-00'),
(1045, 351, 9, 2, '3k07', 'Efflux transporter CusA, apo-protein', '3.52', 'A in', 27.4, 1.2, 0, 0, -166.7, '', 3, 33, '', '', '0000-00-00'),
(1046, 351, 9, 2, '3kss', 'Efflux transporter CusA, Cu(i) complex', '3.88', 'A in', 28.8, 0.5, 0, 0, -147.7, '', 3, 33, '', '', '0000-00-00'),
(1182, 370, 215, 26, '1a1p', 'Compstatin', 'NMR', 'out', 3.4, 1.9, 72, 18, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1183, 371, 14, 4, '1btq', 'Band 3 anion transport protein SLC4A1, fragment  405-424', 'NMR', 'A out', 13.6, 2.1, 67, 11, -22.5, '', 1, 0, '', '', '0000-00-00'),
(1184, 371, 14, 4, '1bts', 'Band 3 anion transport protein SLC4A1, fragment 436-456', 'NMR', 'out', 9.2, 0.3, 84, 2, -14.8, '', 1, 0, '', '', '0000-00-00'),
(468, 178, 14, 9, '1r5l', 'Alpha-tocopherol transfer protein, closed state with ligand', '1.5', 'in', 4.3, 1.0, 77, 9, -11.8, '', 1, 0, '', 'Binds alpha-tocopherol and enhances its transfer between separate membranes.', '2006-03-17'),
(469, 179, 14, 5, '1efv', 'Electron transfer flavoprotein', '2.1', 'in', 4.6, 1.3, 79, 12, -4.6, '', 2, 0, '', 'The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase.', '2006-03-17'),
(470, 179, 27, 2, '1efp', 'Electron transfer flavoprotein', '2.6', 'in', 4.3, 1.1, 90, 13, -4.8, '', 2, 0, '', 'The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase.', '2006-03-17'),
(471, 180, 6, 14, '1auv', 'Synapsin I', '2.1', 'in', 1.9, 1.1, 86, 11, -5.2, '', 1, 0, 'Membrane-interacting residues have been identified as coming from the regions 166-192, 233-258, or/and 278-327 (Cheetham et al. 2001) in agreement with our results (residues L168, V172, and L297 are buried in the membrane core). ', 'Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. ', '2006-03-17'),
(472, 181, 145, 2, '1e6c', 'Shikimate kinase', '1.8', 'in', 2.6, 1.8, 90, 12, -5.8, '', 2, 0, 'No experimental data about association with lipid bilayers. Dimerization modes of shikimate kinases 1e6c and 1via are different.', '', '2006-03-17'),
(473, 181, 107, 2, '1via', 'Shikimate kinase', '1.5', 'in', 3.9, 1.4, 89, 11, -5.0, '', 2, 0, 'No experimental data about association with lipid bilayers. Dimerization modes of shikimate kinases 1e6c and 1via are different.', '', '2006-03-17'),
(1338, 66, 14, 23, '3fw5', 'Neutrophil gelatinase-associated lipocalin', '2.3', 'out', 2.0, 1.2, 45, 9, -3.1, '', 1, 0, '', '', '0000-00-00'),
(475, 183, 205, 23, '1oxw', 'Patatin', '2.2', 'out', 3.9, 2.0, 28, 11, -6.5, '', 1, 0, '', 'Patatin is a nonspecific lipid acyl hydrolase that accounts for approximately 40% of the total soluble protein in mature potato tubers, and it has potent insecticidal activity against the corn rootworm. It has a Ser-Asp catalytic dyad and an active site like that in human cytosolic phospholipase A2 (Rydel et al. 2003).', '2006-03-17'),
(476, 184, 218, 4, '1ea5', 'Acetylcholinesterase', '1.8', 'out', 1.8, 1.1, 34, 5, -4.7, '', 1, 0, 'GPI-anchor amidated serine 564, consitent with calculated orientation.', 'Isoform H form is attached to the membrane by a GPI-anchor. Isoform T is attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.', '2006-03-17'),
(477, 184, 53, 4, '1n5m', 'Acetylcholinesterase', '2.2', 'out', 3.7, 1.3, 28, 6, -6.1, '', 1, 0, '', 'Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes.', '2006-03-17'),
(478, 184, 14, 4, '1f8u', 'Acetylcholinesterase', '2.9', 'out', 2.6, 1.0, 60, 9, -7.3, '', 2, 0, '', '', '2006-03-17'),
(479, 184, 14, 4, '1p0i', 'Butyryl cholinesterase', '2.0', 'out', 3.1, 0.8, 43, 10, -6.4, '', 1, 0, '', '', '2006-03-17'),
(480, 184, 6, 23, '1aql', 'Bile-salt activated lipase', '2.8', 'out', 5.7, 1.1, 78, 7, -9.6, '', 1, 0, '', 'Different conformations of loops on 1aql and 1akn.', '2006-03-17'),
(481, 184, 14, 23, '1f6w', 'Bile-salt activated lipase', '2.3', 'out', 1.8, 0.5, 81, 10, -5.1, '', 1, 0, '', '', '2006-03-17'),
(482, 185, 21, 22, '1f0n', 'Antigen 85b', '1.8', 'out', 3.7, 0.9, 33, 7, -7.4, '', 1, 0, '', 'Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure necessary for maintaining cell wall integrity.', '2006-03-17'),
(483, 185, 21, 22, '1va5', 'Antigen 85c', '2.02', 'out', 4.2, 0.2, 34, 3, -8.2, '', 1, 0, '', 'Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure necessary for maintaining cell wall integrity.', '2006-03-17'),
(484, 185, 21, 22, '1sfr', 'Antigen 85a', '2.7', 'out', 2.8, 0.8, 27, 9, -7.5, '', 1, 0, '', 'Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure necessary for maintaining cell wall integrity.', '2006-03-17'),
(485, 186, 14, 23, '1hlg', 'Gastric lipase', '3.0', 'out', 3.2, 1.4, 6, 12, -5.6, '', 1, 0, '', '', '2006-03-17'),
(486, 186, 111, 23, '1k8q', 'Gastric lipase, open (active) state', '2.7', 'out', 7.2, 0.5, 78, 6, -12.6, '', 1, 0, '', '', '2006-03-17'),
(487, 187, 6, 24, '1eh5', 'Palmitoyl protein thioesterase 1', '2.5', 'out', 5.3, 0.9, 59, 6, -8.1, '', 1, 0, '', '', '2006-03-17'),
(488, 187, 14, 24, '1pja', 'Palmitoyl protein thioesterase 2', '2.7', 'out', 3.7, 1.6, 60, 15, -4.6, '', 1, 0, '', '', '2006-03-17'),
(489, 291, 209, 23, '1jfr', 'Lipase', '1.9', 'out', 5.0, 1.3, 60, 10, -6.4, '', 1, 0, '', '', '2006-03-17'),
(490, 189, 108, 23, '1lbs', 'Triacylglycerol lipase', '2.6', 'out', 3.7, 1.0, 76, 6, -12.7, '', 1, 0, '', '', '2006-03-17'),
(491, 189, 197, 23, '3tgl', 'Triacylglycerol lipase, closed (inactive) state', '1.9', 'out', 2.7, 1.1, 39, 7, -5.8, '', 1, 0, '', 'There are two alternative membrane binding modes.', '2006-03-17'),
(492, 189, 197, 23, '4tgl', 'Triacylglycerol lipase, open (active) state', '2.6', 'out', 8.8, 0.9, 64, 11, -18.2, '', 1, 0, '', '', '2006-03-17'),
(493, 189, 160, 23, '1ein', 'Triacylglycerol lipase, open (active) state', '3.0', 'out', 8.1, 0.8, 63, 4, -14.5, '', 1, 0, 'This lipase associates with membrane by its hydrophobic surface (near the bound phosphatidyl choline) according to our calculations. That is inconsistent with two different orientations of this lipase described in ESR studies (Hedin et al. 2002, 2005). Under the experimental conditions, the protein was probably in the closed state (see 1dt5 and 1tib) and associated electrostatically only with membrane surface (no penetration) through the alternative charged spots, since the ionic strength was very low. Authors used "exposure factors" of spin-labeled residues (determined using the negatively charged spin-relaxation agent Crox), instead of the standard membrane penetration depth parameter, which is based on the contrast between two uncharged polar and nonpolar agents. The latter parameter is more reliable as follows from EPR studies of transmembrane proteins and C2 domains.        ', '', '2006-03-17'),
(494, 189, 198, 23, '1lgy', 'Triacylglycerol lipase', '2.2', 'out', 1.9, 1.8, 33, 16, -4.8, '', 1, 0, '', '', '2006-03-17'),
(495, 189, 110, 23, '1lpp', 'Lipase 1, open (active) state', '2.0', 'out', 10.0, 0.4, 83, 1, -28.0, '', 1, 0, '', '', '2006-03-17'),
(496, 189, 110, 23, '1gz7', 'Lipase 2', '1.9', 'out', 4.8, 1.3, 87, 10, -8.5, '', 1, 0, '', 'Two alternative membrane association modes.', '2006-03-17'),
(497, 189, 109, 23, '1cle', 'Type-B carboxylesterase/lipase', '2.0', 'out', 10.2, 0.0, 83, 0, -24.7, '', 1, 0, '', '', '2006-03-17'),
(498, 190, 90, 23, '1isp', 'Lipase A', '1.3', 'out', 1.9, 0.8, 59, 12, -5.2, '', 1, 0, '', '', '2006-03-17'),
(499, 190, 191, 23, '1qge', 'Lipase', '1.7', 'out', 3.7, 0.9, 24, 3, -7.7, '', 1, 0, '', '', '2006-03-17'),
(500, 190, 103, 23, '5lip', 'Lipase', '2.9', 'out', 9.0, 1.0, 46, 2, -30.6, '', 1, 0, '', '', '2006-03-17'),
(501, 190, 28, 23, '1ex9', 'Lipase, open (active) state', '2.5', 'out', 11.0, 1.0, 52, 5, -30.0, '', 1, 0, '', '', '2006-03-17'),
(502, 190, 191, 23, '1cvl', 'Lipase', '1.6', 'out', 9.9, 1.0, 53, 9, -8.7, '', 1, 0, '', '', '2006-03-17'),
(503, 190, 89, 23, '1ku0', 'Lipase L1', '2.0', 'out', 4.0, 0.6, 23, 9, -8.9, '', 1, 0, '', '', '2006-03-17'),
(504, 190, 89, 23, '1ji3', 'Lipase L1, different isoform', '2.2', 'out', 3.5, 1.7, 22, 10, -8.0, '', 1, 0, '', '', '2006-03-17'),
(505, 191, 113, 23, '1gpl', 'Pancreatic lipase', '2.1', 'out', 5.8, 1.0, 86, 9, -7.8, '', 1, 0, '', '', '2006-03-17'),
(506, 191, 55, 23, '1bu8', 'Pancreatic lipase', '1.8', 'out', 3.5, 1.3, 87, 10, -6.1, '', 1, 0, '', '', '2006-03-17'),
(507, 192, 147, 23, '1oxm', 'Cutinase 1', '2.3', 'out', 6.8, 1.1, 36, 15, -9.1, '', 1, 0, '', 'Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.', '2006-03-17'),
(508, 193, 9, 2, '1f0k', 'Peptidoglycan biosynthesis glycosyltransferase MurG', '1.9', 'in', 5.3, 1.2, 55, 7, -8.6, '', 1, 0, '', 'This is a peripheral membrane protein involved in cell wall formation. Catalyzes the transfer of a GlcNAc subunit. 1f0k and 1nlm have different conformations of loop 63-79 that interacts with membrane. ', '2006-03-17'),
(509, 194, 14, 5, '1hrk', 'Ferrochelatase', '2.0', 'in', 2.7, 0.1, 90, 0, -9.9, '', 2, 0, 'Membrane-associated protein. Crystallization with detergent (SODIUM CHOLATE). Results are consitent with orientation proposed by Wu et al. (2001).', 'Catalyzes the ferrous insertion into protoporphyrin IX: protoporphyrin + Fe(2+) = protoheme + 2 H(+).', '2006-03-17'),
(511, 196, 169, 9, '1z9h', 'Microsomal prostaglandin E synthase 2', '2.6', 'in', 4.8, 0.5, 90, 4, -15.7, '', 2, 0, 'Membrane-associated protein. Crystallized with N-DODECYL-beta-D-MALTOPYRANOSIDE. \r\nCalculated orientation is compatible with the proposed membrane-anchoring role of missing N-terminal segment of the protein (Yamada et al 2005).  An opposite orientation of the protein has been proposed based on a secondary structure prediction of the missing segment (Yamada et al 2005).  A TM helix might be present in the missing segment, as indicated in UniProt.  ', 'Isomerase that catalyzes the conversion of unstable intermediate of prostaglandin E2 H2 (PGH2) into the more stable prostaglandin E2 (PGE2) form. ', '2006-03-17'),
(512, 197, 100, 8, '1coy', 'Cholesterol oxidase', '1.8', 'out', 4.4, 1.1, 43, 10, -6.8, '', 1, 0, 'The calculated protein orientation is in agreement with a fluorescence labeling study of a residue in position 81 (Chen et al. 2000). Fluorescence quenching shows  penetration of the protein into the hydrocarbon interior of the lipid bilayer. Maximal membrane binding affinity is -4.8 kcal/mol (Chen et al. 2000).', '', '2006-03-17'),
(513, 198, 229, 8, '2bng', 'Epoxide Hydrolase', '2.5', 'out', 8.2, 0.6, 88, 4, -24.0, '', 2, 0, 'No experimental data about interaction of this epoxide hydrolase from Mycobacteria with lipid bilayers. However, mammalian microsomal epoxide hydrolases associate with membranes (Ivanov et al. 1993).', '', '2006-03-17'),
(1181, 366, 14, 6, '2yd0', 'Endoplasmic reticulum aminopeptidase 1, different conformation', '2.70', 'out', 4.1, 2.2, 59, 8, -4.6, '', 1, 0, '', '', '0000-00-00'),
(1178, 366, 14, 6, '3mdj', 'Endoplasmic reticulum aminopeptidase 1', '2.95', 'A out', 1.9, 3.6, 63, 10, -4.6, '', 1, 0, '', '', '0000-00-00'),
(1179, 367, 256, 4, '2xu0', 'Erythrocyte membrane protein 1', '2.06', 'A out', 3.3, 6.0, 75, 45, -3.2, '', 1, 0, '', '', '0000-00-00'),
(1180, 367, 256, 4, '3c64', 'Erythrocyte membrane protein 1 variant', '2.40', 'out', 5.3, 2.5, 52, 3, -9.6, '', 1, 0, '', 'This is a calculated binding mode of monomer. Homodimer was also predicted to interact with lipid bilayer, but in a different orientation.  ', '0000-00-00'),
(516, 200, 53, 10, '1bg1', 'STAT3b', '2.2', 'in', 2.4, 10.4, 90, 10, -8.2, '', 2, 0, 'No experimental data about interactions with lipid bilayers. ', 'Membrane-binding site may participate in protein-protein interaction.', '2006-03-17'),
(517, 201, 25, 4, '1c44', 'Sterol carrier protein 2', '1.8', 'in', 3.7, 1.2, 74, 17, -4.8, '', 1, 0, '', 'Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. ', '2006-03-17'),
(518, 202, 36, 4, '1iou', 'Synaptobrevin homolog 1', 'NMR', 'in', 3.4, 1.1, 79, 12, -6.0, '', 1, 0, 'This is a membrane-assocuiated protein. Location of S-farnesyl cysteine 197 (at the end of v-SNARE doain) is compatible with the calculated orientation. Orientations of this domain here and in the signal recognition particle alpha-beta complex (1nrj) are similar. ', 'This is structure of longin domain (3-140). It does not include v-SNARE coiled-coil homology domain (residues 140-200).', '2006-03-17'),
(520, 204, 53, 4, '1jss', 'Cholesterol-regulated Start protein 4  (StarD4)', '2.2', 'in', 2.7, 1.4, 68, 10, -5.2, '', 1, 0, '', 'May be involved in the intracellular transport of sterols or other lipids.', '2006-03-17'),
(521, 204, 14, 4, '1ln1', 'Phosphatidylcholine transfer protein', '2.4', 'in', 3.8, 1.8, 53, 16, -4.8, '', 1, 0, '', 'Catalyzes the transfer of phosphatidylcholine between membranes.', '2006-03-17'),
(522, 205, 167, 23, '1zwx', 'Sphingomyelinase C', '1.9', 'out', 6.2, 0.5, 55, 1, -10.1, '', 1, 0, 'Consistent with membrane-association mode proposed by Openshaw et al. (2005).', '', '2006-03-17'),
(523, 206, 128, 23, '1ejg', 'Crambin', '0.5', 'out', 4.0, 1.7, 79, 15, -7.0, '', 1, 0, '', '', '2006-03-17'),
(524, 206, 220, 23, '1bhp', 'beta-Purothionin', '1.7', 'out', 2.9, 2.0, 56, 19, -4.8, '', 1, 0, '', '', '2006-03-17'),
(525, 206, 156, 23, '1nbl', 'Hellethionin D', 'NMR', 'out', 2.2, 0.9, 45, 9, -7.4, '', 1, 0, '', '', '2006-03-17'),
(526, 77, 14, 12, '1hyi', 'Early endosome antigen 1 (EEA1), monomer', 'NMR', 'in', 3.0, 2.0, 24, 17, -3.5, '', 1, 0, 'This orientation is in agreement with studies of monomeric FYVE domain in micelles, which shows that exposed V21 and T22 residues are buried in the hydrophobic core (Kutateladze and Overduin 2001, Brunecky et al. 2005). However, the orientations of monomeric FYVE domains change when they form a dimer through an additional coiled-coil domain (see 1joc). ', 'This orientation is in agreement with results of computational modeling of FYVE domains based on electrostatic interactions (Diraviyam et al. 2003). However, FYVE domain penetrates by ~15A deeper into the membrane according to our results: nonpolar residues are inserted in the membrane hydrocarbon core, not in the head group region.', '2006-03-17'),
(527, 207, 166, 23, '1cw6', 'Leucocin A', 'NMR', 'out', 3.6, 1.1, 90, 16, -6.2, '', 1, 0, 'Studied in detergent (DPC).', '', '2006-03-17'),
(528, 207, 163, 23, '1ohm', 'Sakacin P', 'NMR', 'out', 1.8, 1.1, 90, 11, -4.4, '', 1, 0, 'Studied in detergent (DPC).', '', '2006-03-17'),
(529, 208, 93, 23, '1kv4', 'Moricin', 'NMR', 'out', 6.1, 0.6, 77, 14, -10.3, '', 1, 0, '', 'Has antibacterial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure.', '2006-03-17'),
(530, 208, 206, 23, '1x22', 'Moricin', 'NMR', 'out', 4.4, 1.1, 70, 5, -9.2, '', 1, 0, '', 'Antibacterial peptide.', '2006-03-17'),
(531, 209, 162, 23, '1myu', 'Kassinin', 'NMR', 'out', 3.4, 1.5, 59, 16, -4.5, '', 1, 0, '', 'Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.', '2006-03-17'),
(532, 209, 140, 23, '1mxq', 'Eledoisin', 'NMR', 'out', 2.9, 1.7, 59, 19, -5.0, '', 1, 0, '', 'Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.', '2006-03-17'),
(533, 209, 11, 23, '1n6t', 'Neurokinin A', 'NMR', 'out', 6.8, 1.2, 60, 17, -4.9, '', 1, 0, '"Deuterating substance P and neurokinin A at their carboxy-terminals, our results show two populations of label for each peptide. One is very close to the water-hydrocarbon interface, the other some 13 Angstrom deeper" (Darkes et al. 1997).', 'Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.', '2006-03-17'),
(534, 210, 155, 23, '1p0l', 'Antimicrobial peptide HP', 'NMR', 'out', 5.3, 0.6, 79, 9, -10.5, '', 1, 0, '', 'An antibacterial peptide originating from the N-terminal end of ribosomal protein L1. Released by H.pylori to kill E.coli and B.megaterium.', '2006-03-17'),
(535, 211, 57, 23, '1icy', 'Neuropeptide Y analogue', 'NMR', 'out', 6.4, 1.1, 73, 9, -8.2, '', 1, 0, 'Penetration of amphiphilic helix 17-32 in the membrane interior was supported by  spin-labeling study (Thomas et al. 2005). Membrane binding affinity at pH=7.4 was -4.7 kcal/mol (Thomas et al. 2005).', '', '2006-03-17'),
(536, 212, 57, 23, '1gcn', 'Glucagon', '3.0', 'out', 5.3, 1.0, 78, 12, -6.6, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17');
INSERT INTO `protein` (`id`, `family_id`, `species_id`, `membrane_id`, `pdbid`, `name`, `resolution`, `topology`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`, `tau`, `numsubunits`, `numstrands`, `verification`, `comments`, `date_added`) VALUES
(537, 213, 14, 23, '1lbj', 'Motilin', 'NMR', 'out', 8.6, 1.6, 51, 18, -4.9, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(538, 214, 215, 26, '1smz', 'Transportan', 'NMR', 'out', 9.1, 0.8, 87, 7, -8.9, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(539, 215, 14, 23, '1p9f', 'Neurokinin B', 'NMR', 'out', 5.8, 1.2, 89, 18, -6.8, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(540, 216, 14, 23, '1wso', 'Orexin-A', 'NMR', 'out', 6.4, 1.7, 72, 14, -5.5, '', 1, 0, '', 'Membrane-binding site participates in protein-protein interaction', '2006-03-17'),
(541, 217, 184, 23, '1g92', 'Poneratoxin', 'NMR', 'out', 22.8, 8.5, 29, 7, -12.9, '', 1, 0, 'When expressed in insect cells, poneratoxin was observed attached to cell membranes (Szolajska et al. 2004).', 'Blocks nicotinc synaptic transmission in insect CNS and affects voltage-dependent sodium channels.', '2006-03-17'),
(542, 218, 14, 23, '1edn', 'Endothelin-1', '2.1', 'out', 4.3, 1.2, 71, 25, -5.4, '', 1, 0, '', '', '2006-03-17'),
(543, 96, 142, 23, '1ih9', 'Zervamicin IIb', 'NMR', 'out', 11.5, 2.0, 74, 10, -12.3, '', 1, 0, 'Orientation and membrane penetration depth of the peptide are consistent with solid-state NMR and fluorescence quenching studies (Bechinger et al. 2001, Kropacheva et al. 2005). 3D structure of the peptide was determined in DPC micelles (Shenkarev et al. 2002). The structure does not change in methanol (Shenkarev et al. 2004). Transfer energy of the peptide is strongly overestimated (experimental binding affinity is -7.8 kcal/mol, Kropacheva et al. 2005), because part of this energy must be spent to fold an alpha-helix from the coil in aqueous solution, prior to insertion of the helix into the membrane.', 'There are small energetic differences between the surface and transmembrane arrangements of the peptide. The shown arrangement has the lowest transfer energy.', '2006-03-17'),
(544, 96, 68, 23, '1m24', 'Trichotoxin a50e', '0.9', 'out', 10.4, 1.8, 75, 32, -14.3, '', 1, 0, '', 'There are small energetic differences between the surface and transmembrane arrangements of the peptide. The shown arrangement has the lowest transfer energy.', '2006-03-17'),
(545, 96, 71, 23, '1ob4', 'Cephaibol A', '0.9', 'out', 14.1, 2.5, 58, 18, -14.7, '', 1, 0, '', 'There are small energetic differences between the surface and transmembrane arrangements of the peptide. The shown arrangement has the lowest transfer energy.', '2006-03-17'),
(546, 96, 71, 23, '1ob6', 'Cephaibol B', '0.8', 'out', 15.0, 5.0, 42, 17, -15.3, '', 1, 0, '', 'There are small energetic differences between the surface and transmembrane arrangements of the peptide.  The shown arrangement has the lowest transfer energy. The dimer (from the crystal structure) is probably unstable.', '2006-03-17'),
(547, 96, 71, 23, '1ob7', 'Cephaibol C', '0.8', 'out', 15.0, 2.1, 55, 21, -15.0, '', 1, 0, '', 'There are small energetic differences between the surface and transmembrane arrangements of the peptide. The shown arrangement has the lowest transfer energy.', '2006-03-17'),
(548, 96, 141, 23, '1joh', 'Antiamoebin I', '1.4', 'out', 8.1, 0.8, 82, 5, -11.7, '', 1, 0, 'Orientation and membrane penetration depth are consistent with fluorescence quenching studies (Kropacheva et al. 2005).', 'There are small energetic differences between the surface and transmembrane arrangements of the peptide. The shown arrangement has the lowest transfer energy.', '2006-03-17'),
(549, 219, 124, 23, '1pen', 'alpha-conotoxin PNI1', '1.1', 'out', 5.2, 1.7, 27, 19, -3.8, '', 1, 0, 'Detected membrane-interaction site is also involved in protein-protein binding: see complex with acetylcholine receptor, 2br8 (A10L substitution in conotoxin).', 'Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. ', '2006-03-17'),
(550, 219, 124, 23, '1akg', 'alpha-conotoxin PNIB', '1.1', 'out', 4.2, 1.4, 42, 19, -5.9, '', 1, 0, 'Detected membrane-binding site interacts with acetylcholine receptor. See structures of the complexes (2br8 and 2c9t).', 'Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. ', '2006-03-17'),
(551, 219, 122, 23, '1mii', 'alpha-conotoxin MII', 'NMR', 'out', 2.7, 1.8, 45, 19, -4.2, '', 1, 0, 'Detected membrane-binding site interacts with acetylcholine receptor. See structures of the complexes (2br8 and 2c9t).', 'Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. In contrast to other alpha-conotoxins, this peptide has no detectable activity at the muscle subtype of receptor, but instead, it potently targets neuronal nAChR. ', '2006-03-17'),
(552, 219, 120, 23, '1dg2', 'alpha-conotoxin auIB', 'NMR', 'out', 5.1, 1.7, 89, 16, -4.9, '', 1, 0, 'Detected membrane-interaction site is also involved in protein-protein binding.  See complexes of other conotoxins with acetylcholine receptor (2br8 and 2c9t).', 'Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. ', '2006-03-17'),
(553, 220, 99, 15, '1brv', 'Major surface glycoprotein G  fragment', 'NMR', 'out', 2.6, 1.6, 40, 19, -4.0, '', 1, 0, '', 'This is fragment 158-189 of major surface glycoprotein G of bovine respiratory syncytial virus (1-257). The protein has a potential TMH 38-66. Expressed on the surface of the infected cells and incorporated in the membrane of the virions. May carry a lot of separate O-linked carbohydrate chains distributed among serine and threonine residues.', '2006-03-17'),
(554, 221, 14, 4, '1xq8', 'Alpha-synuclein', 'NMR', 'in', 8.7, 1.1, 87, 4, -15.7, '', 1, 0, 'This model does not correspond the real membrane-bound structure because the exact mutual arrangement and geometries of the helices were not defined by NMR. According to spin-labeling data, residues T59, V63, G67, V70, V74, V77, T81, A85 and A89 are buried in the hydrophobic interior of the membrane, while residues E61, N65, G68, T72, A76, Q79, and E83 are exposed to water in the membrane-bound state (Jao et al. 2004).', 'The protein is involved in the regulation of dopamine release and transport. Normally, this is a soluble protein, localized primarily at the presynaptic region of axons. However it can also form filamentous aggregates that are that are involved in several neurodegenerative diseases. This structure is probably a misfolded state, which is formed in the presence of detergents or in lipid bilayers. ', '2006-03-17'),
(555, 222, 193, 23, '1z64', 'Pleurocidin', 'NMR', 'out', 5.4, 1.3, 87, 18, -12.8, '', 1, 0, 'Calculated position is in agreement with burial of W2 in the membrane core (flurescence data) and with the overall orientation and membrane penetration depth of the peptide determined by solid-state NMR (Mason et al. 2006).  3D structure was determined in DPC micelles. Each micelle contains at least two pleurocidin molecules. The peptide forms ion channels in lipid bilayers.', 'Antimicrobial peptide with potent activity against Gram-positive and Gram-negative bacteria. Inhibits nucleic acid and protein synthesis.', '2006-03-17'),
(556, 223, 6, 23, '1lfc', 'Lactoferricin B', 'NMR', 'out', 4.6, 0.5, 90, 6, -5.3, '', 1, 0, 'The calculated orientation is in agreement with fluorescence of two Trp residues (Schibli et al. 2002, Nguyen et al. 2005).', 'This is an antimicrobial peptide released by pepsin cleavage of lactoferrin, an 80 kDa iron-binding glycoprotein with many immunologically important functions. The NMR structure of LfcinB reveals a somewhat distorted antiparallel beta-sheet. This contrasts with the X-ray structure of bovine lactoferrin, in which residues 1-13 (of LfcinB) form an alpha-helix (Hwang et al. 1998). Human lactoferricin (1z6v, 1z6w) also forms an alpha-helix. A six-residue segment of bovine lactoferricin was studied in SDS micelles (1y58, 1y5c).', '2006-03-17'),
(557, 224, 14, 23, '1m4e', 'Hepcidin', 'NMR', 'out', 2.4, 1.5, 89, 19, -4.2, '', 1, 0, '', 'Hepcidin is a antibacterial and antifungal protein expressed in the liver and is also a signaling molecule in iron metabolism.', '2006-03-17'),
(558, 225, 154, 23, '1o8y', 'Cyclic trypsin inhibitor STFI-1', 'NMR', 'out', 3.4, 1.3, 83, 18, -6.0, '', 1, 0, '', 'This trypsin inhibitor (see structure of the complex, 1sfi) was identified as potentially interacting with lipid bilayers. ', '2006-03-17'),
(559, 226, 9, 23, '1s7p', 'Microcin J25', 'NMR', 'out', 4.7, 1.2, 83, 18, -5.7, '', 1, 0, 'This is a thermolysin-digested version of the peptide.  Due to poor solubility in water, the structure was determined in methanol. See also comments for 1q71. ', 'The peptide works as an antibiotic through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption.', '2006-03-17'),
(560, 226, 9, 23, '1q71', 'Microcin J25', 'NMR', 'out', 3.3, 3.2, 75, 17, -5.2, '', 1, 0, 'Due to poor solubility in water, the structure was determined in methanol. The peptide has two alternative orientations with nearly identical transfer energies: a strongly tilted and a parallel to the membrane surface. The tilted arrangement is in a better agreement with decreased fluorescence of tyrosines (Rintoul et al. 2000). There are two alternative configurations of the peptide when it interacts with uncharged phospholipid monolayers (Bellomio et al. 2005). ', 'Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. ', '2006-03-17'),
(561, 227, 90, 23, '1pxq', 'Subtilosin A', 'NMR', 'out', 7.6, 0.8, 86, 3, -9.3, '', 1, 0, 'Results are consistent with the partially buried location of subtilosin A in lipid bilayers parallel to the membrane surface, and Trp34 facing towards the center of the lipid bilayer (Thennarasu et al. 2005).', 'This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids.', '2006-03-17'),
(562, 228, 194, 23, '1b5n', 'Plasmatocyte-spreading peptide PSP1', 'NMR', 'out', 3.1, 1.2, 87, 16, -3.7, '', 1, 0, 'No experimental data about interactions with lipid bilayers. ', 'Mediates the spreading of plasmatocytes to foreign surfaces.', '2006-03-17'),
(563, 228, 93, 23, '1irr', 'Paralytic peptide', 'NMR', 'out', 2.2, 1.9, 74, 19, -3.3, '', 1, 0, 'No experimental data about interactions with lipid bilayers. ', '', '2006-03-17'),
(564, 229, 212, 23, '1rpb', 'Tricyclic peptide RP71935', 'NMR', 'out', 4.2, 1.3, 85, 15, -8.3, '', 1, 0, 'No experimental data about interactions with lipid bilayers.', 'Active against HIV-1 virus (replication inhibitor).', '2006-03-17'),
(565, 230, 215, 26, '1soc', 'Octreotide', 'NMR', 'out', 8.9, 1.8, 77, 21, -7.7, '', 1, 0, 'Maximal membrane binding affinity is -5.4 kcal/mol (Beschiaschvili and Seelig 1992).', 'Membrane-binding site participates in protein-protein interaction.', '2006-03-17'),
(1175, 23, 55, 4, '1a11', 'Acetylcholine receptor subunit delta, TMH 2', 'NMR', 'A in', 24.4, 5.6, 17, 10, -14.2, '', 1, 1, '', '', '0000-00-00'),
(1176, 13, 9, 2, '1b9u', 'ATP synthase subunit b', 'NMR', 'A out', 29.8, 4.0, 41, 2, -23.1, '', 1, 1, '', '2khk and 1l2p are structures of water-soluble cytoplasmic domain', '0000-00-00'),
(567, 232, 3, 23, '1tk2', 'Gramicidin S', '1.5', 'out', 8.5, 1.7, 86, 21, -8.6, '', 1, 0, 'Maximal membrane binding affinity is -12.1 kcal/mol (Abraham et al. 2005).', 'Gramicidin S is taken from the complex with proteinase savinase.', '2006-03-17'),
(568, 233, 73, 23, '1aj1', 'Actagardine, structure in acetonitrile solution', 'NMR', 'out', 3.0, 1.1, 90, 11, -5.7, '', 1, 0, '', 'Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The 14-19 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor.', '2006-03-17'),
(569, 234, 88, 23, '1qow', 'Mersacidin, crystal structure', '1.0', 'out', 3.2, 2.7, 72, 31, -5.5, '', 3, 0, 'Peptide forms hexamer in the crystal (Schneider et al. 2000). However, it can be inserted in the lipid bilayer only as trimer or monomer . ', 'Kills a number of Gram-positive bacteria. Acts at the level of cell wall biosynthesis by interfering with bacterial peptidoglycan biosynthesis. Specifically inhibits the conversion of the lipid II intermediate into polymeric nascent glycan strands by transglycosylation. \r\nMaturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The carboxy-terminal beta-methyllanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor. ', '2006-03-17'),
(570, 234, 88, 23, '1mqx', 'Mersacidin, structure in methanol solution', 'NMR', 'out', 1.9, 1.3, 87, 15, -2.9, '', 1, 0, '', '', '2006-03-17'),
(571, 234, 88, 23, '1mqy', 'Mersacidin, structure in DPC micelles', 'NMR', 'out', 5.3, 0.9, 90, 12, -6.1, '', 1, 0, '', '', '2006-03-17'),
(572, 234, 88, 23, '1mqz', 'Mersacidin, structure of lipid II bound peptide in DPC micelles', 'NMR', 'out', 4.2, 2.8, 83, 15, -4.2, '', 1, 0, '', '', '2006-03-17'),
(573, 235, 164, 23, '1wco', 'Nisin-Lipid II complex in DMSO solution', 'NMR', 'out', 8.1, 1.0, 90, 5, -8.0, '', 1, 0, 'Calculated position seems to be consistent with sets of buried residues of nisin in lipid bilayers and micelles (van der Hoven et al. 1996, Bonev et al. 2000, Hsu et al. 2002). However, the comparison is difficult because the peptide is highly flexible, and its conformations in DMSO (1wco) and lipid bilayer may differ (Hsu et al. 2004). Maximal membrane binding affinity is -5.5 kcal/mol, based on the apparent binding constant at low concentration of the peptide (Breukink et al. 2000).', '', '2006-03-17'),
(574, 236, 9, 23, '1etn', 'Heat-stable enterotoxin ST-IA/ST-P', '0.8', 'out', 3.0, 3.7, 33, 39, -2.1, '', 1, 0, '', 'Enterotoxin binds to a membrane-associated guanylyl cyclase C which is located on intestinal epithelial cell membranes. Prokaryotic heat-stable enterotoxins are responsible for acute diarrhea.', '2006-03-17'),
(575, 237, 210, 23, '1w3m', 'Tsushimycin', '1.0', 'out', 9.5, 2.1, 54, 24, -8.6, '', 1, 0, '', 'The dimers possess a large hydrophobic surface capable of interacting with the bacterial cell membrane.', '2006-03-17'),
(576, 237, 211, 23, '1t5m', 'Daptomycin, Ca-free', 'NMR', 'out', 2.3, 1.3, 33, 6, -7.9, '', 1, 0, 'Kyn14 residue is situated at the lipid-water interface and penetrates deeper into the membrane in the Ca-bound state (Lakey and Ptak 1988). ', 'Daptomycin is a cyclic anionic lipopeptide antibiotic recently approved for the treatment of complicated skin infections (Cubicin). Its function is dependent on calcium (as Ca2+). The NMR structure of daptomycin indicated that Ca2+ induced a conformational change in daptomycin that increased its amphipathicity (Jung et al. 2004). ', '2006-03-17'),
(577, 63, 53, 4, '2b3r', 'Phosphatidylinositide 3-kinase C2 alpha', '2.3', 'in', 1.4, 1.5, 88, 16, -4.4, '', 2, 0, '', 'Tilt angle was calculated for one subunit, not for the dimer.', '2006-03-17'),
(578, 111, 119, 23, '1kho', 'Alpha-toxin, different sequence (PHLC2_CLOPE in Uniprot)', '2.4', 'out', 3.8, 1.0, 87, 4, -8.2, '', 1, 0, '', '', '2006-03-17'),
(579, 111, 119, 23, '1gyg', 'Alpha-toxin (PHLC1_CLOPE), closed state (inactive)', '1.9', 'out', 6.1, 2.0, 75, 6, -5.9, '', 1, 0, 'Results are consistent with the important role of Y331 and F334 for asociation with lipid bilayers (Jepson et al. 2001). ', '', '2006-03-17'),
(580, 54, 14, 6, '1w0f', 'Cytochrome P450 3A4, a different conformation', '2.6', 'in', 5.7, 0.8, 70, 3, -16.5, '', 1, 0, 'This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', '', '2006-03-17'),
(581, 54, 25, 6, '1po5', 'Cytochrome P450 2B4, open state 2', '1.6', 'in', 3.5, 1.4, 79, 9, -7.2, '', 1, 0, 'This cytochrome presumably forms TMH 1-21, consistent with calculated orientation.', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin.', '2006-03-17'),
(582, 173, 70, 23, '1gym', 'Phosphatidylinositol-specific phospholipase C, ligand-bound', '2.2', 'out', 4.9, 1.0, 67, 11, -7.2, '', 1, 0, '', '', '2006-03-17'),
(583, 173, 168, 23, '1aod', 'Phosphatidylinositol-specific phospholipase C, ligand-bound', '2.2', 'out', 7.4, 1.0, 79, 10, -9.2, '', 1, 0, '', '', '2006-03-17'),
(1083, 113, 226, 23, '1y75', 'Snake phospholipase A2 isoform 5, group I', '2.30', 'out', 4.4, 0.7, 81, 10, -5.7, '', 1, 0, '', 'One of two chains in a heterodimer.', '0000-00-00'),
(1084, 113, 320, 23, '1oqs', 'Snake phospholipase A2 RV-7, group II ', '1.90', 'out', 2.7, 1.1, 87, 8, -7.9, '', 1, 0, '', 'Non-active inhibiting subunit in heterodimer.', '0000-00-00'),
(585, 113, 226, 23, '1s6b', 'Snake phospholipase A2, group I', '1.6', 'out', 3.0, 1.1, 81, 10, -7.5, '', 1, 0, '', '', '2006-03-17'),
(586, 113, 181, 23, '1gp7', 'Snake phospholipase A2, group I, acidic 1', '2.6', 'out', 4.6, 1.0, 84, 12, -5.8, '', 1, 0, '', '', '2006-03-17'),
(587, 189, 160, 23, '1tib', 'Triacylglycerol lipase, closed (inactive) state', '1.8', 'out', 2.6, 1.5, 38, 10, -5.2, '', 1, 0, '', 'See comments for 1ein. This is a slightly different conformation of closed state.', '2006-03-17'),
(588, 189, 160, 23, '1dt5', 'Triacylglycerol lipase, closed (inactive) state', '2.4', 'out', 5.1, 0.9, 79, 13, -5.9, '', 1, 0, 'See comments for 1ein.', '', '2006-03-17'),
(589, 56, 6, 4, '1ann', 'Annexin IV, monomeric state', '2.3', 'in', 2.2, 1.0, 77, 3, -6.0, '', 1, 0, '', 'This protein undergoes major conformational changes upon association with membranes.', '2006-03-17'),
(590, 184, 6, 23, '1akn', 'Bile-salt activated lipase, different conformations of loops', '2.8', 'out', 3.8, 1.5, 77, 15, -6.7, '', 1, 0, '', 'Conformations of membrane-interacting loops in 1aql and 1akn are different.', '2006-03-17'),
(591, 189, 110, 23, '1trh', 'Lipase 1, closed (inactive) state', '2.1', 'out', 4.9, 1.3, 85, 7, -7.4, '', 1, 0, '', 'Two alternative orientations.', '2006-03-17'),
(592, 191, 14, 23, '1n8s', 'Pancreatic lipase, complex with colipase from Pig', '3.0', 'out', 7.6, 0.6, 45, 4, -10.8, '', 2, 0, '', 'Loosely packed (probably non-native) association mode of the proteins.', '2006-03-17'),
(593, 191, 14, 23, '1lpa', 'Pancreatic lipase, complex with colipase from Pig', '3.0', 'out', 11.3, 0.1, 82, 1, -24.5, '', 2, 0, '', ' ', '2006-03-17'),
(594, 178, 14, 9, '1oiz', 'Alpha-tocopherol transfer protein, open state with detergent', '1.8', 'in', 8.1, 1.0, 64, 10, -17.6, '', 1, 0, 'Consistent with membrane-association mode discussed by Meier et al. (2003).', 'Open state was formed in the presence of detergent: molecules of TRITON X-100 penetrate between "entrance" alpha-helices. This protein binds alpha-tocopherol and enhances its transfer between separate membranes.', '2006-03-17'),
(595, 193, 9, 2, '1nlm', 'Peptidoglycan biosynthesis glycosyltransferase MurG', '2.5', 'in', 4.8, 1.1, 50, 7, -7.5, '', 1, 0, '', 'This is a peripheral membrane protein involved in cell wall formation. Structures 1f0k and 1nlm have different conformations of loop 63-79 that interacts with membrane (probably due to binding of glycerol in 1nlm).\r\n\r\n\r\n', '2006-03-17'),
(596, 81, 9, 2, '2cfq', 'Lactose permease, structure at neutral pH', '2.95', 'A in', 31.9, 1.1, 5, 1, -87.9, '', 1, 12, 'Results are consistent with chemical modification and spin-labeling studies of lactose permease (Voss et al. 1996, Frillingos et al. 1998, Zhao et al. 1999, Kwaw et al. 2001, Guan et al. 2002, Ermolova et al. 2003, Venkatesan et al. 2000a,b,c, Zhang et al. 2003). Average tilt angle of TM helices (20 degrees) is smaller than estimated by ATR FTIR (Le Coutre et al. 1997). Hydrophobic thickness is ~2 A smaller than was calculated for the lower resolution structure (1pv6).', '', '2006-03-17'),
(597, 238, 36, 4, '1zi7', 'Oxysterol-binding protein homolog 4 (KES1), N-terminal helix removed', '2.5', 'in', 2.5, 0.5, 75, 8, -6.9, '', 1, 0, 'The results are consitent with membrane-binding orientation proposed by Im et al. (2005).', 'This is an engineered (lid-truncated) protein.', '2006-03-17'),
(673, 27, 39, 8, '2hyd', 'Multidrug ABC transporter SAV1866, closed state', '3.0', 'A in', 31.8, 1.7, 3, 3, -110.5, '', 2, 12, '', 'TM portions of this transporter and lipid flippases have completely different 3D stuctures, although the proteins are homologous. EM-based model of homologous transporter from E.coli (2i68) also seems to be different. ', '0000-00-00'),
(683, 153, 239, 15, '1rer', 'Fusion glycoprotein E1', '3.2', 'out', 2.6, 2.0, 38, 5, -6.5, '', 3, 0, 'Structures of mononers in the trimer are slightly different. The symmetry axis of the trimer is strongly tilted.  It is also tilted according to EM data. A really symmetric structure is a pentamer of the trimers (Gibbons et al. 2004). ', 'E1 is a class II viral fusion protein.  This trimeric (low-pH-iduced) form is fusion active, and promotes release of viral nucleocapsid in cytoplasm after cell and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. N-terminal domain of this protein: 1dyl(NMR), 1vcp, 1vcq.', '0000-00-00'),
(598, 174, 53, 6, '1y5m', 'Corticosteroid 11-beta-dehydrogenase, isozyme 1', '2.3', 'out', 4.6, 0.4, 89, 2, -19.3, '', 2, 0, 'N-terminal segment 7-23 from each subunit was shown to form a TM helix (single-pass  type II membrane protein). The dimer of water-soluble domains presumably associates with membranes through the C-terminal helices (Zhang et al. 2005), as calculated.', '', '0000-00-00'),
(1250, 204, 14, 4, '2pso', 'StAR-related lipid transfer protein 13', '2.8', 'in', 3.1, 4.0, 77, 27, -4.6, '', 1, 0, '', '', '0000-00-00'),
(600, 66, 11, 23, '1iiu', 'Retinol binding protein, plasma isoform', '2.5', 'out', 1.9, 1.8, 35, 17, -4.4, '', 1, 0, '', '', '2006-04-13'),
(601, 117, 14, 4, '1swx', 'Glycolipid transfer protein, apo-form', '1.6', 'in', 4.6, 1.0, 87, 8, -7.1, '', 1, 0, '', 'Accelerates the intermembrane transfer of various glycolipids. The formation of the intramolecular disulfide bond enhances the transfer activity of GLTP.', '2006-04-13'),
(602, 117, 14, 4, '1sx6', 'Glycolipid transfer protein, bound form', '1.9', 'in', 4.3, 1.1, 85, 5, -10.1, '', 1, 0, '', 'Accelerates the intermembrane transfer of various glycolipids. The formation of the intramolecular disulfide bond enhances the transfer activity of GLTP.', '2006-04-13'),
(603, 241, 90, 8, '1tf5', 'Translocation ATPase SecA', '2.1', 'in', 2.5, 1.1, 64, 5, -7.0, '', 1, 0, 'Interacts with lipid bilayers in monomeric state (1tf2, 1tf5) and undergoes significant conformational changes (Osborne et al. 2004). The structure of dimer (1m74, 1m6n) is different. More data on iteractions of SecA from E.coli with membranes and SecY:  van Dalen and de Kruijff (2004), Breukink et al. (1992), Dapic and Oliver (2000).', 'Part of the prokaryotic protein translocation apparatus which comprise secA, secB, secD, secE, secF, secG and secY. SecA has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane.', '2006-04-13'),
(605, 189, 230, 23, '1thg', 'Lipase 2', '1.8', 'out', 6.4, 1.7, 23, 14, -4.7, '', 1, 0, '', '', '2006-04-13'),
(606, 399, 14, 4, '1hh4', 'Rho GDP-dissociation inhibitor 1, complex with G-protein RAC2', '2.7', 'in', 4.0, 0.6, 88, 6, -7.2, '', 2, 0, 'The inhibitor is bound to RAC2 protein (Ras-related C3 botulinum toxin substrate 2). RAC2 has S-geranylgeranyl cysteine 189. The  geranylgeranyl residue can be  buried in the membrane if the C-terminus of RAC2 is extended or unfolded (the C-terminal residues are missing in the crystal structure). The interaction with membrane is weak, since this is the inactive (GDP-bound) state. RAC2 is membrane-associated when activated.', 'Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. ', '2006-04-13'),
(607, 399, 14, 4, '1qvy', 'Rho GDP-dissociation inhibitor 1', '1.6', 'in', 2.8, 1.7, 53, 19, -5.1, '', 1, 0, '', 'Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.', '2006-04-13'),
(608, 151, 14, 4, '1fl7', 'Follicle-stimulating hormone, complex of alpha and beta chains', '3.0', 'out', 2.0, 1.6, 74, 9, -5.3, '', 4, 0, '', 'The initial membrane binding mode of the tetramer (prior to its dissociation) is asymmetric and similar to that of the hormone-receptor complex (1xwd).', '2006-04-13'),
(609, 174, 14, 6, '1xu7', 'Corticosteroid 11-beta-dehydrogenase, isozyme 1', '1.8', 'out', 7.9, 0.2, 89, 1, -20.2, '', 2, 0, 'N-terminal segment 7-23 from each subunit was shown to form a TM helix (single-pass type II membrane protein), consistent with calculated orientation of the dimer.', 'Membrane binding mode is slightly asymmetric, because conformations of segments 228-233 in the monomeric units are different. ', '2006-04-13'),
(610, 89, 9, 3, '1kmp', 'Outer membrane transporter FecA, different conformation', '2.5', 'A out', 24.9, 0.9, 4, 0, -74.0, '', 1, 22, '', '', '2006-04-13'),
(611, 39, 24, 3, '1uyo', 'Autotransporter NalP, different conformation', '3.2', 'X out', 23.6, 1.4, 8, 0, -42.7, '', 1, 12, '', '', '2006-04-13'),
(647, 250, 9, 2, '1t7d', 'Type 1 signal peptidase,  complex with lipopeptide inhibitor', '2.4', 'out', 3.9, 1.0, 65, 11, -7.6, '', 1, 0, 'This is a two-pass TM protein (UniProt). See comments for 1kn9.', 'Consistent with membrane binding mode proposed by Paetzel et al. (2004).', '0000-00-00'),
(612, 237, 211, 23, '1xt7', 'Daptomycin, Ca-free', 'NMR', 'out', 9.3, 3.9, 10, 45, -6.4, '', 1, 0, 'Kyn14 residue is situated at the lipid-water interface and penetrates deeper into the membrane in the Ca-bound state (Lakey and Ptak 1988). ', 'Daptomycin is a cyclic anionic lipopeptide antibiotic recently approved for the treatment of complicated skin infections (Cubicin). Its function is dependent on calcium (as Ca2+). The NMR structure of daptomycin indicated that Ca2+ induced a conformational change in daptomycin that increased its amphipathicity (Jung et al. 2004).', '2006-04-13'),
(613, 237, 211, 23, '1t5n', 'Daptomycin, Ca-bound', 'NMR', 'out', 8.6, 2.0, 21, 24, -9.0, '', 1, 0, 'Residue Kyn14 is situated at the lipid-water interface and penetrates deeper into the membrane in the Ca-bound state (Lakey and Ptak 1988). ', 'Daptomycin is a cyclic anionic lipopeptide antibiotic recently approved for the treatment of complicated skin infections (Cubicin). Its function is dependent on calcium (as Ca2+). The NMR structure of daptomycin indicated that Ca2+ induced a conformational change in daptomycin that increased its amphipathicity (Jung et al. 2004).', '2006-04-13'),
(624, 242, 14, 4, '1zvr', 'Myotubularin-related protein 2', '2.0', 'in', 3.1, 0.4, 89, 8, -5.0, '', 1, 0, 'Calculated orientation is in agreement with membrane binding mode through alpha-helix 6 proposed by Begley et al. (2006). ', '', '0000-00-00'),
(614, 74, 14, 12, '1o7k', 'PX domain of NADH oxidase (p47phox),  ligand-bound', '2.0', 'in', 15.2, 1.7, 60, 15, -18.4, '', 1, 0, 'This is membrane-association mode with specifically bound phosphoinositol lipid: the interaction occurs through W80, in agreement with experimental studies (Stahelin et al. 2003). Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Lipid-free structure of p47phox had two alterantive membrane-binding modes with nearly identical transfer energies: (1) through I60 and I65 and (2) through hydrophobic beta-turn F18-V19 (ligand-free p47pox associates with membrane through I65 according to Stahelin et al. 2003). The exposed hydrophobic areas are masked in the inactive state of the PX domain (Karathanassis et al. 2002). Transfer energy was calculated with bound lipid.', 'The position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Subcellular localization of PX domains - see Cho and Stahelin (2005). ', '0000-00-00'),
(1279, 31, 25, 6, '3ar8', 'Calcium ATPase, E2-Pi state, different conformation', '2.6', 'A in', 28.6, 1.8, 19, 0, -60.6, '', 1, 10, '', '', '0000-00-00'),
(617, 391, 28, 3, '2erv', 'Lipid A deacylase PagL', '2.0', 'A in', 24.7, 1.8, 20, 2, -41.1, '', 1, 8, '', 'PagP and PagL enzymes have no detectable sequence homology. PagL seems to be weakly homologous to outer membrane protein NspA from OmpA family (1p4t) after structural superposition.', '0000-00-00'),
(615, 74, 14, 12, '1kq6', 'PX domain of NADH oxidase (p47phox),  ligand-free, longer chain', '1.1', 'in', 2.4, 1.6, 88, 12, -4.6, '', 1, 0, 'This orientation is consistent with association of p47phox to the membrane through residue I65, as observed when this domain is not bound to phosphoinositol lipid (Stahelin et al. 2003). Also see comments for 1o7k.', 'PX domain can be "open" or "closed" for strong association with lipid bilayers depending on interactions with other domains (Karathanassis et al. 2002). This structure may represent the "closed" state, since the hydrophobic beta-turn V18-F19 was buried from water by an additional segment of the polypeptide chain which is missing in 1ok7.  Note also different conformations of a loop with exposed W80 residue and different oligomeric states of PX domain in 1ok7 and 1kq6 PDB entries. Both oligomeric states are probably non-native.  Therefore, the membrane-bound orientations are calculated for monomers. Subcellular localization of PX domains - see Cho and Stahelin (2005).', '0000-00-00'),
(616, 197, 212, 8, '1b4v', 'Cholesterol oxidase', '1.5', 'out', 5.4, 0.6, 39, 4, -8.4, '', 1, 0, '', 'Maximal membrane binding affinity: -8.7 kcal/mol (Ahn and Sampson 2004).', '0000-00-00'),
(659, 253, 14, 19, '1zza', 'Stannin', 'NMR', 'A in', 29.8, 2.1, 13, 6, -24.6, '', 1, 1, '', 'Calculated orientation and hydrophobic thickness of this protein are unreliable, because the experimental structure was determined by combining distance constraints obtained for individual alpha-helices in micelles with orientational constraints obtained in the lipid bilayer (Buck-Koehntop et al. 2005). The transmembrane topology is tentative (Davidson et al. 2004).', '0000-00-00'),
(649, 250, 9, 2, '1b12', 'Type 1 signal peptidase, complex with inhibitor', '1.9', 'out', 5.4, 1.8, 88, 7, -5.1, '', 1, 0, 'This is a two-pass TM protein (UniProt). See comments for 1kn9.', 'Consistent with membrane binding mode proposed by Paetzel et al. (1998).', '0000-00-00'),
(618, 183, 14, 25, '1cjy', 'Cytosolic phospholipase A2, group IVA', '2.5', 'in', 5.8, 1.0, 70, 9, -9.9, '', 1, 0, 'Mutations of residues I399, L400 and L552 slightly affect membrane binding (Das and Cho 2002). However, these residues are completely buried in the protein interior.  This is probably an indirect effect (authors suggest conformational changes). Maximal membrane binding afinity: -11 kcal/mol (Stahelin and Cho 2001).', 'Orientation of an isolated C2 domain (1rlw) is nearly the same.  Patatin and catalytic domain of cPLA have clear sequence identity, despite of the numerous structural differences. ', '0000-00-00'),
(648, 250, 9, 2, '1kn9', 'Type 1 signal peptidase, apo-enzyme', '2.4', 'out', 3.4, 1.4, 80, 6, -7.8, '', 1, 0, 'This is a two-pass TM protein (Uniprot). The isolated periplasmic domain des(2-75) is catalytically active (Paetzel et al. 2002) and associates with lipid bilayers (van Klompenburg et al. 1998, van den Brink-van der Laan et al. 2001). It inserts preferentially into bilayers with decreased headgroup lateral pressure (van den Brink-van der Laan et al. 2004). The following residues of the apo-enzyme are buried in the membrane interior: W300, M301, F303, L314, and L316. This is consistent with the important role of W300 for membrane association (Kim et al. 1995) and with location of N-terminal membrane-anchoring domain. Calculated orientation is similar to that proposed by Paetzel et al. (1998).', 'Function - see review by Paetzel et al. (2002).', '0000-00-00'),
(619, 65, 14, 4, '1dbh', 'Son of sevenless homolog 1 (two domains)', '2.3', 'in', 2.7, 2.8, 28, 19, -4.2, '', 1, 0, '', 'Promotes the exchange of Ras-bound GDP by GTP.', '0000-00-00'),
(620, 78, 53, 4, '1kbf', 'Kinase supressor of Ras, Ksr', 'NMR', 'in', 1.8, 1.0, 63, 11, -5.4, '', 1, 0, '', '', '0000-00-00'),
(621, 78, 14, 4, '1faq', 'RAF-1 proto-oncogene serine/threonine-protein kinase', 'NMR', 'in', 4.8, 1.1, 30, 14, -7.3, '', 1, 0, 'Membrane-binding affinity: -5.5 kcal/mol (from Kd in Table 1, Johnson and Cornell, 1999).', 'Involved in the transduction of mitogenic signals from the cell membrane to the nucleus.  This protein also includes Ras-binding domain (RBD, residues 51-132) that interacts with G-protein Rap1A (PDB entries 1c1y, 1gua, and 1rfa). ', '0000-00-00'),
(622, 78, 196, 4, '1tbn', 'Protein kinase C-gamma', 'NMR', 'in', 4.8, 1.6, 42, 19, -3.7, '', 1, 0, 'Calculated orientation is in agreement with broadening of amide signals in the presence of lipid micelles (residues 106-111, 113-116, 120-127, and 130) (Xu et al. 1997). However, many of the affected residues are situated in the membrane interface (residues buried in the model: 111, 112, 114, and 118-125). The structure was determined in the presence of 25% CD3CH/75% H2O, due to solubility problems (Xu et al. 1997). ', '', '0000-00-00'),
(623, 78, 14, 4, '1r79', 'Diacylglycerol kinase delta', 'NMR', 'in', 3.3, 1.6, 34, 19, -4.9, '', 1, 0, '', '', '0000-00-00'),
(625, 74, 36, 13, '1kmd', 'PX domain of vacuolar morphogenesis protein VAM7', 'NMR', 'in', 3.4, 1.2, 76, 8, -7.8, '', 1, 0, '', 'Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure.', '0000-00-00'),
(626, 74, 36, 12, '1ocu', 'PX domain of sorting nexin GRD19, ligand-bound', '2.3', 'in', 15.3, 0.8, 88, 6, -34.9, '', 2, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Spatial positions of the protein calculated with and without the bound lipid are almost identical. Transfer energy was calculated without contribution from the bound lipid.', 'Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Subcellular localization of PX domains - see Cho and Stahelin (2005).', '0000-00-00'),
(627, 74, 36, 12, '1ocs', 'PX domain of sorting nexin GRD19, ligand-free', '2.0', 'in', 2.5, 1.1, 88, 11, -5.4, '', 1, 0, '', 'Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Subcellular localization of PX domains - see Cho and Stahelin (2005).', '0000-00-00'),
(628, 149, 14, 24, '1pub', 'Ganglioside GM2 activator, different conformation', '2.5', 'out', 4.9, 0.7, 50, 8, -7.3, '', 1, 0, 'GM2 activator interacts with lipid bilayers (Giehl et al. 1999). Calculated orientation is in agreement with membrane binding mode proposed by Wright et al. (2003).', 'Extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.', '0000-00-00'),
(629, 149, 14, 24, '2ag4', 'Ganglioside GM2 activator, apo-protein', '1.8', 'out', 3.1, 1.3, 58, 12, -5.4, '', 1, 0, 'GM2 activator interacts with lipid bilayers (Giehl et al. 1999). Calculated orientation is in agreement with membrane binding mode proposed by Wright et al. (2003).', 'Extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.', '0000-00-00'),
(630, 204, 14, 12, '1em2', 'Lipid transport protein Mln64 (StARD3)', '2.2', 'in', 2.0, 1.1, 82, 12, -5.0, '', 1, 0, 'This protein contains a water-soluble domain (START) and a TM domain (MENTAL, 46-217; 4 predicted TMH).', 'Binds and transports cholesterol. Promotes steroidogenesis in placenta and brain.', '0000-00-00'),
(631, 100, 14, 4, '1hci', 'Alpha-actinin-2', '2.8', 'in', 0.4, 0.7, 90, 12, -5.1, '', 2, 0, '', 'F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ', '0000-00-00'),
(1373, 30, 53, 5, '2lck', 'Mitochondrial uncoupling protein 2', 'NMR', 'out', 29.8, 1.1, 9, 2, -33.2, '', 1, 6, '', '', '0000-00-00'),
(1374, 405, 9, 2, '3rko', 'Respiratory complex I', '3.0', 'L out', 29.6, 0.0, 9, 0, -236.7, '', 6, 58, '', '', '0000-00-00'),
(1327, 66, 53, 6, '2ktd', 'Prostaglandin-H2 D-isomerase', 'NMR', 'in', 0.0, 1.4, 73, 14, -2.2, '', 1, 0, '', '', '0000-00-00'),
(1328, 143, 14, 4, '2wut', 'Myelin P2 protein', '1.85', 'in', 4.1, 0.5, 47, 7, -3.4, '', 1, 0, '', '', '0000-00-00'),
(1329, 66, 6, 23, '3nq9', 'Beta-lactoglobulin', '1.90', 'out', 0.5, 0.9, 89, 4, -2.7, '', 1, 0, '', '', '0000-00-00'),
(1330, 66, 14, 23, '2hzq', 'Apolipoprotein D', '1.80', 'out', 4.5, 0.9, 69, 5, -7.8, '', 1, 0, '', '', '0000-00-00'),
(634, 65, 14, 4, '1w1g', 'PH domain of 3-phosphoinositide-dependent protein kinase 1', '1.4', 'in', 3.8, 1.8, 20, 18, -4.8, '', 1, 0, '', '', '0000-00-00'),
(635, 65, 53, 4, '1v5p', 'PH domain of TAPP2', 'NMR', 'in', 1.4, 1.3, 61, 5, -3.7, '', 1, 0, '', '', '0000-00-00'),
(636, 243, 53, 4, '1nu2', 'Disabled homolog 1', '1.9', 'in', 14.8, 1.1, 46, 12, -17.6, '', 1, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Transfer energy was calculated without contribution from the bound lipid(orientation of the protein without bound lipid is different). Membrane penetration depth of the protein is poorly defined because  it strongly depends on the bound lipid conformation (the protein can move away of the hydrophobic boundary).', 'Adapter molecule functioning in neural development. Associates with the SH2 domains of Src, Fyn and Abl. Interacts with SIAH1. ', '0000-00-00'),
(637, 244, 55, 4, '1t27', 'Phosphatidylinositol transfer protein alpha isoform', '2.2', 'in', 2.3, 1.9, 12, 12, -4.1, '', 1, 0, '', 'Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.', '0000-00-00'),
(638, 244, 14, 4, '1uw5', 'Phosphatidylinositol transfer protein alpha isoform', '2.9', 'in', 4.3, 1.5, 18, 16, -5.4, '', 1, 0, '', 'Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.', '0000-00-00'),
(639, 245, 36, 6, '1nrj', 'Signal recognition particle receptor', '1.7', 'out', 3.9, 1.4, 82, 11, -5.5, '', 2, 0, 'Membrane-associated protein (Schwartz and Blobel 2003). It has a TM helix 3-23 in beta subunit, which is compatible with calculated orientation (beta-subunit belongs to G-proteins).', 'Ensures, in conjunction with SRP, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. May be directly involved in mitochondrial protein import. Heterodimer of an alpha and a beta chain.', '0000-00-00'),
(640, 246, 53, 25, '1h3q', 'Trafficking protein particle complex protein 2 (Sedlin)', '2.4', 'out', 3.3, 0.8, 14, 11, -6.3, '', 1, 0, 'The detected potential membrane-association site is probably involved in interaction with another protein. Note that orientation of sedlin is different from orientations of other proteins from this familiy.', 'Part of the multisubunit TRAPP (transport protein particle) complex. Binds to MBP1, prevents MBP1-mediated transcriptional repression and antagonizes MBP1-mediated cell death.', '0000-00-00'),
(641, 247, 6, 4, '1a0r', 'Phosducin/Transducin beta-gamma complex, conformation 1', '2.8', 'in', 2.3, 1.0, 50, 4, -7.4, '', 3, 0, '', 'Phosducin probably facilitates removal of the beta-gamma complex from the membrane, starting from transfer of farnesyl from membrane to the binding cavity in beta-subunit (Gaudet et al. 1999). This is probably an initial membrane-bound state when phosducin is not phosphorylated. This orientation is similar to one proposed by Murray et al. (2001).', '0000-00-00'),
(642, 247, 55, 4, '2trc', 'Phosducin/Transducin beta-gamma complex, conformation 2', '2.4', 'in', 2.2, 1.0, 62, 10, -4.9, '', 3, 0, '', 'Phosducin probably facilitates removal of the beta-gamma complex from the membrane (Gaudet et al. 1999). This is an intermediate state when a large loop of phosducin is partially disordered.', '0000-00-00'),
(643, 247, 55, 4, '1b9x', 'Phosducin/Transducin beta-gamma complex, conformation 3', '3.0', 'in', 1.0, 1.6, 49, 12, -3.9, '', 3, 0, '', 'A model of phosphorylated state of phosducin (Gaudet et al. 1999). The complex is almost detached from the membrane.', '0000-00-00'),
(644, 249, 53, 4, '1i7e', 'Tubby protein, ligand-bound', '1.9', 'in', 3.8, 1.9, 75, 13, -4.7, '', 1, 0, '', 'Some membrane-interacing loops are disordered.', '0000-00-00'),
(645, 249, 53, 4, '1c8z', 'Tubby protein, ligand-free', '1.9', 'in', 2.8, 0.9, 89, 13, -5.8, '', 1, 0, '', 'All membrane-interacting loops are present.', '0000-00-00'),
(646, 248, 55, 4, '1hfa', 'Clathrin assembly lymphoid myeloid leukemia (CALM) protein', '2.0', 'in', 14.2, 2.0, 44, 14, -17.9, '', 1, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Membrane penetration depth of the protein strongly depends on the bound lipid conformation (the protein can move away of the hydrophobic boundary). Transfer energy was calculated without contribution of the bound lipid (orientation of the protein without bound lipid is different). ', 'Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly.', '0000-00-00'),
(650, 54, 14, 6, '2f9q', 'Cytochrome P450 2D6', '3.0', 'in', 7.0, 1.8, 29, 10, -12.0, '', 1, 0, '', 'Responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It is involved in the metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants. Highly polymorphic. Induction by pregnancy. D230 and R231 were replaced by Leu (to be as in wild type protein).  ', '0000-00-00'),
(651, 54, 25, 6, '2bdm', 'Cytochrome P450 2B4, open state 1', '2.3', 'in', 10.6, 1.0, 48, 15, -16.2, '', 1, 0, '', 'This cytochrome forms a nonnative interwinded dimer in crystal. Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin.', '0000-00-00'),
(652, 54, 14, 6, '1r9o', 'Cytochrome P450 2C9, different conformation', '2.0', 'in', 4.0, 1.1, 59, 8, -10.1, '', 1, 0, '', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.', '0000-00-00'),
(653, 54, 25, 6, '1dt6', 'Cytochrome P450 2C5, different conformation', '3.0', 'in', 7.3, 1.0, 13, 7, -8.8, '', 1, 0, '', 'Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This protein differs from other forms of cytochrome P450 in that it catalyzes the 21-hydroxylation of progesterone, resulting in the formation of deoxycorticosterone.', '0000-00-00'),
(654, 178, 36, 9, '1aua', 'Phosphatidylinositol transfer protein sec14p', '2.5', 'in', 8.8, 1.1, 75, 10, -14.3, '', 1, 0, 'Consistent with the generally assumed membrane binding mode of the protein (Phillips et al. 2006).', 'Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro. Forms stable dimer in crystal.', '0000-00-00'),
(655, 77, 14, 12, '1joc', 'Early endosome antigen 1 (EEA1), model of dimer with lipids', '2.2', 'in', 15.0, 0.4, 2, 11, -34.0, '', 2, 0, 'This is calculation with bound lipids. Acyl chains of two lipids were modelled.\r\nCalculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Depending on conformations of bound lipids, the protein can penetrate deeper by ~2 A. Results for the dimer without bound lipids are exactly the same as for lipid-free EEA1 monomer (1hyi). Transfer energy was calculated without contribution from the bound lipid.', '', '0000-00-00'),
(656, 251, 9, 2, '2gfp', 'Multidrug transporter EmrD', '3.5', 'A in', 31.6, 1.5, 9, 0, -58.0, '', 1, 12, '', '', '0000-00-00'),
(657, 65, 14, 4, '1bwn', 'PH domain of tyrosine-protein kinase BTK', '2.1', 'in', 15.3, 0.5, 90, 10, -33.3, '', 2, 0, 'Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid.', 'Other domains of this protein: 1aww and 1k2p. Acyl chains of two lipids were modelled. Transfer energy was calculated without contribution from the bound lipid.', '0000-00-00'),
(756, 35, 215, 26, '2jmm', 'Transmembrane beta-barrel platform protein', 'NMR', 'A in', 23.9, 1.3, 4, 4, -32.3, '', 1, 8, '', '', '0000-00-00'),
(757, 277, 14, 6, '2uuh', 'Leukotriene C4 synthase', '2.15', 'A out', 29.4, 1.1, 0, 0, -55.2, '', 3, 12, '', 'Hydrophobic thickness is relatively uncertain due to significant misplacement of C-terminal helix, probably induced by binding of detergent in the substrate-binding site. This C-terminal TM helix is expected to significantly move along the bilayer normal after dissociation of ligand.  The transmembrane topopogy published in JBC was incorrect (?).  ', '0000-00-00'),
(658, 252, 232, 3, '2gr7', 'Autotransporter Hia', '2.3', 'A out', 22.7, 2.0, 0, 1, -43.5, '', 3, 15, '', '', '0000-00-00'),
(660, 2, 187, 7, '2bhw', 'Light-Harvesting Complex II', '2.5', 'A in', 29.4, 1.0, 0, 0, -123.2, '', 3, 9, '', '', '0000-00-00'),
(750, 276, 59, 1, '2onk', 'Molybdate transporter ModBC, open state', '3.1', 'C in', 32.0, 1.7, 0, 1, -100.7, '', 2, 12, '', '', '0000-00-00'),
(661, 89, 9, 3, '2grx', 'Ferric hydroxamate uptake receptor FhuA, complex with TonB', '3.3', 'A in', 24.6, 1.1, 3, 0, -77.2, '', 1, 22, '', '', '0000-00-00'),
(662, 45, 9, 3, '2gsk', 'Outer membrane cobalamin transporter BtuB, complex with TonB', '2.1', 'A in', 23.4, 0.7, 5, 0, -77.5, '', 1, 22, '', '', '0000-00-00'),
(663, 69, 54, 23, '2cdx', 'Cardiotoxin-A1 (cytotoxin 1)', 'NMR', 'out', 2.6, 1.4, 85, 17, -6.9, '', 1, 0, '', '', '0000-00-00'),
(664, 69, 175, 23, '1rl5', 'Cytotoxin-1', 'NMR', 'out', 5.2, 2.0, 51, 16, -5.7, '', 1, 0, '', '', '0000-00-00'),
(665, 69, 233, 23, '1ctx', 'alpha-Cobratoxin', '2.8', 'out', 2.8, 1.7, 29, 18, -4.6, '', 1, 0, '', '', '0000-00-00'),
(666, 98, 31, 2, '1cxa', 'Cytochrome c2', '2.2', 'out', 2.0, 1.2, 88, 13, -4.3, '', 1, 0, '', 'See this cytochrome in bacterial photosynthetic reaction center - 1l9b.', '0000-00-00'),
(667, 63, 55, 4, '2cjs', 'Protein unc-13 homolog A, C2A domain', '1.8', 'in', 3.5, 2.0, 47, 12, -5.0, '', 1, 0, '', 'The homodimer is strongly asymmetric.  Membrane-binding region of one subunit interacts with another subunit.', '0000-00-00'),
(668, 255, 29, 1, '2deo', 'Membrane protease specific for a stomatin homolog', '3.0', 'in', 3.3, 1.8, 73, 17, -7.0, '', 1, 0, 'This protein probably has an additional C-terminal domain with 4 TM alpha-helices (Yokoyama et al. 2006) - compatible with the calculated orientation.', '', '0000-00-00');
INSERT INTO `protein` (`id`, `family_id`, `species_id`, `membrane_id`, `pdbid`, `name`, `resolution`, `topology`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`, `tau`, `numsubunits`, `numstrands`, `verification`, `comments`, `date_added`) VALUES
(669, 254, 9, 3, '2f1c', 'Outer membrane protein G (OMPG)', '2.3', 'A in', 23.8, 1.4, 1, 4, -56.7, '', 1, 14, '', 'Some loops are disordered (missing) in this structure but present in 2iwv and 2iww. This structure, 2iwv, and 2iww represent different crystal forms of the protein (different space groups).', '0000-00-00'),
(670, 254, 9, 3, '2iwv', 'Outer membrane protein G (OMPG), open state', '2.3', 'A in', 25.3, 1.4, 3, 5, -61.3, '', 1, 14, '', '', '0000-00-00'),
(671, 254, 9, 3, '2iww', 'Outer membrane protein G (OMPG), closed state', '2.7', 'A in', 24.7, 1.4, 6, 4, -63.3, '', 1, 14, '', '', '0000-00-00'),
(674, 43, 9, 3, '2j1n', 'Osmoporin OMPC', '2.0', 'A in', 25.1, 1.2, 0, 2, -126.2, '', 3, 48, '', '', '0000-00-00'),
(675, 25, 9, 2, '2gif', 'Multidrug efflux transporter AcrB', '2.9', 'A in', 29.0, 0.2, 1, 0, -187.5, '', 3, 36, '', 'Residues 499-515 are ordered in 2gif and 2hrt but disordered in all other structures of AcrB.  Three subunits are not identical. Therefore, their tilt angles and some transmembrane segments are slightly different. The substrate is bound to the stronger tilted subunit B.', '0000-00-00'),
(677, 6, 31, 2, '2fyn', 'Cytochrome bc1, bacterial', '3.2', 'A in', 30.1, 0.8, 0, 0, -170.8, '', 6, 20, '', '', '0000-00-00'),
(966, 330, 36, 6, '3a36', 'ATPase Get3, homodimer', '2.80', 'in', 5.6, 3.0, 66, 10, -6.6, '', 2, 0, '', 'Other related ATPases are 2woj, 2woo, 3ibg and 1f48/1ihu/1ii0/1ii9. Their membrane-interacting loops are apparently disordered.', '0000-00-00'),
(689, 259, 6, 4, '1got', 'Transducin', '2.0', 'out', 4.9, 1.2, 61, 8, -7.0, '', 3, 0, '', 'This is a model with reconstructed membrane-anchoring residues. Transfer energy and penetration depth reflect immersion of myristoyl residue.  Alpha-subunit is a species chimera. Other PDB entries of bovine transducin have different subunit compositions. ', '0000-00-00'),
(678, 206, 220, 23, '2plh', 'Alpha-1-purothionin', '2.5', 'out', 2.4, 2.0, 53, 17, -4.6, '', 1, 0, 'This protein associates with lipid vesicles (Caaveiro et al. 1998).', '', '0000-00-00'),
(679, 206, 234, 23, '1okh', 'Viscotoxin A3', '1.7', 'out', 4.6, 1.3, 32, 19, -4.9, '', 1, 0, 'Interacts with lipid bilayers (see the references). It possibly forms ion channels (Giudici et al. 2006). ', '', '0000-00-00'),
(680, 206, 234, 23, '1jmp', 'Viscotoxin B', 'NMR', 'out', 1.2, 1.4, 52, 13, -3.2, '', 1, 0, 'Viscotoxins A2 and B associate with lipid bilayers weaker than viscotoxin A3 (Coulon et al. 2003), in agreement with results of the calculations.', '', '0000-00-00'),
(681, 206, 234, 23, '1jmn', 'Viscotoxin A2', 'NMR', 'out', 2.3, 0.3, 63, 8, -3.3, '', 1, 0, 'Viscotoxins A2 and B associate with lipid bilayers weaker than viscotoxin A3 (Coulon et al. 2003), in agreement with results of the calculations.', '', '0000-00-00'),
(682, 256, 55, 5, '2h4t', 'Carnitine O-palmitoyltransferase 2', '1.9', 'in', 4.0, 1.2, 67, 10, -9.4, '', 1, 0, 'This protein can be classified as integral monotopic (Mattevi 2006).  Calculated orientation  corresponds to membrane-binding mode proposed by Rufer et al. (2006). ', 'Catalytic activity: Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.', '0000-00-00'),
(684, 153, 240, 15, '1urz', 'Envelope glycoprotein', '2.7', 'out', 5.9, 0.9, 1, 8, -10.3, '', 3, 0, '', '', '0000-00-00'),
(685, 257, 241, 23, '2czp', 'Mastoparan', 'NMR', 'out', 5.2, 1.6, 88, 16, -9.8, '', 1, 0, '', '', '0000-00-00'),
(686, 104, 14, 24, '1sn6', 'Saposin C, open structure in micelles', 'NMR', 'out', 4.8, 1.1, 82, 7, -7.1, '', 1, 0, '', 'Structure in solution (1m12) is different. See also closed monomeric (3bqp,3bqq) and open dimeric (2z9a) forms of saposin D. This segment 311-390. Structures representing other segments of this chain: 2dob (60-140), 1n69 (195-273), 2r0r, 2r1q,2rb3,3bop,3bqq (405-484).', '0000-00-00'),
(687, 258, 158, 6, '1r7g', 'Nonstructural protein 5a, anchor domain, structure in micelles', 'NMR', 'in', 5.3, 0.9, 90, 5, -15.1, '', 1, 0, '', '', '0000-00-00'),
(688, 258, 242, 6, '2ajo', 'Nonstructural protein 5a, anchor domain, structure in micelles', 'NMR', 'in', 5.0, 1.0, 86, 15, -11.8, '', 1, 0, '', '', '0000-00-00'),
(692, 261, 14, 4, '2hac', 'Zeta-zeta dimer of T cell receptor', 'NMR', 'A out', 31.9, 2.3, 7, 10, -43.2, '', 2, 2, '', 'Other PDB structures correspond to water soluble domains.', '0000-00-00'),
(693, 15, 6, 4, '2i37', 'Rhodopsin, a photobleached state', '4.15', 'A out', 31.9, 1.5, 5, 1, -79.1, '', 1, 7, '', 'This is probably a photobleached state, not metarhodopsin II.', '0000-00-00'),
(694, 260, 232, 2, '2nr9', 'Protease GlpG', '2.20', 'A in', 28.2, 1.6, 13, 3, -52.0, '', 1, 6, '', 'Calculated hydrophobic thickness is much smaller than in a homologoues (~40% sequence identity) protease from E. coli.', '0000-00-00'),
(690, 15, 6, 4, '2i36', 'Rhodopsin, a dimer', '4.1', 'A out', 30.0, 1.4, 4, 4, -125.6, '', 2, 14, '', 'Two structures of retinal-free opsin (2i36 and 2i37) contain a loosely packed dimer formed through association of TM helices I.  This is one of several GPCR dimerization modes discussed in the literature. Similar I-to-I dimers were found in 2D crystals of rhodopsin (Krebs et al. 2003). However, tilts of invividual molecules of rhodopsin with respect to non-crystallographic C2 symmetry axis in 2D crystals were smaller.', '0000-00-00'),
(691, 260, 9, 2, '2ic8', 'Protease GlpG', '2.1', 'A in', 28.2, 1.6, 14, 0, -62.1, '', 1, 6, '', '', '0000-00-00'),
(695, 262, 9, 3, '2j58', 'Outer membrane lipoprotein Wza', '2.25', 'A in', 31.1, 0.8, 0, 0, -123.8, '', 8, 8, '', '', '0000-00-00'),
(696, 70, 14, 23, '1zmi', 'Alpha-defensin 2', '1.15', 'out', 2.3, 1.1, 81, 17, -3.7, '', 1, 0, '', '', '0000-00-00'),
(697, 70, 14, 23, '1fd3', 'Beta-defensin 2', '1.3', 'out', 5.2, 1.2, 80, 12, -9.1, '', 1, 0, '', '', '0000-00-00'),
(698, 70, 53, 23, '1tv0', 'Alpha-defensin cryptdin-4', 'NMR', 'out', 2.9, 1.4, 67, 13, -4.5, '', 1, 0, '', '', '0000-00-00'),
(699, 70, 14, 23, '1zmm', 'Alpha-defensin 4', '1.60', 'out', 2.2, 1.0, 76, 10, -5.5, '', 1, 0, '', '', '0000-00-00'),
(700, 70, 14, 23, '1zmp', 'Alpha-defensin 5', '1.65', 'out', 4.2, 1.6, 84, 14, -2.8, '', 1, 0, '', '', '0000-00-00'),
(701, 70, 14, 23, '1zmq', 'Alpha-defensin 6', '2.10', 'out', 3.7, 1.6, 76, 18, -3.6, '', 1, 0, '', '', '0000-00-00'),
(702, 65, 243, 4, '1fho', 'PH domain of muscle M-line assembly protein unc-89', 'NMR', 'in', 2.3, 1.2, 25, 14, -4.3, '', 1, 0, '', '', '0000-00-00'),
(703, 65, 14, 4, '1u5d', 'PH domain of Src-associated adaptor 55  protein', 'NMR', 'in', 4.0, 1.8, 68, 18, -6.4, '', 2, 0, '', '', '0000-00-00'),
(704, 65, 53, 4, '1u5f', 'PH domain of Src-associated adaptor protein 2 homologue', '1.90', 'in', 2.2, 2.0, 56, 12, -4.9, '', 2, 0, '', '', '0000-00-00'),
(705, 65, 53, 4, '1u5e', 'PH domain of Src-associated adaptor protein 2', '2.6', 'in', 3.2, 2.0, 39, 13, -4.6, '', 2, 0, '', '', '0000-00-00'),
(706, 65, 14, 4, '1xd4', 'Son of sevenless homolog 1 (SOS-1)', '3.6', 'in', 1.9, 3.0, 79, 2, -4.5, '', 1, 0, '', 'Promotes the exchange of Ras-bound GDP by GTP.', '0000-00-00'),
(707, 65, 53, 4, '2d9v', 'PH domain containing retinal protein 1', 'NMR', 'in', 1.3, 1.3, 58, 14, -5.1, '', 1, 0, '', '', '0000-00-00'),
(708, 65, 14, 4, '2d9w', 'PH domain of docking protein 2', 'NMR', 'in', 2.2, 1.2, 13, 17, -3.5, '', 1, 0, '', '', '0000-00-00'),
(709, 65, 14, 4, '2d9x', 'Oxysterol binding protein-related protein 11', 'NMR', 'in', 1.4, 1.7, 55, 18, -3.1, '', 1, 0, '', '', '0000-00-00'),
(710, 263, 177, 23, '1aun', 'Osmotin-like protein', '1.8', 'out', 5.8, 1.0, 85, 11, -6.7, '', 1, 0, '', 'Induced by tobacco mosaic virus infection and wounding.', '0000-00-00'),
(711, 263, 177, 23, '1pcv', 'Osmotin', '2.3', 'out', 2.4, 1.9, 82, 19, -2.7, '', 1, 0, '', 'Induced by salt stress, abscisic acid (ABA), viral infection and wounding. Inhibits the germination and growth of the fungus Phytophthora infestans.', '0000-00-00'),
(712, 205, 70, 23, '2ddt', 'Sphingomyelinase C', '1.8', 'out', 4.1, 1.1, 59, 8, -7.6, '', 1, 0, '', 'Required, with sphingomyelinase, to effect target cell lysis (hemolysis). 	Sphingomyelin + H(2)O = N-acylsphingosine + choline phosphate.', '0000-00-00'),
(713, 264, 244, 23, '1xx1', 'Sphingomyelinase D 1', '1.7', '-12.0', 8.1, 1.0, 70, 8, -10.6, '', 1, 0, '', 'Has sphingomyelinase activity. Induces complement-dependent hemolysis.  Sphingomyelin + H(2)O = ceramide phosphate + choline.', '0000-00-00'),
(714, 126, 53, 4, '1ksg', 'ADP-ribosylation factor-like protein 2, complex with human PDEdelta', '2.3', 'in', 6.9, 1.7, 77, 15, -5.7, '', 1, 0, '', 'Probable regulator of PDEdelta binding to prenylated proteins. ', '0000-00-00'),
(715, 265, 51, 4, '1fjr', 'Ectodomain of G-protein coupled receptor Mth', '2.3', 'out', 1.8, 1.5, 56, 13, -4.3, '', 1, 0, '', '', '0000-00-00'),
(716, 399, 14, 4, '1doa', 'Rho GDP-dissociation inhibitor 1, complex with cell division control protein 42', '2.6', 'in', 1.1, 1.3, 87, 4, -3.1, '', 2, 0, '', 'Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.', '0000-00-00'),
(717, 63, 55, 4, '2chd', 'Rabphilin-3A, C2A domain', '1.9', 'in', 2.9, 1.6, 57, 19, -2.7, '', 1, 0, '', 'Other domains of this protein: RabBD (1zbd) and second C2 (3rpb).', '0000-00-00'),
(719, 63, 14, 4, '1yrk', 'Protein kinase C delta', '1.7', 'in', 2.0, 1.6, 52, 19, -1.8, '', 1, 0, '', '', '0000-00-00'),
(720, 266, 14, 4, '1rw6', 'E2 domain of amyloid beta A4 protein precursor', '2.8', 'out', 3.7, 0.8, 90, 1, -7.5, '', 8, 0, 'This complex may interacts simultaneously with two membrabes (Wang and Ha 2004).', 'Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Single-pass type I membrane protein.', '0000-00-00'),
(721, 58, 14, 10, '1h9f', 'Lamina-associated polypeptide 2 isoform alpha', 'NMR', 'in', 1.4, 1.1, 64, 16, -3.6, '', 1, 0, '', 'May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Different domain -1h9e.', '0000-00-00'),
(722, 74, 14, 12, '1xte', 'PX domain of serine/threonine-protein kinase Sgk3', '1.6', 'in', 1.2, 1.4, 77, 11, -2.9, '', 1, 0, '', 'Involved in the activation of potassium channels.', '0000-00-00'),
(723, 111, 70, 23, '1p6d', 'Phospholipase C', '2.0', 'out', 2.8, 1.0, 52, 6, -8.4, '', 1, 0, '', 'Required, with sphingomyelinase, to effect target cell lysis (hemolysis). 	A phosphatidylcholine + H(2)O = 1,2-diacylglycerol + choline phosphate.', '0000-00-00'),
(724, 77, 245, 12, '1z2q', 'LM-5 FYVE domain', 'NMR', 'in', 1.5, 1.5, 22, 19, -3.4, '', 1, 0, '', '', '0000-00-00'),
(725, 77, 14, 14, '1x4u', 'FYVE domain of protein 27', 'NMR', 'in', 4.3, 1.9, 38, 19, -6.9, '', 1, 0, '', 'Multi-pass membrane protein.', '0000-00-00'),
(726, 77, 53, 14, '1wfk', 'FYVE domain of protein 19', 'NMR', 'in', 4.3, 1.8, 17, 16, -5.5, '', 1, 0, '', '', '0000-00-00'),
(727, 78, 14, 4, '1xa6', 'Beta-chimaerin', '3.2', 'in', 2.1, 1.7, 65, 7, -5.1, '', 1, 0, '', 'GTPase-activating protein for p21-rac. Contains phorbol-ester/DAG-type zinc finger (C1 domain), Rho-GAP domain, and SH2 domain.', '0000-00-00'),
(728, 78, 55, 4, '1y8f', 'C1 domain of unc-13 homolog A', 'NMR', 'in', 2.5, 1.9, 16, 17, -2.9, '', 1, 0, '', 'Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. C2 domains of this protein: 2cjs, 2cjt.', '0000-00-00'),
(729, 78, 14, 4, '2db6', 'C1 domanin of SH3 and cysteine-rich domain-containing protein 3', 'NMR', 'in', 2.7, 0.1, 75, 0, -4.8, '', 1, 0, '', '', '0000-00-00'),
(730, 173, 91, 23, '1t6m', 'Phosphatidylinositol-specific phospholipase C', '2.1', 'out', 3.8, 1.4, 89, 13, -4.9, '', 1, 0, '', 'Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors. 	1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol. W47A/W242A mutant (2or2 PDB entry) forms dimer and has different conformation of membrane-interacting loops. ', '0000-00-00'),
(731, 143, 144, 4, '1yiv', 'Myelin P2 protein', '2.1', 'in', 1.3, 1.7, 53, 11, -4.8, '', 1, 0, '', '', '0000-00-00'),
(732, 244, 55, 4, '2a1l', 'Phosphatidylinositol transfer protein beta isoform', '2.1', 'in', 4.7, 1.7, 36, 17, -4.3, '', 1, 0, '', 'Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.', '0000-00-00'),
(733, 201, 44, 2, '2cx7', 'Sterol carrier protein 2', '1.7', 'in', 4.7, 1.3, 73, 13, -6.9, '', 1, 0, '', '', '0000-00-00'),
(734, 267, 246, 23, '2dde', 'Cinnamycin', 'NMR', 'out', 3.6, 1.9, 30, 24, -5.4, '', 1, 0, '', 'Can act as inhibitor of phospholipase A2, and of the angiotensin-converting enzyme. Shows inhibitory activities against herpes simplex virus and immunopotentiating activities. ', '0000-00-00'),
(735, 268, 21, 8, '2byo', 'Lipoprotein lppX', '2.10', 'out', 1.9, 1.7, 80, 13, -4.8, '', 1, 0, 'N-palmitoyl cysteine 27.', '', '0000-00-00'),
(736, 269, 14, 23, '2a01', 'Apolipoprotein A-I', '2.4', 'out', 4.8, 1.2, 63, 11, -6.5, '', 1, 0, '', '', '0000-00-00'),
(737, 270, 9, 2, '2hi7', 'DsbB - DsbA complex', '3.70', 'B in', 24.3, 3.0, 30, 0, -34.9, '', 1, 4, 'Calculated hydrophobic thickness and orientation are unreliable; they depend on position of a flexible loop.', 'Oxidizes periplasmic protein DsbA (included in the complex), which in turn oxidizes cysteines in other periplasmic proteins to make disulfide bonds. ', '0000-00-00'),
(738, 271, 215, 26, '2irg', 'Amphipathic alpha-helix of apolipoprotein', 'model', 'out', 6.4, 1.7, 83, 15, -12.1, '', 1, 0, 'Consistent with X-ray diffraction study by Hristova et al. (1999). ', '', '0000-00-00'),
(814, 110, 14, 4, '3d3l', '12S-Lipoxygenase', '2.6', 'A in', 5.0, 0.6, 51, 3, -9.0, '', 1, 0, '', '', '0000-00-00'),
(740, 15, 14, 4, '2iqr', 'Melanocortin-4 receptor model (active state) with agonist NDP-MSH', 'model', 'A out', 33.5, 2.0, 24, 0, -60.6, '', 1, 7, '', '', '0000-00-00'),
(741, 15, 14, 4, '2iqv', 'Melanocortin-4 receptor model (inactive state) with antagonist AGRP', 'model', 'A out', 31.9, 1.1, 19, 0, -49.1, '', 1, 7, '', '', '0000-00-00'),
(742, 15, 55, 4, '2iqo', 'Mu-opioid receptor model in active state with agonist', 'model', 'A out', 33.6, 1.6, 6, 5, -73.5, '', 1, 7, '', '', '0000-00-00'),
(743, 15, 55, 4, '2iql', 'Mu-opioid receptor model (inactive state) with antagonist', 'model', 'A out', 33.8, 1.6, 9, 1, -78.6, '', 1, 7, '', '', '0000-00-00'),
(744, 272, 247, 2, '2j7a', 'Cytochrome c nitrite reductase complex', '2.30', 'L in', 31.8, 3.1, 0, 2, -42.9, '', 2, 2, '', '', '0000-00-00'),
(745, 26, 232, 2, '2nq2', 'ABC transporter permease HI1471', '2.40', 'A in', 31.9, 0.9, 1, 1, -124.2, '', 2, 20, '', '', '0000-00-00'),
(746, 273, 28, 3, '2o4v', 'Porin OprP', '1.94', 'A in', 23.9, 1.1, 0, 0, -129.6, '', 3, 48, '', 'An arginine ladder in OprP mediates phosphate specific transfer across the outer membrane', '0000-00-00'),
(747, 275, 53, 4, '1gc6', 'Radixin', '2.9', 'in', 15.4, 1.8, 17, 12, -17.9, '', 1, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Membrane penetration depth of the protein strongly depends on the bound lipid conformation (the protein can move away of the hydrophobic boundary). Transfer energy was calculated without contribution of the bound lipid (orientation of the protein without bound lipid is different). \r\n', '', '0000-00-00'),
(748, 65, 53, 4, '1btn', 'Spectrin beta chain', '2.0', 'in', 13.7, 1.6, 57, 19, -17.3, '', 1, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Membrane penetration depth of the protein is poorly defined because it strongly depends on the bound lipid conformation (the protein can move away of the hydrophobic boundary). Transfer energy was calculated without contribution of the bound lipid (orientation of the protein without bound lipid is different).\r\n', '', '0000-00-00'),
(749, 65, 53, 4, '1fhx', 'Cytohesin-3 (Grp1)', '2.5', 'in', 15.0, 1.2, 18, 15, -16.4, '', 1, 0, 'This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Membrane penetration depth of the protein strongly depends on the bound lipid conformation (the protein can move away of the hydrophobic boundary). Transfer energy was calculated without contribution of the bound lipid (orientation of the protein without bound lipid is different).\r\n', 'The disulfide-bound dimer is possibly an artifact (?).', '0000-00-00'),
(751, 29, 29, 1, '2nwl', 'Proton glutamate symport protein, outward-facing state', '3.0', 'A in', 29.8, 1.3, 0, 0, -202.1, '', 3, 39, '', '', '0000-00-00'),
(752, 277, 55, 6, '2h8a', 'Microsomal glutathione S-transferase 1', '3.20', 'A out', 29.7, 0.7, 0, 1, -47.7, '', 3, 12, '', 'Fold is similar to that in a subdomain of main subunit of cytochrome c oxidase.', '0000-00-00'),
(753, 89, 9, 3, '2hdi', 'Colicin I receptor complex with binding domain of Colicin Ia', '2.50', 'A out', 23.4, 0.9, 3, 3, -72.7, '', 1, 22, '', '', '0000-00-00'),
(754, 89, 9, 3, '2hdf', 'Colicin I receptor', '2.65', 'A in', 23.4, 0.9, 4, 0, -70.9, '', 1, 22, '', '', '0000-00-00'),
(755, 6, 18, 7, '2e74', 'Cytochrome b6f', '3.00', 'A in', 31.2, 0.8, 0, 0, -222.1, '', 16, 26, '', '', '0000-00-00'),
(759, 277, 14, 6, '2q7r', 'FLAP protein (5-lipoxygenase activator)', '4.00', 'A out', 30.3, 1.3, 0, 1, -70.8, '', 3, 12, '', 'Hydrophobic thickness is poorly defined due to significant misplacement of C-terminal helix, probably induced by binding of inhibitor, like C4 leucotriene synthase (2uuh). This protein interacts with lipoxygenase (see 1lox in OPM).', '0000-00-00'),
(760, 43, 9, 3, '2ixx', 'Osmoporin OMPC,  isoform 1', '2.5', 'A out', 26.2, 1.3, 0, 1, -142.5, '', 3, 48, '', '', '0000-00-00'),
(761, 43, 9, 3, '2ixw', 'Osmoporin OMPC, isoform 2', '2.70', 'A out', 24.5, 1.0, 0, 0, -121.0, '', 3, 48, '', '', '0000-00-00'),
(762, 279, 248, 3, '2qdz', 'Filamentous hemagglutinin transporter FhaC', '3.15', 'A out', 24.4, 1.1, 7, 7, -69.1, '', 1, 16, '', '', '0000-00-00'),
(763, 280, 44, 2, '2yvx', 'Magnesium ion transporter-E (MgtE)', '3.5', 'A in', 31.1, 0.9, 0, 0, -69.2, '', 2, 10, '', '', '0000-00-00'),
(764, 281, 11, 4, '2qts', 'Acid-sensing ion channel', '1.90', 'A in', 36.6, 0.9, 15, 0, -67.8, '', 3, 6, '', 'Asymmetric trimer.', '0000-00-00'),
(765, 282, 28, 3, '2odj', 'Outer membrane porin OprD', '2.90', 'A in', 23.0, 0.8, 8, 0, -63.1, '', 1, 18, '', '', '0000-00-00'),
(766, 191, 144, 23, '1w52', 'Pancreatic lipase-related protein 2', '2.9', 'out', 4.8, 0.2, 83, 0, -12.7, '', 1, 0, '', '', '0000-00-00'),
(767, 113, 137, 23, '2qhd', 'Snake phospholipase A2, group II (ecarpholin S)', '1.9', 'out', 8.1, 0.6, 79, 5, -12.5, '', 1, 0, '', '', '0000-00-00'),
(768, 113, 252, 23, '2i0u', 'Snake phospholipase A2', '2.2', 'out', 5.6, 0.9, 88, 9, -15.2, '', 1, 0, '', '', '0000-00-00'),
(769, 190, 249, 23, '2dsn', 'Thermostable lipase', '1.5', 'out', 4.9, 0.9, 32, 3, -7.7, '', 1, 0, '', '', '0000-00-00'),
(770, 54, 14, 6, '2hi4', 'Cytochrome P450 1A2', '1.9', 'in', 6.9, 1.0, 66, 9, -16.2, '', 1, 0, 'This cytochrome has a tentative N-terminal TMH, consistent with the calculated orientation.', '', '0000-00-00'),
(771, 189, 250, 23, '2qua', 'Lipase LipA', '1.9', 'out', 8.9, 0.2, 59, 0, -37.5, '', 1, 0, '', '', '0000-00-00'),
(772, 291, 251, 23, '2fx5', 'Lipase', '1.8', 'out', 5.5, 1.0, 50, 5, -8.4, '', 1, 0, '', '', '0000-00-00'),
(773, 283, 9, 2, '2qfi', 'Ferrous-iron efflux pump fieF', '3.80', 'A in', 25.0, 1.3, 1, 2, -32.4, '', 2, 12, '', '', '0000-00-00'),
(774, 15, 14, 4, '2rh1', 'Beta-2 adrenergic receptor, dimer', '2.4', 'A out', 31.8, 0.9, 0, 1, -143.2, '', 2, 14, '', '2rh1 and 3d4s represent chimera of adrenergic receptor and T4 lysozyme. 2r4r, 2r4s and 3kj6 represent complex with antibodies (not included because the cytoplasmic parts of TM helices and loops are disordered and missing in the crystal structures).  ', '0000-00-00'),
(775, 39, 9, 3, '2qom', 'Serine protease EspP, postcleavage state', '2.66', 'A out', 25.1, 1.6, 6, 7, -55.9, '', 1, 12, '', '', '0000-00-00'),
(776, 54, 14, 6, '3b6h', 'Prostacyclin synthase (cytochrome P450 8A1)', '1.62', 'in', 5.0, 1.6, 64, 18, -6.3, '', 1, 0, 'It has a tentative N-terminal TMH, consistent with the calculated orientation.', '', '0000-00-00'),
(777, 22, 178, 2, '3b9w', 'Rh-like protein', '1.30', 'A out', 31.0, 1.4, 0, 0, -145.2, '', 3, 24, '', '', '0000-00-00'),
(778, 17, 55, 4, '2r9r', 'Potassium channel Kv1.2., structure in a membrane-like environment', '2.40', 'B in', 30.8, 0.6, 0, 0, -252.0, '', 4, 28, '', '', '0000-00-00'),
(779, 276, 9, 2, '2r6g', 'Maltose transporter MalFGK, outward conformation', '2.8', 'F in', 29.9, 1.1, 3, 1, -98.0, '', 2, 14, '', '', '0000-00-00'),
(780, 27, 278, 2, '3b60', 'Lipid flippase MsbA', '3.70', 'A in', 31.8, 0.9, 0, 0, -98.5, '', 2, 12, '', '3b5w and 3b5x are CA atom structures of MsbA from E. coli and Vibrio cholerae ', '0000-00-00'),
(781, 4, 187, 7, '2o01', 'Photosystem I', '3.40', 'A in', 26.9, 0.0, 3, 0, -269.9, '', 16, 43, '', 'Calculated boundaries are unreliable due to the relatively poor quality of the structure. Subunit "K" of unassigned sequence has been removed. This is a mixture of subunits from different species.', '0000-00-00'),
(782, 31, 25, 6, '3b9b', 'Calcium ATPase, E2-Pi state, alternative conformation', '2.65', 'A in', 29.9, 1.6, 16, 2, -58.1, '', 1, 10, '', '', '0000-00-00'),
(783, 31, 57, 4, '3b8e', 'Sodium-potassium pump,  E2-Pi state', '3.50', 'A in', 30.7, 0.9, 12, 0, -93.6, '', 3, 12, '', '', '0000-00-00'),
(784, 31, 253, 4, '3b8c', 'Plasma membrane ATPase 2, E1-ATP state', '3.6', 'A in', 29.5, 1.5, 9, 0, -56.8, '', 1, 10, '', '', '0000-00-00'),
(785, 45, 9, 3, '2guf', 'Outer membrane cobalamin transporter BtuB, meso form', '1.95', 'A in', 23.4, 0.9, 6, 7, -69.3, '', 22, 22, '', '', '0000-00-00'),
(786, 14, 13, 1, '2ei4', 'Archaerhodopsin-2, trimeric', '2.10', 'A out', 30.5, 1.2, 0, 1, -143.9, '', 3, 21, '', '', '0000-00-00'),
(787, 17, 254, 2, '3beh', 'Bacterial cyclic nucleotide regulated ion channel', '3.10', 'A in', 30.6, 0.8, 0, 0, -205.7, '', 4, 28, '', '3beh and 2zd9 represent structure of TM domain (5-230)', '0000-00-00'),
(788, 287, 14, 4, '2jwa', 'Receptor tyrosine kinase erbB-2 dimer', 'NMR', 'A out', 31.9, 2.9, 13, 9, -46.6, '', 2, 2, '', '', '0000-00-00'),
(789, 285, 20, 1, '3b4r', 'Site-2 protease (S2P) metalloprotease', '3.30', 'B in', 29.9, 1.4, 23, 0, -65.0, '', 1, 6, '', 'It forms a trimer of antiparallel dimers. Structures of two molecules in each dimer (e.g. A and B) are significantly different. This structure (subunit B) is more "closed". ', '0000-00-00'),
(790, 286, 52, 15, '3bkd', 'M2 proton channel of Influenza A, open state, ligand-free', '2.05', 'E out', 29.8, 1.4, 5, 2, -55.4, '', 4, 4, '', 'This detergent-disordered structure is not exactly symmetric. Subunits (helices) G and H are closer packed with each other than others. Two crystal structures (3bkd and 3c9j) are close to each other (CA atom rmsd of 1.1 A) but strongly differ from NMR structure, 2rlf (rmsd of 3.8-3.9 A). 3c9j is similar to amantadine-bound solid state NMR model 2h95 (rmsd of 2.4A). ', '0000-00-00'),
(791, 288, 145, 2, '2vl0', 'Ligand gated ion channel, inactive conformation', '3.30', 'A out', 31.8, 1.3, 0, 0, -107.6, '', 5, 20, '', '', '0000-00-00'),
(792, 286, 52, 15, '3c9j', 'M2 proton channel of Influenza A, open state, complex with amantadine', '3.50', 'A out', 29.4, 1.4, 2, 3, -65.6, '', 4, 4, '', 'The tetramer is not exactly symmetric. Two crystal structures (3bkd and 3c9j) are close to each other (CA atom rmsd of 1.1 A) but strongly differ from NMR structure, 2rlf (rmsd of 3.8-3.9 A). This structure is similar to amantadine-bound solid state NMR model 2h95 (rmsd of 2.4A). ', '0000-00-00'),
(793, 176, 14, 19, '2z5x', 'Monoamine oxidase A', '2.2', 'A out', 30.3, 2.1, 19, 1, -21.3, '', 1, 1, '', '', '0000-00-00'),
(800, 42, 257, 3, '3bry', 'Toluene transporter TbuX', '3.20', 'A out', 25.4, 1.5, 1, 2, -57.7, '', 1, 14, '', '', '0000-00-00'),
(801, 42, 258, 3, '3bs0', 'Toluene transporter TodX', '2.60', 'A out', 23.4, 1.4, 7, 7, -61.3, '', 14, 14, '', '', '0000-00-00'),
(803, 15, 260, 4, '2vt4', 'Beta-1 adrenergic receptor, complex with antagonist', '2.70', 'B out', 32.4, 2.1, 4, 1, -76.0, '', 1, 7, '', '', '0000-00-00'),
(804, 282, 28, 3, '2qtk', 'Protein OpdK', '2.80', 'A in', 23.3, 1.0, 3, 0, -62.4, '', 1, 18, '', '', '0000-00-00'),
(805, 32, 261, 2, '3chx', 'Particulate Methane Monooxygenase', '3.90', 'B in', 29.8, 0.4, 0, 0, -152.0, '', 10, 30, '', '', '0000-00-00'),
(806, 292, 14, 19, '2k4t', 'VDAC-1 channel', 'NMR', 'A in', 22.0, 1.5, 1, 1, -34.8, '', 1, 19, '', 'Transmembrane topology was predicted based on the distribution of charged residues ', '0000-00-00'),
(807, 287, 14, 4, '2k1k', 'Receptor tyrosine kinase EphA1', 'NMR', 'A out', 30.2, 1.5, 0, 5, -43.3, '', 2, 2, '', 'This is NMR model at normal pH. At the lower pH, N-terminus of TM helix partly unfolds, which produces a wider interhelical angle (see 2k1l).', '0000-00-00'),
(808, 15, 6, 4, '3dqb', 'Opsin, complex with C-terminal peptide of Galpha subunit of transducin ', '3.20', 'A out', 31.9, 1.1, 8, 0, -76.4, '', 1, 7, '', '', '0000-00-00'),
(809, 16, 14, 4, '3d9s', 'Aquaporin-5', '2.0', 'A in', 30.3, 0.9, 0, 0, -133.3, '', 4, 32, '', '', '0000-00-00'),
(810, 20, 9, 2, '2vv5', 'Mechanosensitive channel protein MscS, open state', '3.45', 'A out', 27.8, 1.9, 0, 0, -138.7, '', 7, 21, '', '', '0000-00-00'),
(811, 54, 14, 6, '3e6i', 'Cytochrome P450 2E1', '2.2', 'A in', 8.3, 2.0, 49, 8, -14.2, '', 1, 0, '', '', '0000-00-00'),
(812, 54, 14, 6, '3czh', 'Cytochrome P450 2R1', '2.30', 'A in', 8.3, 1.5, 48, 13, -13.2, '', 1, 0, '', '', '0000-00-00'),
(813, 291, 14, 4, '3d59', 'Plasma platelet activating factor acetylhydrolase ', '1.5', 'A out', 5.5, 1.2, 87, 10, -13.6, '', 1, 0, '', '', '0000-00-00'),
(815, 28, 62, 2, '3din', 'Preprotein translocase SecY', '4.5', 'C in', 26.9, 0.1, 5, 0, -63.3, '', 3, 13, '', '', '0000-00-00'),
(816, 270, 9, 2, '2k74', 'Disulfide bond formation protein B', 'NMR', 'A in', 29.7, 2.4, 26, 1, -50.2, '', 1, 4, '', 'Calculated hydrophobic thilness and orientation are unreliable; they depend on positions of flexible loops. Spin-labeling data indicate much deeper penetration of loop 114-120.', '0000-00-00'),
(1263, 392, 9, 3, '2y8p', 'Endo-type membrane-bound lytic murein transglycosylase A', '2.00', 'in', 0.0, 3.6, 86, 15, -2.2, '', 1, 0, '', 'A purely interfacial binding mode, with peptidoglycan binding cavity and lipidated N-terminus oriented towards the membrane (Cys 15 missing in the structure is lipidated).', '0000-00-00'),
(817, 292, 14, 19, '2jk4', 'VDAC-1 channel', '4.10', 'A in', 23.4, 2.3, 0, 1, -40.0, '', 1, 19, '', 'Derived from X-ray diffraction and NMR data. Forms a dimer in crystal.', '0000-00-00'),
(818, 28, 44, 2, '2zjs', 'Preprotein translocase SecY', '3.20', 'Y in', 30.7, 1.2, 7, 0, -100.7, '', 2, 11, '', '', '0000-00-00'),
(819, 14, 263, 2, '3ddl', 'Xanthorhodopsin', '1.90', 'A out', 28.2, 1.8, 11, 0, -60.7, '', 1, 7, '', '', '0000-00-00'),
(820, 15, 14, 4, '3eml', 'A2A adenosine receptor, complex with antagonist', '2.60', 'A out', 31.8, 1.2, 8, 12, -66.1, '', 1, 7, '', '', '0000-00-00'),
(821, 189, 108, 23, '2veo', 'Triacylglycerol lipase, closed (inactive) state', '2.20', 'out', 8.0, 1.0, 84, 10, -7.1, '', 1, 0, '', '', '0000-00-00'),
(822, 54, 264, 13, '3dan', 'Plant cytochrome P450 74A (allene oxide synthase)', '1.80', 'in', 7.5, 0.4, 64, 2, -24.1, '', 1, 0, '', 'Localized in lipid monolayer of rubber particles.', '0000-00-00'),
(823, 204, 14, 9, '2e3q', 'STAR-related lipid transfer protein 11, complex with C18 ceramide', '2.00', 'in', 4.3, 2.0, 41, 17, -3.7, '', 1, 0, '', '', '0000-00-00'),
(824, 204, 14, 9, '2e3m', 'STAR-related lipid transfer protein 11, apoprotein (open state)', '2.20', 'in', 3.4, 1.1, 44, 12, -6.1, '', 1, 0, '', '', '0000-00-00'),
(825, 189, 265, 23, '2ory', 'Lipase', '2.20', 'out', 6.3, 1.1, 62, 10, -12.0, '', 1, 0, '', '', '0000-00-00'),
(826, 190, 266, 23, '2z8x', 'Lipase', '1.40', 'out', 6.8, 1.7, 74, 6, -8.2, '', 1, 0, '', '', '0000-00-00'),
(827, 252, 232, 3, '3emo', 'Autotransporter Hia, a different conformation', '3.00', 'A out', 22.8, 1.9, 4, 0, -40.1, '', 3, 12, '', '', '0000-00-00'),
(828, 288, 268, 2, '3eam', 'Ligand gated ion channel, active conformation', '2.90', 'A out', 32.7, 0.9, 0, 1, -183.4, '', 5, 20, '', '', '0000-00-00'),
(829, 294, 267, 8, '2jln', 'Sodium-hydantoin transporter Mhp1, outward-facing conformation', '2.85', 'A in', 29.8, 1.5, 16, 0, -98.9, '', 1, 12, '', '', '0000-00-00'),
(830, 295, 262, 2, '3dh4', 'Sodium/sugar symporter vSGLT, substrate-bound', '2.70', 'A in', 30.0, 0.7, 0, 0, -184.0, '', 2, 30, '', 'Hydrophobic thickness is underestimated due to poorly ordered protein structure near the hydrocarbon boundaries. ', '0000-00-00'),
(831, 42, 28, 3, '3dwo', 'FadL homologue', '2.20', 'X out', 24.8, 1.6, 6, 3, -54.7, '', 1, 14, '', '', '0000-00-00'),
(832, 292, 53, 19, '3emn', 'VDAC-1 channel', '2.30', 'X out', 23.4, 1.1, 5, 1, -52.5, '', 1, 19, '', '', '0000-00-00'),
(833, 296, 44, 3, '3dzm', 'Major outer membrane protein from Thermus thermophilus', '2.8', 'A in', 28.5, 2.6, 6, 10, -50.3, '', 1, 8, '', '', '0000-00-00'),
(834, 35, 16, 3, '2k0l', 'Outer membrane protein A from Klebsiella', 'NMR', 'A in', 24.3, 2.3, 18, 6, -26.8, '', 1, 8, '', 'One of loops with undefined position has been removed. ', '0000-00-00'),
(835, 89, 250, 3, '3csl', 'Hemophore receptor HasR', '2.70', 'A in', 25.4, 1.3, 4, 5, -72.2, '', 1, 22, '', '', '0000-00-00'),
(836, 6, 270, 7, '2zt9', 'Cytochrome b6f', '3.00', 'A in', 31.2, 1.0, 0, 1, -214.2, '', 16, 26, '', '', '0000-00-00'),
(837, 297, 278, 3, '3fid', 'Lipid A deacylase LpxR', '1.90', 'A in', 25.6, 2.0, 24, 0, -58.6, '', 1, 12, '', '', '0000-00-00'),
(839, 26, 9, 2, '2qi9', 'ABC transporter BtuCD, complex with BtuF', '2.60', 'A in', 29.4, 0.9, 4, 4, -123.5, '', 2, 22, '', 'The dimer is significantly asymmetric, unlike 1l7v. ', '0000-00-00'),
(840, 5, 42, 7, '3bz1', 'Photosystem II', '2.90', 'D in', 31.6, 0.4, 0, 0, -409.7, '', 34, 72, '', 'This model combines PDB entries 3bz1 and 3bz2. Subunit "y" was renamed as "W" to avoid duplication.', '0000-00-00'),
(841, 286, 52, 15, '2rlf', 'M2 proton channel of Influenza A, closed state', 'NMR', 'A out', 33.2, 2.5, 17, 5, -66.5, '', 4, 4, '', 'This is structure in a micelle. A significant rearrangement of C-terminal surface helix was detected by EPR spin-labeling in membrane: FFK segment probably forms a continuation of TM helix, whereas the C-terminal helices bind to the membrane surface and go in direction opposite to the central channel. This model with classic "rows into grooves" packing of TM helices differs from two crystallographic structures (3bkd and 3c9j; CA atom rmsd of 3.8-3.9 A), and from all solid state NMR models (rmsd >3 A; 2h95 is the closest, with rmsd of 2.3 A). 2kih is S31N mutant.', '0000-00-00'),
(842, 301, 53, 4, '3g5u', 'P-glycoprotein', '3.80', 'A in', 31.8, 1.2, 4, 0, -100.6, '', 1, 12, '', '', '0000-00-00'),
(843, 274, 14, 4, '2k9j', 'Integrin alphaIIb-beta3 transmembrane complex', 'NMR', 'A out', 36.4, 3.3, 20, 1, -56.4, '', 2, 2, '', 'This is a heterodimer. Related PDB structures are shown for TM domain of integrin beta3 (2k1a is alphaIIb segment in bicelles; 2rmz and 2rn0 are NMR models of beta3 TM segment in bicelles). \r\n\r\n\r\nStructures of C-terminal cytoplasmic domain include partially unfolded conformations in the presence of micelles (2kv9,2l1c,1kup,1kuz,1m8o,1s4x) and folded crystal structures (1mk7,1mk9).\r\n\r\nStructures of N-terminal extracellular domain - see 3fcs.', '0000-00-00'),
(844, 276, 9, 2, '3dhw', 'Methionine importer MetNI', '3.70', 'A out', 29.1, 1.2, 1, 2, -82.3, '', 2, 10, '', '', '0000-00-00'),
(845, 300, 14, 19, '2j5d', 'BNip3 transmembrane domain dimer', 'NMR', 'A out', 30.8, 2.5, 12, 0, -35.8, '', 2, 2, '', 'The dimer is strongly asymmetric, apparently a result of dynamics and insufficient  constraints.', '0000-00-00'),
(846, 45, 248, 3, '3efm', 'Outer membrane receptor FauA', '2.33', 'A in', 24.7, 0.6, 11, 0, -77.5, '', 1, 22, '', '', '0000-00-00'),
(847, 16, 14, 4, '3gd8', 'Aquaporin-4', '1.8', 'A in', 29.8, 1.1, 0, 1, -122.9, '', 4, 32, '', '', '0000-00-00'),
(849, 85, 271, 2, '2qks', 'Kir3.1-prokaryotic Kir channel chimera', '2.20', 'A in', 30.5, 1.4, 0, 1, -88.6, '', 4, 12, '', '', '0000-00-00'),
(850, 302, 272, 4, '2zw3', 'Connexin 26 gap junction channel (beta-2 protein)', '3.50', 'A in', 32.2, 0.5, 0, 0, -155.9, '', 6, 24, '', '', '0000-00-00'),
(851, 25, 9, 2, '2rdd', 'Multidrug efflux transporter AcrB with YajC subunit ', '3.50', 'A in', 28.4, 0.5, 0, 0, -156.2, '', 6, 39, '', '', '0000-00-00'),
(852, 270, 9, 2, '2zup', 'DsbB - DsbA complex', '3.70', 'B in', 24.2, 2.9, 3, 8, -18.3, '', 1, 4, '', 'Hydrophobic thickness and orientation are affected by a highly flexible loop.', '0000-00-00'),
(853, 270, 9, 2, '2zuq', 'Disulfide bond formation protein B', '3.30', 'A in', 27.9, 3.1, 27, 1, -36.6, '', 1, 4, '', '', '0000-00-00'),
(854, 17, 41, 8, '3eff', 'Potassium channel KcsA, full-length, closed', '3.80', 'K in ', 31.8, 1.3, 0, 0, -107.3, '', 12, 12, '', '', '0000-00-00'),
(855, 368, 9, 2, '2qcu', 'Glycerol-3-phosphate dehydrogenase (GlpD)', '1.75', 'A in', 4.5, 1.5, 74, 11, -8.4, '', 1, 0, '', '', '0000-00-00'),
(856, 176, 212, 8, '2rgh', 'Alpha-glycerophosphate oxidase (GlpO)', '2.30', 'A in', 3.9, 1.4, 71, 12, -6.2, '', 1, 0, '', '', '0000-00-00'),
(857, 178, 36, 25, '3b7n', 'Yeast Sec14 Homolog Sfh1 (YKL091C)', '1.86', 'A in', 2.9, 1.5, 65, 18, -5.8, '', 1, 0, '', '', '0000-00-00'),
(858, 303, 273, 2, '2q3l', 'Uncharacterized protein', '2.25', 'A in', 6.0, 0.5, 64, 4, -12.6, '', 1, 0, '', '', '0000-00-00'),
(859, 178, 14, 4, '1o6u', 'SEC14-like protein 2 (supernatant factor protein)', '2.05', 'A in ', 3.6, 1.4, 62, 14, -4.9, '', 1, 0, '', 'Weakly bound GOLD domain was removed from the structure during calculations.', '0000-00-00'),
(860, 244, 53, 4, '1kcm', 'Phosphatidylinositol transfer protein alpha isoform', '2.00', 'A in', 5.3, 1.4, 59, 5, -11.0, '', 1, 0, '', '', '0000-00-00'),
(861, 31, 274, 4, '2zxe', 'Sodium-potassium pump, E2-Pi state', '2.40', 'A in', 31.9, 1.8, 9, 0, -96.3, '', 3, 13, '', '', '0000-00-00'),
(862, 15, 36, 4, '2k9p', 'TM1-TM2 fragment of fungal STE2 receptor', 'NMR', 'A out', 29.8, 3.1, 21, 4, -10.5, '', 1, 2, '', '', '0000-00-00'),
(863, 25, 28, 2, '2v50', 'Multidrug exporter MexB', '3.0', 'A in', 28.6, 1.0, 0, 1, -167.3, '', 3, 36, '', '', '0000-00-00'),
(864, 13, 38, 7, '2w5j', 'ATP synthase of chloroplast', '3.80', 'A out', 32.8, 0.7, 0, 0, -116.3, '', 14, 28, '', '', '0000-00-00'),
(865, 305, 39, 22, '2olv', 'Penicillin-binding protein 2', '2.8', 'out', 3.7, 2.0, 58, 8, -7.3, '', 1, 0, '', 'Protein contains a TM helix (not in the structure).', '0000-00-00'),
(866, 305, 58, 2, '2oqo', 'Penicillin-binding protein 1A', '2.1', 'out', 3.0, 1.0, 40, 6, -11.0, '', 1, 0, '', 'This is only one of several domains. Orientation was calculated for a monomer. The physiological significance of the dimer observed in crystal was debated. Protein contains a TM helix (not in the structure).', '0000-00-00'),
(867, 305, 9, 2, '3fwm', 'Penicillin-binding protein 1B', '2.1', 'out', 29.9, 4.6, 23, 4, -18.9, '', 1, 0, '', 'The structure contains a part of TM helix (it is longer in the lower resolution structure, 3fwl).', '0000-00-00'),
(868, 304, 9, 2, '3h5m', 'Arginine/agmatine antiporter (AdiC), outward-facing conformation', '3.61', 'A in ', 29.0, 0.8, 0, 0, -128.9, '', 2, 26, '', '', '0000-00-00'),
(869, 175, 58, 2, '3h28', 'Sulfide:quinone oxidoreductase', '2.00', 'out', 2.4, 0.1, 90, 0, -19.4, '', 3, 0, '', '', '0000-00-00'),
(870, 16, 277, 4, '2w2e', 'Aquaporin AQY1', '1.15', 'A in', 30.2, 0.8, 0, 0, -131.7, '', 4, 32, '', '', '0000-00-00'),
(871, 201, 14, 4, '2c0l', 'Sterol carrier protein 2, complex with Pex5p', '2.30', 'in', 5.7, 1.4, 89, 16, -6.2, '', 2, 0, '', '', '0000-00-00'),
(872, 135, 219, 23, '2gvm', 'Hydrophobin I', '2.30', 'out', 5.3, 1.1, 27, 18, -8.7, '', 1, 0, '', '', '0000-00-00'),
(873, 201, 14, 11, '1ikt', 'Sterol carrier protein 2 like domain of multifunctional enzyme type 2 ', '1.75', 'in', 3.5, 1.2, 75, 17, -4.0, '', 1, 0, '', '', '0000-00-00'),
(874, 305, 39, 22, '3hzs', 'Glycosyltransferase MtgA', '2.10', 'out', 7.0, 1.1, 54, 9, -14.6, '', 1, 0, '', '', '0000-00-00'),
(875, 54, 14, 6, '2q9f', 'Cytochrome P450 46A1 (cholesterol 24-hydrolase)', '1.90', 'in', 2.8, 1.0, 86, 7, -5.8, '', 0, 0, '', '', '0000-00-00'),
(876, 307, 9, 2, '2kdc', 'Diacylglycerol kinase (DAGK)', 'NMR', 'A in', 25.5, 1.8, 0, 0, -39.9, '', 3, 9, '', '', '0000-00-00'),
(877, 304, 278, 2, '3hqk', 'Arginine/agmatine antiporter (AdiC), outward-facing conformation', '3.20', 'A in', 29.8, 1.0, 0, 0, -124.6, '', 2, 26, '', '', '0000-00-00'),
(878, 300, 14, 19, '2ka1', 'BNip3 transmembrane domain dimer', 'NMR', 'A out', 31.8, 2.3, 24, 8, -34.9, '', 2, 2, '', '', '0000-00-00'),
(879, 89, 279, 3, '3fhh', 'Outer membrane heme transporter ShuA', '2.60', 'A in', 24.6, 0.9, 5, 0, -70.7, '', 1, 22, '', '', '0000-00-00'),
(885, 73, 256, 5, '3i65', 'Dihydroorotate dehydrogenase', '2.50', 'in', 5.1, 1.0, 47, 6, -13.6, '', 1, 0, '', '', '0000-00-00'),
(884, 309, 9, 23, '2wcd', 'Pore-forming haemolysin E (HlyE)', '3.29', 'A in', 30.8, 0.7, 0, 0, -148.3, '', 12, 36, '', 'Water-soluble form of this protein - 1qoy.', '0000-00-00'),
(883, 308, 55, 4, '3hd7', 'SNARE complex (syntaxin 1A, SNAP-25 and synaptobrevin 2)', '3.40', 'A in', 28.5, 1.9, 3, 7, -29.3, '', 2, 2, '', '', '0000-00-00'),
(886, 174, 113, 6, '3g49', 'Corticosteroid 11-beta-dehydrogenase, isozyme 1', '2.50', 'out', 7.0, 0.5, 90, 1, -15.9, '', 2, 0, '', 'Single N-terminal TM helix 8-24, consistent with calculated orientation of the water-soluble dimer. ', '0000-00-00'),
(887, 277, 14, 6, '3dww', 'Microsomal prostaglandin E synthase 1', '3.50', 'A out', 31.9, 1.1, 2, 1, -97.3, '', 3, 12, '', '', '0000-00-00'),
(888, 310, 131, 4, '3h9v', 'ATP-gated P2X4 ion channel in the closed state', '3.10', 'A in ', 27.6, 1.3, 0, 1, -61.3, '', 3, 6, '', '', '0000-00-00'),
(889, 311, 280, 2, '2q6v', 'Beta-1,2-glucuronosyltrnansferase GumK', '2.28', 'in', 5.2, 1.0, 61, 8, -9.5, '', 1, 0, '', '', '0000-00-00'),
(890, 312, 9, 2, '2h1h', 'Heptosyltransferase WaaC', '2.40', 'in', 5.0, 1.1, 67, 5, -9.1, '', 1, 0, '', '', '0000-00-00'),
(891, 312, 9, 2, '1psw', 'LPS heptosyltransferase II', '2.00', 'in', 3.1, 1.1, 58, 8, -5.6, '', 1, 0, '', '', '0000-00-00'),
(892, 287, 14, 4, '2k9y', 'Receptor tyrosine kinase EphA2', 'NMR', 'A out', 31.8, 3.2, 12, 14, -32.1, '', 2, 2, '', '', '0000-00-00'),
(893, 304, 20, 1, '3gia', 'ApcT transporter, inward-facing conformation', '2.32', 'A in', 29.9, 1.4, 11, 2, -92.1, '', 1, 12, '', '', '0000-00-00'),
(894, 126, 36, 9, '2k5u', 'ADP-ribosylation factor 1 (ARF1)', 'NMR', 'in', 2.9, 1.6, 24, 18, -5.5, '', 1, 0, '', '1mr3 is yeast ARF2', '0000-00-00'),
(895, 54, 14, 6, '3eqm', 'Cytochrome P450 19A1 (aromatase, estrogen synthetase)', '2.90', 'in', 6.1, 1.2, 58, 8, -12.4, '', 1, 0, '', '', '0000-00-00'),
(896, 54, 14, 6, '3ld6', 'Sterol 14-alpha-demethylase (CYP51)', '2.80', 'in', 8.9, 0.6, 57, 2, -16.8, '', 1, 0, '', '', '0000-00-00'),
(897, 369, 57, 5, '2gmh', 'Flavoprotein-ubiquinone oxydoreductase', '2.50', 'in', 7.2, 0.8, 38, 4, -18.5, '', 1, 0, '', '', '0000-00-00'),
(898, 313, 269, 22, '2vql', 'Anion-specific porin B', '3.16', 'in', 6.2, 0.3, 83, 2, -12.7, '', 1, 0, '', 'This is predicted position of the monomer. An oligomer forms transmembrane structure.', '0000-00-00'),
(899, 178, 14, 4, '2d4q', 'Neurofibromin', '2.3', 'in', 1.6, 2.0, 34, 19, -3.3, '', 1, 0, '', 'It also includes a PH domain.', '0000-00-00'),
(901, 318, 9, 2, '3blc', 'Protein OxaA, periplasmic domain', '2.5', 'out', 6.6, 0.5, 40, 11, -7.0, '', 1, 0, '', '', '0000-00-00'),
(902, 317, 9, 2, '3da4', 'Colicin-M', '1.7', 'out', 2.5, 0.9, 49, 11, -5.5, '', 1, 0, '', '', '0000-00-00'),
(903, 316, 286, 4, '2vqp', 'Matrix protein', '1.6', 'in', 2.9, 1.1, 86, 10, -6.1, '', 1, 0, '', '', '0000-00-00'),
(904, 104, 14, 23, '2dwf', 'Pulmonary surfactant-associated protein B fragments', 'NMR', 'out', 5.6, 1.3, 77, 4, -9.5, '', 1, 0, '', '2dwf and 2jou represent the longest fragment 208-278. Shorter fragments: 1rg3 and 1rg4 (263-278); 1kmr (211-225).', '0000-00-00'),
(905, 314, 282, 23, '1ytr', 'Plantaricin-A', 'NMR', 'out', 9.0, 0.5, 78, 10, -9.4, '', 1, 0, '', '', '0000-00-00'),
(906, 315, 283, 23, '2vk9', 'Alpha-toxin', '2.8', 'out', 3.2, 1.0, 80, 2, -5.2, '', 1, 0, '', '', '0000-00-00'),
(907, 257, 281, 23, '1d7n', 'Mastoparan-L', 'NMR', 'out', 6.5, 1.7, 82, 16, -7.5, '', 1, 0, '', '', '0000-00-00'),
(908, 315, 284, 23, '2bvl', 'Toxin B', '2.2', 'out', 2.0, 1.1, 24, 14, -4.2, '', 1, 0, '', '', '0000-00-00'),
(909, 315, 285, 23, '2vkh', 'Cytotoxin L', '2.3', 'out', 1.4, 2.0, 51, 17, -4.5, '', 1, 0, '', '', '0000-00-00'),
(910, 90, 55, 6, '2jp3', 'Na,K-ATPase regulatory protein FXYD1 (phospholemman)', 'NMR', 'A out', 31.8, 3.2, 18, 7, -20.2, '', 1, 1, '', '', '0000-00-00'),
(911, 17, 70, 8, '3e86', 'NaK potassium channel, open state', '1.60', 'A in', 27.6, 0.9, 0, 0, -90.0, '', 4, 12, '', '', '0000-00-00'),
(912, 22, 178, 2, '3b9y', 'Rh-like protein', '1.85', 'A out', 29.8, 1.3, 0, 0, -150.1, '', 3, 33, '', '', '0000-00-00'),
(913, 22, 14, 4, '3hd6', 'Rhesus Glycoprotein RhCG', '2.10', 'A in', 31.8, 0.7, 0, 0, -174.1, '', 3, 36, '', '', '0000-00-00'),
(914, 75, 288, 23, '1wwn', 'Beta-insect excitatory toxin BmKIT1', 'NMR', 'out', 4.2, 1.1, 72, 6, -4.4, '', 1, 0, '', '', '0000-00-00'),
(915, 160, 289, 23, '1lmm', 'Psalmotoxin-1', 'NMR', 'out', 2.4, 1.6, 71, 15, -4.4, '', 1, 0, '', '', '0000-00-00'),
(916, 239, 290, 23, '1wqk', 'Toxin APETx1', 'NMR', 'out', 4.0, 1.4, 32, 18, -7.3, '', 1, 0, '', '', '0000-00-00'),
(917, 239, 290, 23, '1wxn', 'Toxin APETx2', 'NMR', 'out', 4.9, 1.7, 33, 18, -5.5, '', 1, 0, '', '', '0000-00-00'),
(918, 160, 291, 23, '1mb6', 'Huwentoxin-4', 'NMR', 'out', 4.4, 0.8, 70, 12, -5.8, '', 1, 0, '', '', '0000-00-00'),
(919, 320, 123, 23, '2ew4', 'T-2-conotoxin MrIA', 'NMR', 'out', 2.5, 1.5, 81, 19, -3.0, '', 1, 0, '', '', '0000-00-00'),
(920, 160, 292, 23, '2a2v', 'Jingzhaotoxin-11', 'NMR', 'out', 3.0, 1.8, 74, 19, -4.6, '', 1, 0, '', '', '0000-00-00'),
(921, 160, 74, 23, '1oav', 'Omega-agatoxin-4A', 'NMR', 'out', 4.0, 1.1, 75, 14, -4.0, '', 1, 0, '', '', '0000-00-00'),
(922, 63, 14, 4, '3f00', 'Synaptotagmin-1, C2A domain (Calcium free)', '1.36', 'in', 1.4, 1.5, 29, 18, -3.3, '', 1, 0, '', '', '0000-00-00'),
(923, 283, 9, 2, '3h90', 'Ferrous-iron efflux pump fieF', '2.90', 'A in', 29.6, 0.8, 0, 2, -83.9, '', 2, 12, '', '', '0000-00-00'),
(924, 321, 44, 2, '3i9v', 'Hydrophilic domain of respiratory complex I', '3.10', 'in', 5.1, 14.0, 34, 10, -11.6, '', 8, 0, '', '', '0000-00-00'),
(925, 13, 294, 7, '2wie', 'F1F0 ATP synthase', '2.13', 'A out', 31.8, 0.8, 0, 0, -133.6, '', 15, 30, '', '', '0000-00-00'),
(926, 113, 295, 23, '1pa0', 'Phospholipase A2 BnSP-7', '2.2', 'out', 2.8, 1.0, 78, 10, -6.9, '', 1, 0, '', '', '0000-00-00'),
(927, 63, 14, 4, '2nq3', 'E3 ubiquitin-protein ligase Itchy homolog', '1.8', 'in', 3.4, 1.9, 25, 17, -6.7, '', 1, 0, '', '', '0000-00-00'),
(928, 113, 96, 23, '2oqd', 'Phospholipase A2 bothropstoxin-2', '2.3', 'out', 6.0, 0.6, 85, 4, -7.8, '', 1, 0, '', '', '0000-00-00'),
(929, 191, 14, 23, '2ppl', 'Pancreatic lipase-related protein 1', '2.2', 'out', 7.1, 0.9, 79, 6, -10.2, '', 1, 0, '', '', '0000-00-00'),
(930, 63, 14, 4, '2r83', 'Synaptotagmin-1 C2A-C2B domains', '2.7', 'in', 3.0, 1.9, 89, 10, -3.8, '', 1, 0, '', '', '0000-00-00'),
(931, 190, 296, 23, '2w22', 'Triacylglycerol lipase', '2.2', 'out', 5.6, 0.0, 86, 0, -22.4, '', 1, 0, '', '', '0000-00-00'),
(932, 322, 297, 23, '2wg7', 'Phospholipase A2 homolog', '2.0', 'out', 4.0, 1.1, 77, 3, -10.7, '', 1, 0, '', '', '0000-00-00'),
(933, 113, 298, 23, '3dih', 'Phospholipase A2 homolog, ammodytin L', '2.6', 'out', 5.0, 0.4, 82, 5, -14.4, '', 1, 0, '', '', '0000-00-00'),
(934, 323, 9, 3, '2wjr', 'Acidic sugar-specific porin NanC', '1.80', 'A in', 23.3, 1.5, 4, 4, -47.5, '', 1, 12, '', '', '0000-00-00'),
(935, 146, 6, 4, '3fsn', 'Retinal pigment epitelium-specific 65 kDa protein', '2.14', 'in', 7.8, 1.0, 73, 10, -10.3, '', 1, 0, '', '', '0000-00-00'),
(936, 324, 14, 4, '2klu', 'Human CD4', 'NMR', 'A out', 31.8, 2.7, 11, 14, -23.2, '', 1, 1, '', '', '0000-00-00'),
(937, 54, 214, 7, '2ve3', 'Cytochrome P450 120a1', '2.10', 'in', 5.2, 1.5, 52, 15, -6.8, '', 1, 0, '', 'Thylakoid localization was not experimentally verified.', '0000-00-00'),
(938, 54, 221, 6, '3g1q', 'Sterol 14-alpha-demethylase (CYP51)', '1.89', 'in', 8.1, 1.5, 62, 12, -10.8, '', 1, 0, '', '', '0000-00-00'),
(939, 54, 299, 6, '2wuz', 'Sterol 14-alpha-demethylase (CYP51)', '2.35', 'in', 4.0, 1.1, 75, 11, -9.9, '', 1, 0, '', '', '0000-00-00'),
(940, 74, 14, 12, '3fog', 'PX domain of sorting nexin-17 (SNX17)', '2.80', 'in', 3.4, 1.0, 69, 12, -4.9, '', 1, 0, '', '', '0000-00-00'),
(941, 74, 14, 4, '2ar5', 'PX domain of C2alpha-PI3 kinase', '1.80', 'in', 5.6, 0.9, 83, 17, -3.7, '', 1, 0, '', '', '0000-00-00'),
(942, 325, 300, 23, '3hde', 'Lysozyme', '1.95', 'out', 1.8, 1.4, 55, 10, -4.7, '', 1, 0, '', '', '0000-00-00'),
(943, 74, 14, 9, '2wwe', 'PX domain of Phosphoinositide-3-kinase, class 2, gamma polypeptide', '1.25', 'in', 2.5, 1.3, 56, 16, -4.8, '', 1, 0, '', '', '0000-00-00'),
(944, 282, 301, 3, '3jty', 'BenF-like porin', '2.58', 'A in', 24.2, 1.2, 1, 0, -59.8, '', 1, 18, '', '', '0000-00-00'),
(1005, 343, 309, 13, '3n6o', 'DrrA protein, PtdIns(4) binding domain', '2.50', 'in', 5.1, 1.4, 56, 10, -4.9, '', 1, 1, '', '3l0m has longer chain (313-640) but lower resolution; 3l0i (210-534) does not cover the lipid binding domain. 3nku represents N-terminal domain (9-215).', '0000-00-00'),
(945, 111, 119, 23, '2wxu', 'Alpha-toxin (PHLC_CLOP1) ', '1.80', '0ou', 4.0, 0.9, 85, 5, -7.0, '', 1, 0, '', '', '0000-00-00'),
(946, 111, 119, 23, '1qmd', 'Alpha-toxin (PHLC_CLOP1) , different conformation', '2.20', 'out', 4.8, 1.0, 80, 8, -6.7, '', 1, 0, '', '', '0000-00-00'),
(947, 54, 302, 6, '3l4d', 'Sterol 14-alpha-demethylase (CYP51)', '2.75', 'in', 8.4, 1.8, 66, 9, -12.6, '', 1, 0, '', '', '0000-00-00'),
(948, 329, 303, 2, '2j69', 'Dynamin-like protein', '3.00', 'in', 4.0, 7.0, 15, 10, -5.5, '', 1, 0, '', '', '0000-00-00'),
(949, 54, 55, 5, '3k9v', 'Cytochrome P450 24a1 (1,25-dihydroxyvitamin D(3) 24-hydroxylase)', '2.50', 'in', 6.6, 1.0, 49, 6, -9.6, '', 1, 0, '', '', '0000-00-00'),
(950, 326, 46, 2, '3kly', 'Formate transporter 1, FocA', '2.10', 'A in', 31.4, 0.5, 1, 0, -188.2, '', 5, 35, '', '', '0000-00-00'),
(951, 326, 9, 2, '3kcu', 'Formate transporter 1, FocA', '2.24', 'A in ', 29.9, 0.7, 0, 0, -160.9, '', 5, 35, '', '', '0000-00-00'),
(1041, 286, 52, 15, '2kwx', 'M2 proton channel of Influenza A, closed state, V27A mutant', 'NMR', 'A out', 33.4, 1.9, 2, 3, -63.4, '', 4, 4, '', '', '0000-00-00'),
(952, 286, 52, 15, '2kix', 'M2 proton channel of Influenza B', 'NMR', 'A out', 31.8, 1.2, 2, 3, -64.4, '', 4, 4, '', '', '0000-00-00'),
(953, 327, 247, 2, '3k3f', 'Urea transporter', '2.3', 'A in ', 29.4, 0.8, 0, 0, -124.4, '', 3, 30, '', '', '0000-00-00'),
(954, 29, 29, 1, '3kbc', 'Proton glutamate symport protein, inward-facing state', '3.51', 'A in', 28.1, 0.9, 0, 1, -158.8, '', 3, 30, '', '', '0000-00-00'),
(955, 328, 55, 4, '3kg2', 'Glutamate receptor 2', '3.60', 'A out', 31.8, 2.0, 0, 0, -93.0, '', 4, 16, '', '', '0000-00-00'),
(956, 14, 23, 1, '3a7k', 'Halorhodopsin', '2.00', 'A out', 33.8, 1.4, 1, 0, -141.3, '', 3, 21, '', '', '0000-00-00'),
(957, 5, 304, 7, '3a0b', 'Photosystem II', '3.70', 'D in', 31.8, 0.4, 0, 0, -397.1, '', 34, 72, '', '', '0000-00-00'),
(958, 6, 11, 5, '3h1j', 'Cytochrome bc1, mitochondrial', '3.0', 'C in', 28.2, 0.6, 0, 0, -184.8, '', 10, 24, '', '', '0000-00-00'),
(959, 276, 9, 2, '3fh6', 'Maltose transporter MalFGK, inward conformation, TMH 1 deleted', '2.80', 'F in', 29.9, 0.6, 3, 1, -97.8, '', 2, 13, '', '', '0000-00-00'),
(960, 45, 9, 3, '2ysu', 'Outer membrane cobalamin transporter BtuB, complex with colicin E2 R-domain', '3.50', 'A in', 24.2, 1.0, 5, 0, -75.2, '', 1, 22, '', '', '0000-00-00'),
(961, 45, 9, 3, '1ujw', 'Outer membrane cobalamin transporter BtuB, complex with colicin E3 R-domain', '2.75', 'A in', 23.6, 1.1, 5, 0, -71.5, '', 1, 22, '', '', '0000-00-00'),
(962, 28, 20, 1, '2yxr', 'Preprotein translocase SecY, mutant with full-plug (TM2a) deletion', '3.60', 'A in', 29.7, 0.8, 4, 4, -95.6, '', 3, 12, '', 'Mutant with half-plug deletion (2yxq) has the same conformation. ', '0000-00-00'),
(963, 16, 55, 4, '2zz9', 'Aquaporin-4, different conformation of loops with lipids', '2.80', 'A in', 29.5, 0.7, 0, 0, -115.6, '', 4, 28, '', '', '0000-00-00'),
(964, 22, 9, 2, '2ns1', 'Ammonia channel, complex with inhibitory GlnK', '1.96', 'A out', 29.1, 0.7, 0, 0, -148.7, '', 3, 33, '', '', '0000-00-00'),
(965, 6, 30, 2, '1zrt', 'Cytochrome bc1, bacterial', '3.50', 'C in', 29.9, 0.9, 0, 0, -178.6, '', 6, 20, '', 'The structure has many missing side-chain atoms.', '0000-00-00'),
(967, 85, 11, 4, '3jyc', 'Potassium channel Kir 2.2', '3.11', 'A in', 30.5, 1.4, 0, 1, -119.9, '', 4, 12, '', '', '0000-00-00'),
(968, 331, 215, 26, '3cay', 'Self-assembling lipopeptide detergent', '1.20', 'out', 14.5, 1.3, 78, 9, -16.4, '', 2, 0, 'The designed Alacoil dimers are assembled into octameric "micelles". Transfer energy of the dimer was calculated without the covalently attached acyl chains.', '', '0000-00-00'),
(969, 39, 28, 3, '3kvn', 'Esterase EstA', '2.50', 'A out', 24.4, 1.5, 4, 2, -48.7, '', 1, 12, '', 'Full-length autotransporter.', '0000-00-00'),
(971, 286, 52, 15, '2kqt', 'M2 proton channel of Influenza A, complex with amantadine', 'NMR', 'A out', 30.2, 1.3, 0, 4, -59.6, '', 4, 4, '', '', '0000-00-00');
INSERT INTO `protein` (`id`, `family_id`, `species_id`, `membrane_id`, `pdbid`, `name`, `resolution`, `topology`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`, `tau`, `numsubunits`, `numstrands`, `verification`, `comments`, `date_added`) VALUES
(972, 332, 227, 2, '3kp9', 'Vitamin K epoxide reductase', '3.60', 'A in', 29.8, 1.6, 0, 0, -45.1, '', 1, 5, '', '', '0000-00-00'),
(973, 31, 57, 4, '3kdp', 'Sodium-potassium pump, different conformation', '3.50', 'A in', 31.4, 1.4, 7, 0, -95.3, '', 3, 12, '', '', '0000-00-00'),
(974, 16, 305, 2, '3llq', 'Aquaporin Z2', '2.01', 'A in', 29.8, 0.6, 0, 0, -134.5, '', 4, 32, '', '', '0000-00-00'),
(975, 333, 9, 2, '2ksf', 'Sensor protein kdpD', 'NMR', 'A in', 26.2, 4.0, 45, 1, -27.9, '', 1, 4, '', 'Hydrophobic thickness and orientation are unreliable.', '0000-00-00'),
(976, 333, 9, 2, '2ksd', 'Aerobic respiration control sensor protein acrB', 'NMR', 'A in', 27.9, 2.8, 9, 1, -33.6, '', 1, 2, '', 'Hydrophobic thickness and orientation are unreliable.', '0000-00-00'),
(977, 333, 9, 2, '2kse', 'Sensor protein qseC', 'NMR', 'A in', 31.3, 2.5, 19, 0, -35.7, '', 1, 2, '', 'Hydrophobic thickness and orientation are unreliable.', '0000-00-00'),
(978, 298, 9, 2, '3hfx', 'L-carnitine/gamma-butyrbetaine antiporter CaiT, substrate-bound', '3.15', 'A in', 29.8, 0.8, 0, 0, -203.5, '', 3, 42, '', '', '0000-00-00'),
(979, 17, 55, 4, '3lnm', 'Potassium channel Kv1.2. - Kv2.1. paddle chimera', '2.90', 'I in', 31.1, 0.9, 0, 0, -260.7, '', 4, 28, '', '', '0000-00-00'),
(980, 43, 24, 3, '3a2s', 'Porin B (PorB)', '2.20', 'A in', 24.4, 1.0, 0, 0, -102.1, '', 3, 48, '', '', '0000-00-00'),
(981, 204, 14, 4, '2r55', 'StAR-related lipid transfer protein 5', '2.50', 'in', 1.7, 1.2, 47, 19, -4.8, '', 0, 0, '', '', '0000-00-00'),
(982, 334, 306, 8, '3l7l', 'Teichoic acid biosynthesis protein F', '2.70', 'in', 6.9, 2.0, 35, 15, -10.8, '', 1, 0, '', '', '0000-00-00'),
(983, 340, 57, 23, '1d6x', 'Tritrpticin', 'NMR', 'out', 9.4, 2.6, 81, 38, -8.1, '', 1, 0, '', '', '0000-00-00'),
(984, 335, 36, 4, '2kit', 'Serine/threonine-protein kinase TOR1, FATC domain', 'NMR', 'in', 6.3, 1.0, 87, 18, -6.4, '', 1, 0, '', '', '0000-00-00'),
(985, 336, 307, 23, '2kns', 'Pardaxin', 'NMR', 'out', 4.0, 0.7, 84, 7, -11.1, '', 1, 0, '', '', '0000-00-00'),
(986, 337, 14, 23, '2k6o', 'Cathelicidin', 'NMR', 'out', 8.1, 0.4, 86, 8, -15.7, '', 1, 0, '', '', '0000-00-00'),
(987, 223, 6, 23, '1y58', 'Lactoferricin B', 'NMR', 'out', 2.9, 1.4, 86, 18, -3.7, '', 1, 0, '', 'A fragment of lactotransferrin (1blf is full-lenght chain)', '0000-00-00'),
(988, 339, 6, 23, '1qx9', 'Indolicidin (cathelicidin-4), a cyclic analog', 'NMR', 'out', 6.6, 1.9, 46, 15, -7.7, '', 1, 0, '', '', '0000-00-00'),
(989, 341, 215, 26, '1qvl', 'Antimicrobial cationic cyclic hexapeptide', 'NMR', 'out', 4.2, 1.6, 84, 15, -6.8, '', 1, 0, '', '', '0000-00-00'),
(990, 338, 308, 23, '2kjf', 'Carnocyclin A', 'NMR', 'out', 2.1, 1.1, 61, 12, -4.6, '', 1, 0, '', '', '0000-00-00'),
(1146, 28, 111, 6, '2wwb', 'Preprotein translocase Sec61', '6.48', 'A in', 26.3, 0.5, 13, 0, -60.5, '', 3, 12, '', 'Orientation is very approximate due to poor resolution of the structure.', '0000-00-00'),
(991, 294, 267, 8, '2jlo', 'Sodium-hydantoin transporter Mhp1, ligand-bound', '4.0', 'A in', 31.2, 0.8, 15, 0, -96.5, '', 1, 12, '', '', '0000-00-00'),
(992, 294, 267, 8, '2x79', 'Sodium-hydantoin transporter Mhp1, inward-facing conformation', '3.80', 'A in', 30.7, 1.1, 13, 0, -85.0, '', 1, 12, '', '', '0000-00-00'),
(997, 17, 55, 4, '3lut', 'Potassium channel Kv1.2.', '2.90', 'I in', 25.1, 0.5, 0, 0, -153.1, '', 4, 24, '', '', '0000-00-00'),
(1280, 31, 25, 6, '3ar9', 'Calcium ATPase, E2 state, Ca-free, different conformation', '2.6', 'A in', 29.0, 0.9, 20, 0, -73.8, '', 1, 10, '', '', '0000-00-00'),
(998, 85, 5, 2, '2wll', 'Potassium channel Kirbac1.1, closed state', '3.65', 'A in ', 33.4, 2.4, 0, 0, -109.1, '', 4, 8, '', '', '0000-00-00'),
(999, 85, 17, 2, '2wlk', 'Potassium channel Kirbac3.1, latched state', '2.80', 'A in', 29.8, 2.4, 0, 0, -78.7, '', 4, 8, '', '', '0000-00-00'),
(1000, 85, 17, 2, '2wlj', 'Potassium channel Kirbac3.1, semi-latched state', '2.60', 'A in', 29.3, 1.2, 0, 0, -90.7, '', 4, 8, '', '', '0000-00-00'),
(1001, 85, 17, 2, '2wlh', 'Potassium channel Kirbac3.1, unlatched state', '2.60', 'A in', 30.5, 1.3, 0, 0, -99.0, '', 4, 8, '', '', '0000-00-00'),
(1002, 5, 42, 7, '3kzi', 'Photosystem II, monomeric form', '3.60', 'A in ', 31.8, 0.5, 0, 0, -310.1, '', 16, 36, '', '', '0000-00-00'),
(1003, 281, 11, 4, '3hgc', 'Acid-sensitive ion channel, conformation at low pH', '1.90', 'A in', 24.1, 0.7, 0, 0, -37.9, '', 3, 6, '', '', '0000-00-00'),
(1004, 342, 232, 2, '3m73', 'Tellurite resistance protein tehA homolog', '1.15', 'A in', 29.1, 1.4, 0, 0, -157.4, '', 3, 30, '', '', '0000-00-00'),
(1009, 54, 14, 6, '3mdm', 'Cytochrome P450 46A1 (cholesterol 24-hydrolase), different conformer', '1.60', 'in', 3.8, 1.3, 51, 8, -5.9, '', 1, 0, '', '', '0000-00-00'),
(1010, 39, 9, 3, '3aeh', 'Hemoglobin-binding protease Hbp autotransporter', '2.0', 'A out', 25.2, 1.1, 4, 0, -41.9, '', 1, 12, '', '', '0000-00-00'),
(1043, 17, 1, 1, '2kyh', 'Potassium channel KvAP, sensor domain', 'NMR', 'in', 28.6, 1.4, 19, 4, -44.6, '', 1, 5, '', '', '0000-00-00'),
(1012, 126, 36, 9, '2ksq', 'ADP-ribosylation factor 1 (ARF1)', 'NMR', 'in', 4.7, 0.1, 62, 0, -10.4, '', 1, 0, '', '', '0000-00-00'),
(1013, 344, 9, 3, '3jqo', 'Outer membrane complex of type IV secretion system (VirB7/VirB9/VirB10 complex)', '2.6', 'in', 8.3, 1.0, 82, 0, -6.3, '', 42, 0, '', 'VirB10 (TraF) is membrane-associated subunit.', '0000-00-00'),
(1014, 344, 155, 3, '2bhv', 'TrbI protein', '3.0', 'in', 3.1, 1.3, 42, 11, -6.4, '', 1, 0, '', 'Homolog of TraF/VirB10', '0000-00-00'),
(1015, 345, 90, 8, '2wuj', 'Septium site-determining protein DivIVA', '1.40', 'in', 4.0, 1.8, 2, 18, -5.4, '', 2, 0, '', '', '0000-00-00'),
(1016, 123, 159, 15, '2x7r', 'Envelope glycoprotein gp41', '2.0', 'out', 5.5, 1.1, 0, 10, -10.9, '', 3, 0, '', '', '0000-00-00'),
(1017, 346, 53, 14, '3lll', 'Protein kinase C and casein kinase substrate in neurons protein 2', '3.3', 'In', 1.9, 0.4, 88, 1, -5.4, '', 2, 0, '', '', '0000-00-00'),
(1018, 23, 14, 4, '1vry', 'Glycine receptor, alpha1 subunit', 'NMR', 'out', 23.2, 3.7, 5, 9, -25.3, '', 1, 2, '', '', '0000-00-00'),
(1019, 347, 311, 2, '1waz', 'MerF bacterial mercury uptake transporter', 'NMR', 'A in', 20.8, 3.4, 37, 4, -26.5, '', 1, 2, '', '', '0000-00-00'),
(1020, 84, 3, 23, '2xdc', 'Gramicidin A, anti-parallel double helix, left-landed ', '1.70', 'N/A', 22.0, 4.5, 48, 5, -28.0, '', 2, 2, '', '', '0000-00-00'),
(1021, 84, 3, 23, '2izq', 'Gramicidin A, anti-parallel double helix, right-handed ', '0.80', 'N/A', 18.8, 1.2, 28, 25, -18.7, '', 2, 2, '', '', '0000-00-00'),
(1022, 84, 3, 23, '1mic', 'Gramicidin A, parallel double helix, left-handed', 'NMR', 'N/A', 27.5, 5.4, 19, 17, -19.7, '', 2, 2, '', '', '0000-00-00'),
(1023, 17, 41, 8, '3f5w', 'Potassium channel KcsA, open inactivated state', '3.3', 'C in', 29.2, 0.7, 0, 0, -83.5, '', 4, 8, '', '', '0000-00-00'),
(1024, 17, 41, 8, '2a9h', 'Potassium channel KscA, complex with charibdotoxin', 'NMR ', 'A in', 31.8, 1.4, 0, 1, -105.1, '', 4, 8, '', '', '0000-00-00'),
(1025, 17, 41, 8, '3f7y', 'Potassiun channel KcsA, open 17A conformer', '3.4', 'A in', 31.3, 1.3, 0, 0, -82.3, '', 4, 8, '', '', '0000-00-00'),
(1026, 17, 41, 8, '3f7v', 'Potassium channel KcsA, open 23A conformer', '3.20', 'A in', 30.1, 1.1, 0, 0, -95.2, '', 4, 8, '', '', '0000-00-00'),
(1027, 17, 41, 8, '3fb5', 'Potassium channel KcsA, open 14.5 A conformer', '2.80', 'A in ', 33.7, 0.9, 0, 0, -115.9, '', 4, 8, '', '', '0000-00-00'),
(1028, 15, 14, 4, '3ny8', 'Beta-2 adrenergic receptor, slightly different conformation', '2.84', 'A out', 31.7, 1.2, 2, 3, -69.9, '', 1, 7, '', '', '0000-00-00'),
(1029, 17, 60, 1, '3ldc', 'Calcium-gated potassium channel MthK', '1.45', 'A in', 29.8, 0.8, 0, 0, -72.4, '', 4, 8, '', '', '0000-00-00'),
(1030, 40, 9, 3, '1qd5', 'Outer membrane phospholipase A, monomer', '2.17', 'A in', 24.6, 1.2, 6, 0, -52.6, '', 1, 12, '', '', '0000-00-00'),
(1031, 15, 255, 4, '2ziy', 'Squid rhodopsin, monomer', '3.70', 'A out', 32.9, 1.7, 11, 2, -75.1, '', 1, 7, '', '', '0000-00-00'),
(1032, 12, 192, 2, '3mk7', 'Bacterial cytochrome c oxidase, cbb3 type', '3.20', 'A in', 32.8, 1.2, 4, 4, -119.2, '', 4, 17, '', 'There is an additional TM helix of unknown sequence.', '0000-00-00'),
(1036, 222, 313, 23, '2ojm', 'Piscidin 1', 'NMR', '0ut', 10.6, 1.0, 82, 13, -16.3, '', 1, 0, '', '', '0000-00-00'),
(1037, 350, 9, 2, '3o7q', 'L-fucose-proton symporter', '3.14', 'A in', 30.7, 1.3, 6, 0, -85.3, '', 1, 12, '', '', '0000-00-00'),
(1038, 45, 9, 3, '3m8d', 'Outer membrane cobalamin transporter BtuB, with cyanocobalamin', '2.44', 'A in ', 23.3, 0.8, 6, 1, -70.5, '', 1, 22, '', '', '0000-00-00'),
(1039, 298, 9, 2, '2wsx', 'L-carnitine/gamm-butyrbetaine antiporter CaiT, open inward-facing conformation', '3.50', 'A in', 28.6, 0.7, 7, 0, -212.7, '', 3, 42, '', '', '0000-00-00'),
(1040, 298, 315, 2, '2wsw', 'L-carnitine/gamm-butyrbetaine antiporter CaiT, open inward-facing conformation', '2.29', 'A in ', 29.8, 0.5, 0, 0, -218.9, '', 3, 42, '', '', '0000-00-00'),
(1047, 260, 9, 2, '2xow', 'Protease GlpG', '2.09', 'A in', 29.0, 1.7, 15, 2, -59.0, '', 1, 6, '', '', '0000-00-00'),
(1048, 260, 9, 2, '2nrf', 'Protease GlpG', '2.60', 'A in', 26.8, 3.3, 14, 2, -45.5, '', 1, 6, '', '', '0000-00-00'),
(1049, 28, 316, 1, '3mp7', 'Preprotein translocase SecY', '2.90', 'A in', 30.1, 1.0, 5, 6, -94.0, '', 1, 10, '', '', '0000-00-00'),
(1050, 352, 46, 2, '3mkt', 'MDR efflux pump (Na+/drug antiporter)', '3.65', 'A in', 29.8, 1.1, 9, 0, -74.0, '', 1, 12, '', '', '0000-00-00'),
(1051, 19, 317, 4, '3org', 'ClC chloride transporter', '3.5', 'A in', 28.7, 1.3, 0, 2, -140.4, '', 2, 28, '', '', '0000-00-00'),
(1129, 254, 9, 3, '2x9k', 'Outer membrane protein G (OMPG), more complete loops', '2.18', 'A in', 24.7, 1.2, 5, 2, -62.7, '', 1, 14, '', '', '0000-00-00'),
(1052, 15, 14, 4, '3oe6', 'C-X-C chemokine receptor type 4', '3.20', 'A out', 35.3, 2.5, 8, 7, -79.7, '', 1, 7, '', 'Monomeric state.', '0000-00-00'),
(1053, 15, 14, 4, '3oe0', 'C-X-C chemokine receptor type 4', '2.90', 'A out', 32.2, 2.0, 5, 6, -133.2, '', 2, 14, '', 'Dimer. Note the reduced hydrophobic thickness compare to the monomeric state.', '0000-00-00'),
(1054, 15, 14, 4, '3odu', 'C-X-C chemokine receptor type 4', '2.50', 'A out', 31.2, 1.1, 0, 0, -129.5, '', 2, 17, '', '', '0000-00-00'),
(1055, 13, 294, 7, '2xqu', 'F1F0 ATP synthase', '1.84', 'A out', 31.8, 0.8, 0, 0, -129.7, '', 15, 30, '', '', '0000-00-00'),
(1056, 54, 14, 6, '3nxu', 'Cytochrome P450 3A4, an alternative conformation', '2.00', 'in', 9.3, 1.0, 52, 12, -17.5, '', 1, 0, '', '', '0000-00-00'),
(1057, 172, 14, 4, '3ohm', 'Phospholipase C-beta isoform 3, complex with G-protein subunit alpha Q', '2.70', 'in', 7.5, 2.0, 39, 5, -6.9, '', 2, 0, '', '', '0000-00-00'),
(1058, 172, 14, 4, '2zkm', 'Phospholipase C-beta isoform 2', '1.62', 'in', 2.2, 2.9, 38, 12, -3.6, '', 1, 0, '', '', '0000-00-00'),
(1059, 184, 51, 4, '1qon', 'Acetylcholinesterase', '2.72', 'out', 5.5, 1.6, 4, 13, -5.0, '', 1, 0, '', '', '0000-00-00'),
(1060, 110, 189, 4, '3dy5', '8R-Lipoxygenase, complete structure', '3.51', 'in', 2.3, 1.5, 88, 10, -3.2, '', 1, 0, '', 'The structure incudes an additional N-terminal allene oxide synthase domain. However, membrane-interacring loop and alpha-helix from other domains are disordered/missing in this structure.', '0000-00-00'),
(1061, 353, 53, 9, '3cwz', 'Rab6-interacting protein 1', '3.20', 'in', 3.7, 1.0, 77, 2, -5.2, '', 2, 0, '', '', '0000-00-00'),
(1062, 110, 148, 4, '1yge', 'Seed lipoxygenase-1', '1.40', 'in', 3.0, 2.6, 68, 3, -6.4, '', 1, 0, '', '', '0000-00-00'),
(1063, 191, 14, 23, '2oxe', 'Pancreatic lipase-related protein 2', '2.80', 'out', 10.2, 1.1, 88, 8, -10.1, '', 1, 0, '', '', '0000-00-00'),
(1064, 191, 111, 23, '1rp1', 'Pancreatic lipase-related protein 1', '2.10', 'out', 6.3, 1.0, 79, 4, -7.5, '', 1, 0, '', '', '0000-00-00'),
(1065, 110, 148, 4, '1rrh', 'Seed lipoxygenase-3', '2.00', 'in', 3.8, 1.3, 84, 7, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1066, 110, 148, 4, '2iuk', 'Seed lipoxygenase-D', '2.40', 'in', 3.7, 1.7, 85, 8, -6.2, '', 1, 0, '', '', '0000-00-00'),
(1067, 110, 148, 4, '2iuj', 'Seed lipoxygenase-B', '2.40', 'in', 1.7, 3.0, 51, 15, -4.8, '', 1, 0, '', '', '0000-00-00'),
(1068, 56, 14, 4, '2zoc', 'Annexin IV', '2.00', 'in', 3.4, 1.1, 82, 7, -7.6, '', 1, 0, '', '', '0000-00-00'),
(1069, 56, 6, 4, '1avc', 'Annexin VI', '2.90', 'in', 4.4, 1.0, 83, 1, -8.1, '', 1, 0, '', '', '0000-00-00'),
(1070, 56, 253, 4, '1ycn', 'Annexin D1', '2.51', 'in', 2.3, 1.1, 78, 14, -3.4, '', 1, 0, '', '', '0000-00-00'),
(1071, 56, 55, 4, '2zhj', 'Annexin IV', '1.35', 'in', 4.1, 1.0, 80, 1, -7.6, '', 1, 0, '', '', '0000-00-00'),
(1072, 15, 14, 4, '3pbl', 'Dopamine D3 receptor', '2.89', 'A out', 33.0, 1.8, 8, 1, -56.6, '', 1, 7, '', '', '0000-00-00'),
(1073, 63, 53, 14, '3nsj', 'Perforin-1', '2.75', 'out', 3.1, 1.0, 34, 11, -3.3, '', 1, 0, '', '', '0000-00-00'),
(1074, 354, 36, 6, '1rp4', 'Endoplasmic reticulum oxidoreductin', '2.20', 'out', 2.0, 1.8, 16, 9, -4.7, '', 1, 0, '', '', '0000-00-00'),
(1075, 354, 36, 6, '3m31', 'Endoplasmic reticulum oxidoreductin, a mutant', '1.85', 'out', 1.9, 1.2, 27, 9, -6.2, '', 1, 0, '', '', '0000-00-00'),
(1076, 152, 319, 23, '1s3r', 'Intermedilysin', '2.60', 'out', 5.3, 2.0, 61, 16, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1077, 152, 318, 23, '3cqf', 'Anthrolysin O', '3.10', 'out', 2.8, 1.0, 75, 1, -5.8, '', 1, 0, '', '', '0000-00-00'),
(1078, 113, 226, 23, '3jql', 'Snake phospholipase A2, group I, isoform 3', '1.20', 'out', 6.2, 1.0, 85, 5, -7.0, '', 1, 0, '', 'This phospholipase has significant membrane binding affinity only in the complex with bound peptide. ', '0000-00-00'),
(1079, 113, 98, 23, '2ok9', 'Snake phospholipase A2 homolog 1, group II', '2.34', 'out', 3.5, 1.4, 76, 7, -7.6, '', 1, 0, '', 'This is a myotoxin; no PA2 enzymatic activity.', '0000-00-00'),
(1080, 113, 14, 23, '3elo', 'Phospholipase A2, group IB', '1.55', 'out', 0.4, 1.5, 52, 16, -3.5, '', 1, 0, '', 'Very weak predicted membrane association.', '0000-00-00'),
(1081, 113, 98, 23, '2q2j', 'Snake phospholipase A2 homolog 2, group II', '1.65', 'out', 1.9, 1.2, 89, 9, -5.6, '', 1, 0, '', 'Myotoxin, no PLA2 activity.', '0000-00-00'),
(1082, 113, 173, 23, '1p7o', 'Snake phospholipase A2, acidic 2, group I', '2.30', 'out', 2.6, 0.5, 90, 2, -9.4, '', 1, 0, '', '', '0000-00-00'),
(1085, 113, 76, 23, '1ijl', 'Snake phospholipase A2, acidic, group II', '2.60', 'out', 4.2, 1.2, 83, 12, -7.5, '', 1, 0, '', '', '0000-00-00'),
(1086, 113, 298, 23, '3g8g', 'Snake phospholipase A2, ammodytoxin A, group II', '1.70', 'out', 4.1, 0.9, 80, 6, -11.0, '', 1, 0, '', '', '0000-00-00'),
(1087, 113, 96, 23, '3i03', 'Snake phospholipase A2 homolog bothropstoxin-1, group II', '1.48', 'out', 2.5, 0.5, 76, 5, -10.6, '', 1, 0, '', 'Myotoxin.', '0000-00-00'),
(1088, 113, 321, 23, '2qog', 'Snake phospholipase A2 crotoxin basic chain 2, group II', '2.28', 'out', 2.1, 1.1, 84, 8, -7.2, '', 1, 0, '', 'One of two chains in a heterodimer.', '0000-00-00'),
(1089, 113, 298, 23, '3g8h', 'Snake phospholipase A2, ammodytoxin C, group II', '1.35', 'out', 4.1, 1.1, 81, 8, -9.7, '', 1, 0, '', '', '0000-00-00'),
(1090, 113, 323, 23, '1y4l', 'Myotoxin II', '1.70', 'out', 2.8, 0.8, 76, 7, -10.3, '', 1, 0, '', '', '0000-00-00'),
(1091, 113, 324, 23, '2aoz', 'Myotoxin II', '2.08', 'out', 3.4, 0.7, 80, 3, -11.8, '', 1, 0, '', '', '0000-00-00'),
(1092, 113, 325, 23, '2ph4', 'Snake phospholipase A2 homolog zhaoermiatoxin, group II', '2.05', 'out', 4.8, 0.8, 86, 5, -9.2, '', 1, 0, '', 'Myonecrotic protein, low myotoxic activity, no PLA2 activity.', '0000-00-00'),
(1093, 113, 54, 23, '2osh', 'Snake phospholipase A2 natratoxin, group I', '2.20', 'out', 2.6, 1.6, 83, 11, -6.1, '', 1, 0, '', '', '0000-00-00'),
(1094, 113, 326, 23, '2wq5', 'Snake phospholipase A2, acidic, group I', '1.65', 'out', 3.4, 0.3, 89, 6, -6.2, '', 1, 0, '', '', '0000-00-00'),
(1095, 113, 101, 23, '2osn', 'Snake phospholipase A2, isoform 3', '2.50', 'out', 2.4, 0.6, 84, 4, -5.8, '', 1, 0, '', '', '0000-00-00'),
(1096, 113, 320, 23, '2h4c', 'Snake phospholipase A2, acidic', '2.60', 'out', 5.7, 1.1, 88, 10, -9.0, '', 1, 0, '', 'A subunit of heterodimer.', '0000-00-00'),
(1097, 63, 14, 14, '3fdw', 'Synaptotagmin-like protein 4', '2.20', 'in', 3.0, 2.0, 71, 17, -3.6, '', 1, 0, '', '', '0000-00-00'),
(1098, 63, 14, 14, '2d8k', 'Synaptotagmin-7 ', 'NMR', 'in', 2.8, 1.3, 27, 16, -6.6, '', 1, 0, '', '', '0000-00-00'),
(1099, 63, 14, 4, '1wfm', 'Synaptotagmin-13', 'NMR', 'in', 2.2, 1.9, 88, 15, -4.5, '', 1, 0, '', '', '0000-00-00'),
(1100, 63, 14, 4, '2enp', 'Synaptotagmin-17', 'NMR', 'in', 4.6, 1.5, 6, 14, -4.9, '', 1, 0, '', '', '0000-00-00'),
(1101, 63, 14, 4, '2dmg', 'Extended synaptotagmin-2', 'NMR', 'in', 2.4, 1.0, 76, 5, -4.8, '', 1, 0, '', '', '0000-00-00'),
(1103, 63, 14, 4, '2ep6', 'Multiple C2 and transmembrane domain-containing protein 2 (MCTP2)', 'NMR', 'in', 1.5, 1.5, 7, 15, -3.0, '', 1, 0, '', '', '0000-00-00'),
(1104, 63, 14, 4, '2jqz', 'E3 ubiquitin-protein ligase SMURF2', 'NMR', 'in', 4.2, 1.8, 23, 17, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1105, 63, 55, 4, '3kwu', 'Protein unc-13 homolog A, C2C domain', '1.37', 'in', 3.3, 1.9, 67, 16, -3.6, '', 1, 0, '', '', '0000-00-00'),
(1106, 63, 55, 4, '2cm5', 'Rabphilin-3A, C2B domain', '1.28', 'in', 2.5, 2.0, 56, 14, -4.1, '', 1, 0, '', '', '0000-00-00'),
(1107, 77, 55, 4, '1zbd', 'Rabphilin-3A', '2.6', 'in', 3.8, 1.8, 68, 15, -4.0, '', 2, 0, '', '', '0000-00-00'),
(1128, 19, 214, 2, '3nd0', 'ClC chloride transporter', '3.2', 'A in', 29.8, 0.7, 0, 1, -120.9, '', 2, 28, '', '', '0000-00-00'),
(1110, 357, 14, 4, '2l35', 'TYRO protein tyrosine kinase-binding protein', 'NMR', 'A out', 31.6, 3.2, 20, 5, -40.3, '', 2, 3, '', '', '0000-00-00'),
(1111, 358, 39, 8, '3p5n', 'Riboflavin transporter RibU', '3.60', 'A in', 30.6, 1.4, 6, 4, -53.5, '', 1, 6, '', '', '0000-00-00'),
(1112, 92, 329, 23, '1ifl', 'Capsid protein G8P', '5.0', 'A out', 30.8, 0.8, 0, 0, -93.6, '', 10, 10, '', '', '0000-00-00'),
(1113, 93, 328, 23, '2ifo', 'Capsid protein G8P', 'N/A', 'A out', 32.2, 1.9, 16, 3, -58.4, '', 12, 12, '', '', '0000-00-00'),
(1114, 93, 327, 23, '1ql1', 'Capsid protein G8P', '3.1', 'A out', 31.1, 1.6, 10, 0, -55.9, '', 12, 12, '', '', '0000-00-00'),
(1115, 295, 262, 2, '2xq2', 'Sodium/sugar symporter vSGLT, substrate-free', '2.73', 'A in ', 29.8, 0.7, 0, 0, -161.4, '', 2, 30, '', 'Each subunit includes an additional TM helix compare to that in 3dh4.', '0000-00-00'),
(1116, 12, 28, 2, '3o0r', 'Nitric oxide reductase subunit B', '2.7', 'B in', 31.7, 1.6, 5, 0, -107.7, '', 2, 13, '', '', '0000-00-00'),
(1117, 364, 28, 3, '2x27', 'Outer membrane protein OprG', '2.4', 'A in', 23.9, 1.7, 7, 3, -39.6, '', 1, 8, '', '', '0000-00-00'),
(1118, 359, 330, 2, '2xut', 'Bacterial oligopeptide-proton symporter ', '3.62', 'A in', 30.9, 1.4, 10, 0, -102.5, '', 1, 14, '', '', '0000-00-00'),
(1119, 17, 70, 8, '3k03', 'NaK potassium channel, different conformation', '1.62', 'A in', 26.7, 1.1, 0, 0, -87.8, '', 4, 12, '', '', '0000-00-00'),
(1120, 15, 260, 4, '2y02', 'Beta-1 adrenergic receptor, complex with agonist', '2.6', 'A out', 31.4, 1.3, 2, 0, -76.9, '', 1, 7, '', '', '0000-00-00'),
(1121, 15, 6, 4, '3oax', 'Rhodopsin, different conformation of loops', '2.6', 'A out', 30.9, 1.4, 11, 0, -73.6, '', 1, 7, '', '', '0000-00-00'),
(1122, 15, 14, 4, '3p0g', 'Beta 2-adrenergic receptor, complex with antibody', '3.5', 'A out', 30.1, 1.4, 9, 1, -62.9, '', 1, 7, '', '', '0000-00-00'),
(1123, 15, 6, 4, '3pqr', 'Metarhodopsin II, complex with peptide of Galpha subunit of transducin', '2.85', 'A out', 31.8, 1.1, 9, 1, -78.3, '', 1, 7, '', '', '0000-00-00'),
(1124, 15, 6, 4, '3pxo', 'Metarhodopsin II, without transducin peptide', '3.0', 'A out', 31.8, 1.2, 0, 0, -125.4, '', 2, 14, '', '', '0000-00-00'),
(1125, 15, 14, 4, '3qak', 'A2A adenosine receptor, complex with agonist', 'A out', '2.71', 30.2, 1.3, 8, 1, -68.1, '', 1, 7, '', '', '0000-00-00'),
(1126, 31, 57, 4, '2xzb', 'Sodium-potassium pump, gastric', '7.0', 'A in', 29.7, 1.2, 9, 0, -91.4, '', 2, 11, '', '', '0000-00-00'),
(1127, 31, 57, 4, '3n23', 'Sodium-potassium pump, different conformation', '4.6', 'A in', 29.9, 0.9, 6, 0, -96.0, '', 3, 12, '', '', '0000-00-00'),
(1131, 361, 14, 4, '3jw8', 'Monoglyceride lipase MGLL, open ligand-free conformation', '2.10', 'A in', 8.1, 1.3, 11, 9, -11.3, '', 1, 0, '', '', '0000-00-00'),
(1132, 361, 14, 4, '3pe6', 'Monoglyceride lipase MGLL, closed ligand-bound conformation', '1.35', 'A in', 0.9, 3.0, 54, 28, -2.7, '', 1, 0, '', '', '0000-00-00'),
(1133, 110, 14, 4, '3o8y', 'Arachidonate 5-lipoxygenase', '2.39', 'A in', 2.1, 1.0, 89, 4, -3.8, '', 1, 0, '', '', '0000-00-00'),
(1134, 63, 55, 14, '3l9b', 'C2 domain of otoferlin', '1.95', 'in', 2.4, 5.2, 16, 33, -3.4, '', 1, 0, '', 'This is C2 domain of a bitopic TM protein from ferlin family.', '0000-00-00'),
(1136, 4, 42, 7, '3pcq', 'Photosystem I, trimeric complex', '8.98', 'A in', 29.8, 0.8, 0, 0, -429.6, '', 27, 96, '', 'Subunits of the trimer were renamed sequentially in alphabet order.', '0000-00-00'),
(1137, 46, 9, 3, '3pik', 'Cation efflux system protein CusC', '2.3', 'A in', 24.3, 1.2, 1, 0, -33.8, '', 3, 12, '', '', '0000-00-00'),
(1138, 304, 9, 2, '3ob6', 'Arginine/agmatine transporter (AdiC), intermediate conformation', '3.0', 'A in', 29.8, 1.4, 3, 1, -158.7, '', 2, 24, '', '', '0000-00-00'),
(1139, 360, 262, 2, '3pjz', 'Potassium uptake protein TrkH', '3.51', 'A in', 29.7, 0.6, 1, 0, -164.0, '', 2, 20, '', '', '0000-00-00'),
(1140, 362, 143, 23, '2kv5', 'Fst toxin', 'NMR', 'A out', 26.0, 2.9, 35, 8, -18.9, '', 1, 1, '', '', '0000-00-00'),
(1141, 118, 9, 23, '2i88', 'Colicin-E1', '2.5', 'out', 1.1, 3.3, 58, 37, -1.7, '', 1, 0, '', '', '0000-00-00'),
(1142, 31, 331, 4, '1mhs', 'Plasma membrane ATPase', '8.0', 'A in', 29.5, 0.2, 7, 0, -109.6, '', 2, 20, '', '', '0000-00-00'),
(1143, 1, 332, 16, '1xrd', 'Light-harvesting complex LH1, alpha chain', 'NMR', 'A in', 30.3, 3.1, 30, 4, -30.5, '', 1, 1, '', '', '0000-00-00'),
(1144, 298, 269, 2, '2wit', 'Sodium-betaine symporter BetP, substrate-bound', '3.35', 'A in', 30.4, 1.2, 0, 0, -198.6, '', 3, 36, '', '', '0000-00-00'),
(1145, 298, 269, 2, '3p03', 'Sodium-betaine symporter BetP, alternative inward-facing open conformation', '3.35', 'A in', 29.8, 0.7, 1, 0, -160.9, '', 3, 36, '', 'One of TM helices is partially disordered and missing in two subunits.', '0000-00-00'),
(1147, 170, 333, 24, '2vt0', 'Glucosylceramidase', '2.15', 'out', 2.3, 1.0, 86, 5, -7.3, '', 1, 0, '', '', '0000-00-00'),
(1148, 178, 14, 4, '3hx3', 'Retinaldehyde-binding protein 1, closed state', '1.69', 'in', 1.2, 2.9, 77, 32, -4.8, '', 1, 0, '', '', '0000-00-00'),
(1149, 178, 14, 4, '3hy5', 'Retinaldehyde-binding protein 1, closed state, more complete structure', '3.04', 'in', 2.0, 3.9, 55, 17, -4.5, '', 1, 0, '', '', '0000-00-00'),
(1150, 256, 53, 5, '1ndb', 'Carnitine O-acetyltransferase', '1.6', 'in', 3.0, 0.9, 85, 6, -7.6, '', 1, 0, '', '', '0000-00-00'),
(1151, 256, 14, 5, '1nm8', 'Carnitine O-octanoyltransferase', '1.6', 'in', 1.7, 3.0, 67, 15, -5.3, '', 1, 0, '', '', '0000-00-00'),
(1152, 256, 14, 4, '2fy2', 'Choline O-acetyltransferase', '2.25', 'in', 1.5, 2.2, 87, 17, -5.2, '', 1, 0, '', '', '0000-00-00'),
(1153, 256, 55, 4, '1q6x', 'Choline O-acetyltransferase', '2.5', 'in', 3.6, 0.6, 75, 6, -8.5, '', 1, 0, '', '', '0000-00-00'),
(1154, 256, 55, 4, '1t1u', 'Choline O-acetyltransferase', '1.55', 'in', 2.1, 1.7, 73, 15, -6.8, '', 1, 0, '', '', '0000-00-00'),
(1155, 256, 53, 5, '2h3u', 'Carnitine O-acetyltransferase, complex with substrate', '1.0', 'in', 3.0, 1.0, 87, 3, -5.9, '', 1, 0, '', '', '0000-00-00'),
(1156, 154, 223, 23, '2gj0', 'Cycloviolacin-O14', 'NMR', 'out', 3.6, 1.5, 85, 16, -5.4, '', 1, 0, '', '', '0000-00-00'),
(1157, 154, 223, 23, '2kcg', 'Cycloviolacin-O2', 'NMR', 'out', 5.1, 2.9, 58, 36, -6.8, '', 1, 0, '', '', '0000-00-00'),
(1158, 154, 180, 23, '2jwm', 'Kalata-B7', 'NMR', 'out', 2.7, 2.2, 86, 28, -4.8, '', 1, 0, '', '', '0000-00-00'),
(1159, 192, 334, 8, '3hc7', 'Lysin B from mycobacteriophage', '2.0', 'out', 6.6, 2.0, 50, 12, -7.0, '', 1, 0, '', '', '0000-00-00'),
(1160, 192, 22, 23, '3aja', 'Mycobacterial lipase', '2.9', 'out', 6.0, 1.0, 28, 10, -6.7, '', 1, 0, '', '', '0000-00-00'),
(1161, 192, 335, 23, '3gbs', 'Cutinase 1', '1.75', 'out', 11.2, 0.5, 55, 5, -12.6, '', 1, 0, '', '', '0000-00-00'),
(1162, 192, 336, 23, '3dcn', 'Cutinase 1', '1.90', 'out', 5.7, 1.2, 44, 8, -10.1, '', 1, 0, '', '', '0000-00-00'),
(1163, 192, 337, 23, '2czq', 'Cutinase-like protein', '1.05', 'out', 4.9, 1.3, 54, 16, -9.0, '', 1, 0, '', '', '0000-00-00'),
(1164, 154, 50, 23, '2eri', 'Circulin B', 'NMR', 'out', 5.0, 1.0, 69, 20, -8.4, '', 1, 0, '', '', '0000-00-00'),
(1165, 154, 338, 23, '3e4h', 'Varv peptide F', '1.80', 'out', 4.2, 3.0, 87, 43, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1166, 154, 180, 23, '2kux', 'Kalata-B5', 'NMR', 'out', 4.1, 1.0, 61, 25, -6.6, '', 1, 0, '', '', '0000-00-00'),
(1167, 154, 223, 23, '2fqa', 'Violacin 1', 'NMR', 'out', 2.4, 3.4, 70, 46, -4.0, '', 1, 0, '', '', '0000-00-00'),
(1168, 154, 222, 23, '2kuk', 'Leaf cyclotide 2', 'NMR', 'out', 3.4, 1.2, 83, 20, -5.9, '', 1, 0, '', '', '0000-00-00'),
(1169, 154, 222, 23, '1za8', 'Leaf cyclotide 2', 'NMR', 'out', 4.9, 1.3, 48, 24, -8.5, '', 1, 0, '', '', '0000-00-00'),
(1170, 154, 338, 23, '1yp8', 'Tricyclon-A', 'NMR', 'out', 4.4, 1.7, 71, 19, -4.7, '', 1, 0, '', '', '0000-00-00'),
(1171, 154, 180, 23, '1wn8', 'Kalata-B3/B6 propeptide', 'NMR', 'out', 3.6, 1.2, 81, 22, -8.4, '', 1, 0, '', '', '0000-00-00'),
(1172, 154, 223, 23, '1wn4', 'Varv peptide A/Kalata-B1 propeptide', 'NMR', 'out', 6.4, 1.1, 81, 14, -7.2, '', 1, 0, '', '', '0000-00-00'),
(1173, 154, 223, 23, '2aks', 'Vodo peptide  N', 'model', 'out', 4.0, 1.4, 89, 22, -6.7, '', 1, 0, '', '', '0000-00-00'),
(1174, 365, 70, 8, '3qnq', 'Saccharide transporter component, EIIC (ChbC)', '3.30', 'A in', 29.6, 1.0, 1, 0, -140.6, '', 2, 20, '', '', '0000-00-00'),
(1177, 23, 218, 4, '3mra', 'Acetylcholine receptor subunit alpha, TMH 3', 'NMR', 'A out', 31.6, 3.3, 35, 9, -21.7, '', 1, 1, '', '', '0000-00-00'),
(1185, 372, 215, 26, '1djf', 'Human platelet factor 4-based peptide ', 'NMR', 'out', 1.9, 1.4, 87, 8, -4.9, '', 1, 0, '', '', '0000-00-00'),
(1186, 373, 39, 23, '1dtc', 'Delta-hemolysin', 'NMR', 'out', 3.2, 2.2, 87, 19, -8.5, '', 1, 0, '', '', '0000-00-00'),
(1187, 374, 339, 15, '1emz', 'Hepatitis C virus envelope glycoprotein E1', 'NMR', 'out', 6.2, 0.2, 86, 9, -8.5, '', 1, 0, '', '', '0000-00-00'),
(1188, 375, 239, 12, '1fw5', 'Non-structural polyprotein, membrane-bound domain', 'NMR', 'in', 7.9, 1.5, 73, 17, -10.2, '', 1, 0, '', '', '0000-00-00'),
(1189, 337, 25, 23, '1lyp', 'Antimicrobial protein CAP18, segment 135-166', 'NMR', 'out', 7.4, 1.0, 87, 9, -15.6, '', 1, 0, '', '', '0000-00-00'),
(1190, 376, 9, 2, '1o53', 'Membrane-bound helix of phosphotransferase IIA component ', 'NMR', 'in', 3.3, 1.3, 86, 15, -7.8, '', 1, 0, '', '', '0000-00-00'),
(1191, 377, 55, 10, '3hl4', 'Cytidylyltransferase', '2.20', 'in', 2.7, 4.0, 74, 8, -3.2, '', 2, 0, '', 'The dimer is asymmetric.', '0000-00-00'),
(1192, 377, 55, 10, '1peh', 'Cytidylyltransferase, first membrane-anchoring helix', 'NMR', 'in', 3.2, 0.6, 90, 2, -5.0, '', 1, 0, '', '', '0000-00-00'),
(1193, 377, 55, 10, '1pei', 'Cytidylyltransferase, second membrane-anchoring helix', 'NMR', 'in', 4.9, 1.0, 83, 11, -8.2, '', 1, 0, '', '', '0000-00-00'),
(1194, 378, 340, 23, '1t51', 'Cytotoxic linear peptide IsCT', 'NMR', 'out', 4.1, 0.6, 87, 11, -10.5, '', 1, 0, '', '', '0000-00-00'),
(1195, 376, 215, 26, '1vm2', 'Anticancer peptide designed based on the helix of phosphotransferase IIA', 'NMR', 'out', 7.0, 1.8, 78, 15, -12.0, '', 1, 0, '', '', '0000-00-00'),
(1196, 379, 193, 23, '1wfb', 'Antifreeze protein', '1.50', 'out', 2.8, 1.0, 88, 1, -10.1, '', 1, 0, '', '', '0000-00-00'),
(1197, 380, 215, 26, '1xkm', 'Distinctin', 'NMR', 'out', 3.9, 0.4, 87, 2, -4.6, '', 1, 0, '', '', '0000-00-00'),
(1198, 381, 341, 23, '1hvz', 'Theta-defensin 1 (RTD-1)', 'NMR', 'out', 0.8, 1.0, 89, 4, -2.9, '', 1, 0, '', '', '0000-00-00'),
(1199, 381, 341, 23, '2atg', 'Retrocyclin-2', 'NMR', 'out', 2.4, 0.6, 87, 9, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1200, 382, 342, 23, '1vm5', 'Aurein 1.2', 'NMR', 'out', 9.5, 1.8, 63, 14, -9.7, '', 1, 0, '', '', '0000-00-00'),
(1201, 382, 215, 26, '2f3a', 'Aurein 1.2 analogue', 'NMR', 'out', 83.0, 1.6, 88, 24, -11.7, '', 1, 0, '', '', '0000-00-00'),
(1202, 337, 57, 23, '2i1d', 'Prophenin-1', 'NMR', 'out', 4.8, 1.9, 70, 35, -5.9, '', 1, 0, '', '', '0000-00-00'),
(1203, 337, 215, 26, '2i1e', 'Prophenin-1 analogue', 'NMR', 'out', 5.2, 1.0, 53, 7, -7.5, '', 1, 0, '', '', '0000-00-00'),
(1204, 383, 215, 26, '2jq2', 'Anticoccidial peptide PW2', 'NMR', 'out', 6.2, 2.3, 67, 36, -4.5, '', 1, 0, '', '', '0000-00-00'),
(1205, 208, 343, 23, '2jr8', 'Moricin', 'NMR', 'out', 5.9, 1.6, 75, 3, -11.5, '', 1, 0, '', '', '0000-00-00'),
(1206, 83, 215, 26, '2k98', 'Magainin analogue, MSI-594', 'NMR', 'out', 3.2, 0.2, 86, 2, -8.9, '', 1, 0, '', '', '0000-00-00'),
(1207, 61, 14, 4, '2r7e', 'Coagulation factor VIII', '3.7', 'out', 4.5, 3.0, 39, 6, -11.5, '', 2, 0, '', '', '0000-00-00'),
(1208, 218, 55, 23, '3cmh', 'Endothelin-1', 'NMR', 'out', 6.3, 3.9, 72, 40, -4.8, '', 1, 0, '', '', '0000-00-00'),
(1209, 384, 344, 23, '8tfv', 'Thanatin', 'NMR', 'out', 3.7, 1.0, 81, 4, -5.3, '', 1, 0, '', '', '0000-00-00'),
(1210, 385, 215, 26, '1omq', 'Penetratin', 'NMR', 'out', 3.2, 1.0, 79, 7, -7.4, '', 1, 0, '', '', '0000-00-00'),
(1211, 184, 55, 4, '3biw', 'Neuroligin-1, complex with neurexin-1-beta', '3.5', 'out', 5.9, 1.0, 80, 3, -8.8, '', 2, 0, '', 'Bitopic, TMH 698-718.', '0000-00-00'),
(1212, 184, 53, 4, '3bl8', 'Neuroligin-2', '3.30', 'out', 1.7, 1.6, 32, 5, -4.1, '', 1, 0, '', 'Bitopic.', '0000-00-00'),
(1241, 39, 248, 3, '3qq2', 'Autotransporter BrkA', '3.0', 'A in', 24.6, 1.5, 4, 1, -44.1, '', 1, 12, '', '', '0000-00-00'),
(1214, 184, 53, 4, '3b3q', 'Neuroligin-1, complex with human neurexin-1-alpha', '2.40', 'A out', 1.8, 1.0, 81, 1, -3.6, '', 2, 0, '', 'Bitopic.', '0000-00-00'),
(1215, 189, 346, 23, '3g7n', 'Triacylglycerol lipase', '1.3', 'out', 3.8, 1.1, 81, 14, -9.0, '', 1, 0, '', '', '0000-00-00'),
(1216, 189, 347, 23, '3o0d', 'Lipase 2', '1.70', 'out', 6.8, 2.4, 79, 26, -9.4, '', 1, 0, '', '', '0000-00-00'),
(1217, 185, 21, 22, '1r88', 'MPT51/MPB51 antigen', '1.71', 'out', 1.8, 1.0, 28, 26, -3.9, '', 1, 0, '', '', '0000-00-00'),
(1218, 187, 14, 24, '3gro', 'Palmitoyl-protein thioesterase 1', '2.53', 'out', 3.6, 0.1, 55, 3, -6.8, '', 1, 0, '', '', '0000-00-00'),
(1219, 386, 164, 8, '3og9', 'Copper inducible hydrolase YahD', '1.88', 'in', 1.4, 1.1, 33, 10, -4.0, '', 1, 0, '', '', '0000-00-00'),
(1220, 387, 59, 1, '1jji', 'Carboxylesterase (EstA)', '2.2', 'in', 2.8, 1.0, 56, 22, -4.8, '', 1, 0, '', 'Localization and topology are unknown.', '0000-00-00'),
(1224, 386, 70, 8, '2h1i', 'Carboxylesterase', '2.8', 'in', 2.3, 1.8, 32, 31, -3.6, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1223, 387, 348, 8, '1lzk', 'Heroin esterase', '1.45', 'in', 1.5, 1.5, 69, 9, -4.0, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1225, 386, 301, 2, '1auo', 'Carboxylesterase 2', '1.8', 'in', 1.7, 3.0, 33, 21, -3.4, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1226, 184, 14, 4, '2xb6', 'Neuroligin-4, X-linked, complex with neurexin 1-beta', '2.60', 'out', 1.9, 3.0, 84, 11, -3.3, '', 2, 0, '', 'Bitopic proteins.', '0000-00-00'),
(1227, 386, 14, 4, '1fj2', 'Acyl-protein thioesterase 1', '1.50', 'in', 9.6, 2.0, 64, 14, -4.7, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1228, 386, 28, 2, '3cn9', 'Carboxylesterase', '2.09', 'in', 3.5, 2.1, 11, 32, -4.1, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1229, 386, 62, 2, '3doh', 'Thermostable Esterase', '2.60', 'in', 4.0, 2.0, 84, 13, -4.4, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1230, 387, 297, 10, '3ebl', 'Gibberellin receptor GID1', '1.9', 'in', 5.2, 1.5, 59, 14, -9.1, '', 1, 0, '', '', '0000-00-00'),
(1231, 387, 48, 8, '2hm7', 'Carboxylesterase', '2.0', 'in', 5.8, 1.7, 70, 5, -7.7, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1232, 387, 253, 10, '2zsh', 'Gibberellin receptor GID1A', '1.80', 'in', 2.6, 1.2, 89, 6, -5.0, '', 1, 0, '', '', '0000-00-00'),
(1233, 184, 39, 8, '3h04', 'Protein with unknown function', '1.90', 'in', 1.7, 2.8, 67, 23, -3.4, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1234, 387, 349, 8, '3qh4', 'Esterase LipW', '1.75', 'in', 2.4, 1.2, 76, 32, -5.0, '', 1, 0, '', 'Topology and intracellular localization are unknown.', '0000-00-00'),
(1235, 388, 53, 4, '2qmq', 'Protein NDRG2', '1.70', 'in', 8.3, 2.2, 43, 14, -9.6, '', 1, 0, '', '', '0000-00-00'),
(1236, 190, 350, 23, '2x5x', 'PHB depolymerase PhaZ7', '1.20', 'out', 4.1, 3.0, 54, 41, -5.6, '', 1, 0, '', '', '0000-00-00'),
(1237, 389, 351, 23, '3h2g', 'Esterase LipA', '1.86', 'out', 5.1, 1.7, 87, 8, -4.9, '', 1, 0, '', '', '0000-00-00'),
(1238, 187, 352, 2, '1tht', 'Acyl transferase LuxD', '2.1', 'in', 3.3, 1.3, 85, 4, -6.1, '', 1, 0, '', '', '0000-00-00'),
(1239, 388, 14, 4, '2xmr', 'Protein Ndr1', '2.0', 'in', 8.2, 2.6, 50, 10, -8.8, '', 1, 0, '', '', '0000-00-00'),
(1240, 389, 108, 23, '3guu', 'Lipase A, closed state', '2.1', 'out', 4.4, 1.0, 80, 2, -10.9, '', 1, 0, '', '', '0000-00-00'),
(1242, 190, 59, 23, '2zyr', 'Tentative lipase', '1.77', 'out', 3.0, 1.0, 57, 8, -7.5, '', 1, 0, '', '', '0000-00-00'),
(1243, 17, 70, 8, '3ouf', 'NaK potassium channel, different strain of Bacillus cereus', '1.55', 'A in', 27.9, 1.3, 0, 0, -91.0, '', 4, 12, '', '', '0000-00-00'),
(1244, 33, 90, 8, '2w8d', 'Glycerol phosphate lipoteichoic acid synthase 2', '2.35', 'out', 0.0, 6.0, 83, 58, -1.6, '', 1, 0, '', 'This is extracellular domain of transmembrane polytopic protein; a purely interfacial binding mode.', '0000-00-00'),
(1245, 33, 39, 8, '2w5q', 'Glycerol phosphate lipoteichoic acid synthase', '1.20', 'out', 0.4, 3.6, 82, 11, -2.5, '', 1, 0, '', 'This is extracellular domain of transmembrane polytopic protein.', '0000-00-00'),
(1246, 94, 67, 23, '2hil', 'Fimbrial protein, type IV pilin, assembly', '12.5', 'I in', 29.6, 3.0, 13, 1, -15.9, '', 18, 1, '', '', '0000-00-00'),
(1247, 94, 28, 23, '1oqw', 'Fimbrial protein, monomer', '2.00', 'A in', 29.8, 3.0, 31, 8, -28.9, '', 1, 1, '', '', '0000-00-00'),
(1248, 86, 57, 6, '1fjk', 'Phosholamban', 'NMR', 'A in', 30.1, 3.2, 38, 6, -28.3, '', 1, 1, '', '', '0000-00-00'),
(1249, 86, 25, 6, '1n7l', 'Phospholamban', 'NMR', 'A in', 29.8, 3.6, 34, 12, -32.3, '', 1, 1, '', '', '0000-00-00'),
(1251, 204, 14, 19, '3p0l', 'Steroidogenic acute regulatory protein, mitochondrial', '3.4', 'in', 3.0, 1.3, 76, 10, -4.7, '', 1, 0, '', '', '0000-00-00'),
(1252, 204, 14, 6, '3fo5', 'Acyl-coenzyme A thioesterase 11', '2.00', 'in', 2.3, 1.4, 57, 7, -3.9, '', 1, 0, '', '', '0000-00-00'),
(1253, 77, 14, 12, '2yw8', 'RUN and FYVE domain-containing protein 1', '3.0', 'in', 0.7, 3.4, 48, 38, -2.8, '', 1, 0, '', '', '0000-00-00'),
(1254, 117, 353, 4, '3kv0', 'Glycolipid transfer protein Het-c2', '1.9', 'in', 8.3, 1.3, 83, 5, -13.6, '', 1, 0, '', '', '0000-00-00'),
(1255, 146, 354, 7, '3npe', '9-cis-epoxycarotenoid dioxygenase 1, chloroplastic', '3.20', 'in', 6.0, 0.1, 30, 5, -11.1, '', 1, 0, '', '', '0000-00-00'),
(1256, 201, 59, 1, '3cnu', 'Uncharacterized protein', '1.90', 'in', 7.6, 1.7, 69, 20, -7.0, '', 1, 0, '', 'Intracellular localization and topology are unknown.', '0000-00-00'),
(1257, 201, 355, 4, '3bkr', 'Uncharacterized protein', '1.4', 'in', 0.4, 6.2, 50, 73, -1.2, '', 1, 0, '', 'Intracellular localization and topology are unknown.', '0000-00-00'),
(1258, 201, 355, 4, '2qzt', 'Sterol carrier protein 2-like 2', '1.70', 'in', 1.0, 2.0, 45, 12, -3.0, '', 1, 0, '', '', '0000-00-00'),
(1259, 201, 355, 4, '1pz4', 'Sterol carrier protein 2', '1.35', 'in', 0.8, 5.0, 37, 49, -1.3, '', 1, 0, '', '', '0000-00-00'),
(1260, 5, 304, 7, '3arc', 'Photosystem II', '1.90', 'A in', 31.8, 0.0, 0, 0, -406.5, '', 32, 70, '', '', '0000-00-00'),
(1261, 47, 46, 23, '3o44', 'Cytolysin', '2.88', 'A out', 24.6, 0.0, 0, 0, -33.1, '', 7, 14, '', '', '0000-00-00'),
(1262, 28, 9, 2, '3j01', 'Ribosome-SecYE complex', '7.10', 'in', 28.6, 0.0, 5, 0, -86.4, '', 2, 13, '', '', '0000-00-00'),
(1264, 65, 14, 4, '3rcp', 'PH domain of pleckstrin homology domain-containing family A member 3', '1.9', 'in ', 2.8, 1.5, 70, 9, -4.8, '', 1, 0, '', 'The protein was crystallized as interwinded dimer, but it works as a monomer.', '0000-00-00'),
(1265, 54, 14, 5, '3na0', 'Cholesterol side-chain cleavage enzyme, mitochondrial (P450 11A1)', '2.5', 'in', 2.2, 1.2, 37, 14, -5.0, '', 1, 0, '', '', '0000-00-00'),
(1266, 54, 14, 6, '3ibd', 'Cytochrome P450 2B6', '2.0', 'in', 4.7, 1.0, 57, 3, -10.8, '', 1, 0, '', '', '0000-00-00'),
(1267, 54, 14, 6, '3dax', 'Cholesterol 7-alpha-monooxygenase (P450 7A1)', '2.15', 'in', 3.7, 0.8, 84, 6, -4.6, '', 1, 0, '', '', '0000-00-00'),
(1268, 54, 6, 5, '3mzs', 'Cholesterol side-chain cleavage enzyme, mitochondrial (P450 11A1)', '2.5', 'in', 3.2, 0.3, 33, 1, -6.7, '', 1, 0, '', '', '0000-00-00'),
(1269, 54, 14, 6, '3pm0', 'Cytochrome P450 1B1', '2.70', 'in', 3.8, 0.7, 79, 1, -7.0, '', 1, 0, '', '', '0000-00-00'),
(1270, 54, 14, 6, '2p85', 'Cytochrome P450 2A13', '2.35', 'in', 4.9, 0.4, 47, 2, -10.0, '', 1, 0, '', '', '0000-00-00'),
(1271, 113, 356, 23, '2not', 'Phospholipase A2', '3.0', 'out', 2.6, 1.5, 73, 8, -3.9, '', 1, 0, '', '', '0000-00-00'),
(1272, 113, 102, 23, '1bun', 'Phospholipase A2, beta bungarotoxin A1 chain, complex with bungarotoxin', '2.45', 'out', 1.7, 0.9, 79, 3, -3.8, '', 2, 0, '', '', '0000-00-00'),
(1273, 113, 75, 23, '1ppa', 'Phospholipase A2 homolog', '2.0', 'out', 1.2, 0.9, 85, 8, -4.5, '', 1, 0, '', '', '0000-00-00'),
(1274, 113, 226, 23, '1yxh', 'Phospholipase A2 isoform 4', '1.86', 'out', 1.7, 0.5, 81, 2, -5.2, '', 1, 0, '', '', '0000-00-00'),
(1275, 326, 278, 2, '3q7k', 'Formate transporter', '2.80', 'A in', 28.6, 0.0, 0, 0, -148.8, '', 5, 30, '', '', '0000-00-00'),
(1276, 393, 58, 3, '2xci', '3-Deoxy-D-manno-octulosonic-acid transferase (kdotransferase)', '2.0', 'out', 7.9, 0.0, 50, 4, -15.3, '', 1, 0, '', '', '0000-00-00'),
(1277, 54, 25, 6, '3r1a', 'Cytochrome P450 2B4, open state 3', '3.5', 'in', 5.0, 0.0, 54, 1, -12.8, '', 1, 0, '', '', '0000-00-00'),
(1278, 54, 25, 6, '3r1b', 'Cytochrome P450 2B4, closed state, different conformation', '3.0', 'in', 5.7, 0.0, 43, 5, -9.8, '', 1, 0, '', '', '0000-00-00'),
(1281, 394, 44, 2, '3aqp', 'SecDF protein-export membrane protein', '3.3', 'in', 29.8, 0.9, 5, 1, -93.8, '', 1, 12, '', '', '0000-00-00'),
(1282, 287, 14, 4, '2l9u', 'Receptor tyrosine-protein kinase erbB-3', 'NMR', 'A in', 33.8, 2.4, 16, 5, -44.6, '', 2, 2, '', '', '0000-00-00'),
(1283, 15, 14, 4, '2ydv', 'Adenosine receptor A2a', '2.6', 'A out', 31.0, 1.3, 10, 0, -61.4, '', 1, 7, '', '', '0000-00-00'),
(1284, 276, 9, 2, '3puz', 'Maltose transporter MalFGK, a pre-translocation state', '2.9', 'F in', 29.0, 0.8, 7, 0, -107.2, '', 2, 14, '', '', '0000-00-00'),
(1285, 276, 9, 2, '3puy', 'Maltose transporter MalFGK, outward conformation', '3.1', 'F in', 29.4, 0.1, 4, 0, -100.8, '', 2, 14, '', '', '0000-00-00'),
(1286, 25, 9, 2, '3noc', 'Multidrug efflux transporter AcrB, complex with ankyrin repeat', '2.7', 'A in', 28.8, 0.9, 1, 0, -183.9, '', 3, 36, '', '', '0000-00-00'),
(1287, 126, 36, 9, '1moz', 'ADP-ribosylation factor-like protein 1', '3.17', 'in', 0.7, 1.1, 90, 6, -4.3, '', 2, 0, '', '', '0000-00-00'),
(1288, 395, 330, 3, '3pmq', 'Decaheme cytochrome c MtrF', '3.2', 'out', 3.9, 0.9, 86, 2, -6.2, '', 1, 0, '', '', '0000-00-00'),
(1289, 23, 243, 4, '3rhw', 'Glutamate-gated chloride channel GluCl alpha', '3.26', 'out', 30.2, 0.7, 0, 0, -107.9, '', 5, 20, '', '', '0000-00-00'),
(1290, 289, 9, 3, '3ohn', 'Outer membrane usher protein FimD', '3.01', 'A in', 21.2, 1.1, 5, 0, -45.4, '', 1, 24, '', '', '0000-00-00'),
(1291, 289, 9, 3, '3rfz', 'Outer membrane usher protein FimD, complex with FimC-FimH', '2.80', 'B in', 23.8, 0.8, 5, 0, -65.1, '', 3, 24, '', '', '0000-00-00'),
(1292, 15, 260, 4, '2ycw', 'Beta-1 adrenergic receptor, complex with antagonist', '3.0', 'A out', 32.2, 1.3, 2, 0, -77.8, '', 1, 7, '', '', '0000-00-00'),
(1293, 15, 260, 4, '2ycz', 'Beta-1 adrenergic receptor, complex with antagonist, different conformation', '3.65', 'A out', 31.8, 1.5, 1, 1, -73.8, '', 1, 7, '', '', '0000-00-00'),
(1294, 104, 359, 23, '3rfi', 'Saposin-like domain of plant aspartic protease', '1.90', 'out', 5.6, 3.2, 66, 3, -9.1, '', 1, 0, '', '', '0000-00-00'),
(1295, 104, 14, 24, '2dob', 'Saposin A', '2.00', 'out', 2.0, 2.5, 70, 29, -4.2, '', 1, 0, '', '', '0000-00-00'),
(1296, 81, 9, 2, '2v8n', 'Lactose permease, a slightly different conformation', '3.60', 'A in', 31.8, 0.8, 5, 0, -86.4, '', 1, 12, '', '', '0000-00-00'),
(1297, 396, 358, 2, '3rce', 'Ologosaccharyltransferase PglB', '3.40', 'A in', 28.8, 0.9, 8, 0, -89.6, '', 1, 13, '', '', '0000-00-00'),
(1298, 15, 14, 4, '3rze', 'Histamine H1 receptor', '3.10', 'A out', 32.0, 1.4, 1, 1, -72.4, '', 1, 7, '', '', '0000-00-00'),
(1339, 143, 11, 4, '2k62', 'Fatty acid-binding protein', 'NMR', 'in', 0.0, 2.9, 82, 13, -2.0, '', 1, 0, '', '', '0000-00-00'),
(1340, 143, 363, 23, '2a0a', 'Der f 13 allergen', 'NMR', 'out', 3.1, 1.3, 50, 6, -3.5, '', 1, 0, '', '', '0000-00-00'),
(1341, 66, 6, 23, '1bj7', 'Allergen Bos d 2', '1.8', 'out', 3.1, 1.3, 50, 6, -3.5, '', 1, 0, '', '', '0000-00-00'),
(1342, 66, 362, 23, '2kt4', 'Extracellular fatty acid-binding protein', 'NMR', 'out', 3.9, 2.9, 61, 8, -3.4, '', 1, 0, '', '', '0000-00-00'),
(1344, 143, 361, 4, '2ftb', 'Fatty acid-binding protein 2', '2.0', 'in', 0.6, 2.0, 77, 20, -1.7, '', 1, 0, '', '', '0000-00-00'),
(1345, 63, 53, 4, '3n5a', 'Synaptotagmin-7', '1.44', 'in', 2.2, 2.3, 30, 12, -4.1, '', 1, 0, '', 'Bitopic; TMH 17-37', '0000-00-00'),
(1346, 63, 53, 4, '2k3h', 'Rabphilin-3A', 'NMR', 'in', 1.7, 2.1, 78, 16, -4.1, '', 1, 0, '', '', '0000-00-00'),
(1347, 74, 55, 12, '3hpc', 'Sorting nexin-5', '1.47', 'in', 0.0, 2.1, 90, 8, -2.4, '', 1, 0, '', '', '0000-00-00'),
(1348, 74, 14, 12, '2v14', 'Sorting nexin-23 (Kinesin-like protein KIF16B)', '2.2', 'in', 3.3, 3.0, 72, 14, -5.4, '', 1, 0, '', '', '0000-00-00'),
(1349, 74, 14, 4, '3p0c', 'Nischarin', '2.27', 'in', 4.1, 0.5, 82, 13, -7.0, '', 1, 0, '', '', '0000-00-00'),
(1350, 74, 36, 4, '2v6v', 'Bud emergence protein 1', '1.50', 'in', 2.1, 1.2, 75, 6, -5.1, '', 1, 0, '', '', '0000-00-00'),
(1352, 65, 53, 4, '1u27', 'Cytohesin-2', '2.3', 'in', 0.5, 2.4, 53, 9, -2.4, '', 1, 0, '', '', '0000-00-00'),
(1353, 65, 14, 4, '1v88', 'Oxysterol-binding protein-related protein 8', 'NMR', 'in', 1.7, 1.2, 78, 4, -4.6, '', 1, 0, '', '', '0000-00-00'),
(1354, 65, 53, 4, '1wgq', 'FYVE, RhoGEF and PH domain-containing protein 6', 'NMR', 'in', 2.5, 1.8, 68, 17, -3.2, '', 1, 0, '', '', '0000-00-00'),
(1355, 65, 14, 4, '2d9y', 'Pleckstrin homology domain-containing family A member 6 (PLEKHA6)', 'NMR', 'in', 1.0, 0.3, 67, 1, -6.2, '', 1, 0, '', '', '0000-00-00'),
(1356, 65, 14, 4, '2da0', 'Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1', 'NMR', 'in', 1.7, 2.5, 64, 20, -2.5, '', 1, 0, '', '', '0000-00-00'),
(1357, 65, 53, 4, '2dhi', 'Pleckstrin homology domain-containing family B member 2', 'NMR', 'in', 0.6, 1.5, 86, 14, -2.8, '', 1, 0, '', '', '0000-00-00'),
(1358, 65, 14, 4, '2dkp', 'Pleckstrin homology domain-containing family A member 5 (PLEKHA5)', 'NMR', 'in', 3.0, 0.9, 64, 6, -3.9, '', 1, 0, '', '', '0000-00-00'),
(1359, 65, 14, 4, '2dx1', 'Rho guanine nucleotide exchange factor 4', '2.36', 'in', 2.2, 2.2, 80, 10, -3.6, '', 1, 0, '', '', '0000-00-00'),
(1360, 65, 14, 4, '2x18', 'RAC-gamma serine/threonine-protein kinase', '1.46', 'in', 1.5, 1.1, 53, 4, -3.8, '', 1, 0, '', '', '0000-00-00'),
(1361, 65, 36, 4, '3nsu', 'Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1', '2.00', 'in', 0.8, 1.5, 57, 12, -4.0, '', 1, 0, '', '', '0000-00-00'),
(1362, 65, 14, 4, '3pp2', 'Rho GTPase-activating protein 27', '1.42', 'in', 2.5, 2.2, 72, 14, -3.4, '', 1, 0, '', '', '0000-00-00'),
(1363, 65, 14, 4, '3bji', 'Proto-oncogene vav, complex with Ras-related C3 botulinum toxin substrate 1', '2.6', 'in', 2.5, 2.2, 72, 14, -3.4, '', 2, 0, '', '', '0000-00-00'),
(1364, 400, 14, 23, '2l86', 'Islet amyloid polypeptide, fragment 34-70', 'NMR', 'out', 6.2, 0.8, 88, 7, -9.6, '', 1, 0, '', '', '0000-00-00'),
(1365, 400, 14, 23, '2kb8', 'Islet amyloid polypeptide, fragment 34-70', 'NMR', 'out', 3.9, 4.2, 90, 1, -10.2, '', 1, 0, '', '', '0000-00-00'),
(1366, 17, 365, 2, '3rvy', 'Voltage-gated sodium channel', '2.7', 'A in', 29.6, 0.4, 0, 0, -216.9, '', 4, 24, '', '', '0000-00-00'),
(1367, 43, 278, 3, '3nsg', 'Porin OmpF', '2.79', 'A in', 23.6, 0.8, 0, 0, -123.4, '', 3, 48, '', '', '0000-00-00'),
(1368, 401, 14, 5, '2yl4', 'ATP-binding cassete sub-family B member 10 (ABCB10)', '2.85', 'A in', 30.8, 1.0, 1, 1, -75.4, '', 2, 12, '', '', '0000-00-00');

-- --------------------------------------------------------

--
-- Table structure for table `relatedproteins`
--

CREATE TABLE `relatedproteins` (
  `id` int(4) NOT NULL auto_increment,
  `protein_id` int(4) NOT NULL default '0',
  `protein_pdbid` char(5) NOT NULL default '',
  `pdbid` char(5) NOT NULL default '',
  PRIMARY KEY  (`id`),
  KEY `protein_id` (`protein_id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=4527 ;

--
-- Dumping data for table `relatedproteins`
--

INSERT INTO `relatedproteins` (`id`, `protein_id`, `protein_pdbid`, `pdbid`) VALUES
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-- --------------------------------------------------------

--
-- Table structure for table `species`
--

CREATE TABLE `species` (
  `id` smallint(4) NOT NULL auto_increment,
  `name` varchar(80) NOT NULL,
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=367 ;

--
-- Dumping data for table `species`
--

INSERT INTO `species` (`id`, `name`) VALUES
(1, 'Aeropyrum pernix'),
(2, 'Anabaena sp.'),
(3, 'Bacillus brevis'),
(5, 'Burkholderia pseudomallei'),
(6, 'Bos taurus'),
(7, 'Chlamydomonas reinhardtii'),
(8, 'Comamonas acidovorans'),
(9, 'Escherichia coli'),
(10, 'Enterococcus hirae'),
(11, 'Gallus gallus'),
(12, 'Halobacterium salinarum'),
(13, 'Halobacterium sp.'),
(14, 'Homo sapiens'),
(15, 'Ilyobacter tartaricus'),
(16, 'Klebsiella pneumoniae'),
(17, 'Magnetospirillum magnetotacticum'),
(18, 'Mastigocladus laminosus'),
(19, 'Methylococcus capsulatus'),
(20, 'Methanococcus jannaschii'),
(21, 'Mycobacterium tuberculosis'),
(22, 'Mycobacterium smegmatis'),
(23, 'Natronomonas pharaonis'),
(24, 'Neisseria meningitidis'),
(25, 'Oryctolagus cuniculus'),
(26, 'Ovis aries'),
(27, 'Paracoccus denitrificans'),
(28, 'Pseudomonas aeruginosa'),
(29, 'Pyrococcus horikoshii'),
(30, 'Rhodobacter capsulatus'),
(31, 'Rhodobacter sphaeroides'),
(32, 'Rhodopseudomonas acidophila'),
(33, 'Rhodopseudomonas blastica'),
(34, 'Rhodopseudomonas viridis'),
(35, 'Rhodospirillum molischianum'),
(36, 'Saccharomyces cerevisiae'),
(38, 'Spinacia oleracea'),
(39, 'Staphylococcus aureus'),
(40, 'Streptomyces coelicolor'),
(41, 'Streptomyces lividans'),
(42, 'Thermosynechococcus elongatus'),
(43, 'Thermochromatium tepidum'),
(44, 'Thermus thermophilus'),
(45, 'Torpedo marmorata'),
(46, 'Vibrio cholerae'),
(47, 'Wolinella succinogenes'),
(48, 'Alicyclobacillus acidocaldarius'),
(49, 'Centruroides sculpturatus ewing'),
(50, 'Chassalia parviflora'),
(51, 'Drosophila melanogaster'),
(52, 'Influenza virus'),
(53, 'Mus musculus'),
(54, 'Naja atra'),
(55, 'Rattus norvegicus'),
(56, 'Xenopus laevis'),
(57, 'Sus scrofa'),
(58, 'Aquifex aeolicus'),
(59, 'Archaeoglobus fulgidus'),
(60, 'Methanobacterium thermoautotrophicum'),
(61, 'Bacillus ps3'),
(62, 'Thermotoga maritima'),
(63, 'Bacteriophage fd'),
(64, 'Bacteriophage If1'),
(65, 'Bacteriophage Pf3'),
(66, 'Bacteriophage PH75'),
(67, 'Neisseria gonorrhoeae'),
(68, 'Trichoderma viride'),
(69, 'Apiocrea chrysosperma'),
(70, 'Bacillus cereus'),
(71, 'Acremonium tubakii'),
(72, 'Actinia equina'),
(73, 'Actinoplanes liguriae'),
(74, 'Agelenopsis aperta'),
(75, 'Agkistridon piscivorus'),
(76, 'Agkistrodon acutus'),
(77, 'Agkistrodon contortrix laticinctus'),
(78, 'Agkistrodon halys pallas'),
(79, 'Agriosphodrus dohrni'),
(80, 'Alcaligenes xylosoxidans'),
(81, 'Anemonia sulcata'),
(82, 'Anthopleura xanthogrammica'),
(83, 'Apis mellifera'),
(84, 'Aptenodytes patagonicus'),
(85, 'Archaeoprepona demophon'),
(86, 'Arthrospira maxima'),
(87, 'Atrax robustus'),
(88, 'Bacillus sp.'),
(89, 'Bacillus stearothermophilus'),
(90, 'Bacillus subtilis'),
(91, 'Bacillus thuringiensis'),
(92, 'Bacteriophage prd1'),
(93, 'Bombyx mori'),
(94, 'Borrelia burgdorferi'),
(95, 'Bothrops godmani'),
(96, 'Bothrops jararacussu'),
(97, 'Bothrops moojeni'),
(98, 'Bothrops pirajai'),
(99, 'Bovine respiratory syncytial virus'),
(100, 'Brevibacterium sterolicum'),
(101, 'Bungarus caeruleus'),
(102, 'Bungarus multicinctus'),
(103, 'Burkholderia cepacia'),
(104, 'Buthus eupeus'),
(105, 'Buthus martensii'),
(106, 'Buthus tamulus'),
(107, 'Campylobacter jejuni'),
(108, 'Candida antarctica'),
(109, 'Candida cylindracea'),
(110, 'Candida rugosa'),
(111, 'Canis lupus familiaris'),
(112, 'Capsicum annuum'),
(113, 'Cavia porcellus'),
(114, 'Centruroides noxius hoffmann'),
(116, 'Cladophora glomerata'),
(117, 'Clostridium absonum'),
(366, 'Methanococcus maripaludis'),
(119, 'Clostridium perfringens'),
(120, 'Conus aulicus'),
(121, 'Conus ermineus'),
(122, 'Conus magus'),
(123, 'Conus marmoreus'),
(124, 'Conus pennaceus'),
(125, 'Conus striatus'),
(126, 'Conus textile'),
(128, 'Crambe abyssinica'),
(129, 'Crotalus atrox'),
(130, 'Daboia russelli pulchella'),
(131, 'Danio rerio'),
(132, 'Dendroaspis jamesoni kaimosae'),
(133, 'Dengue virus'),
(134, 'Dictyostelium discoideum'),
(227, 'Synechococcus sp.'),
(136, 'Echinococcus granulosus'),
(137, 'Echis carinatus'),
(138, 'Ectatomma tuberculatum'),
(139, 'Ectothiorhodospira vacuolata'),
(140, 'Eledone moschata'),
(141, 'Emercelliopsis sp.'),
(142, 'Emericellopsis salmosynnemata'),
(143, 'Enterococcus faecalis'),
(144, 'Equus caballus'),
(145, 'Erwinia chrysanthemi'),
(146, 'Felis catus'),
(147, 'Fusarium solani'),
(148, 'Glycine max'),
(149, 'Gossypium hirsutum'),
(294, 'Arthrospira platensis'),
(151, 'Gymnema sylvestre'),
(152, 'Hadronyche infensa'),
(153, 'Hadronyche versuta'),
(154, 'Helianthus annuus'),
(155, 'Helicobacter pylori'),
(156, 'Helleborus purpurascens'),
(157, 'Hordeum vulgare'),
(158, 'Human hepatitis C virus'),
(159, 'Human immunodeficiency virus type 1'),
(160, 'Humicola lanuginosa'),
(161, 'Hydra vulgaris'),
(162, 'Kassina senegalensis'),
(163, 'Lactobacillus sake'),
(164, 'Lactococcus lactis'),
(165, 'Leiurus quinquestriatus hebraeus'),
(166, 'Leuconostoc gelidum'),
(167, 'Listeria ivanovii'),
(168, 'Listeria monocytogenes'),
(169, 'Macaca fascicularis'),
(170, 'Marsupenaeus japonicus'),
(171, 'Methylobacterium extorquens'),
(172, 'Methylomonas sp.'),
(173, 'Micropechis ikaheka'),
(174, 'Naja mossambica mossambica'),
(175, 'Naja naja oxiana'),
(176, 'Naja nigricollis'),
(177, 'Nicotiana tabacum'),
(178, 'Nitrosomonas europaea'),
(179, 'Notechis scutatus scutatus'),
(180, 'Oldenlandia affinis'),
(181, 'Ophiophagus hannah'),
(182, 'Palicourea condensata'),
(183, 'Paraphysa scrofa'),
(184, 'Paraponera clavata'),
(186, 'Phaseolus vulgaris'),
(187, 'Pisum sativum'),
(188, 'Plasmodium vivax'),
(189, 'Plexaura homomalla'),
(190, 'Prochlorothrix hollandica'),
(191, 'Pseudomonas glumae'),
(192, 'Pseudomonas stutzeri'),
(193, 'Pseudopleuronectes americanus'),
(194, 'Pseudoplusia includens'),
(195, 'Raphanus sativus'),
(196, 'Rattus rattus'),
(197, 'Rhizomucor miehei'),
(198, 'Rhizopus niveus'),
(199, 'Sarcophaga peregrina'),
(200, 'Schistocerca gregaria'),
(201, 'Schistosoma mansoni'),
(292, 'Chilobrachys guangxiensis (Chinese earth tiger tarantula)'),
(203, 'Shewanella putrefaciens'),
(204, 'Simian virus 5'),
(205, 'Solanum cardiophyllum'),
(206, 'Spodoptera litura'),
(207, 'Stichodactyla helianthus'),
(208, 'Stoichactis helianthus'),
(209, 'Streptomyces exfoliatus'),
(210, 'Streptomyces pseudogriseolus'),
(211, 'Streptomyces roseosporus'),
(212, 'Streptomyces sp.'),
(213, 'Streptomyces violaceoruber'),
(214, 'Synechocystis sp.'),
(215, 'Designed proteins'),
(216, 'Paracoccus versutus'),
(217, 'Tityus serrulatus'),
(218, 'Torpedo californica'),
(219, 'Hypocrea jecorina'),
(220, 'Triticum aestivum'),
(221, 'Trypanosoma brucei'),
(222, 'Viola hederacea'),
(223, 'Viola odorata'),
(224, 'Vipera ammodytes meridionalis'),
(225, 'Vipera russelli'),
(226, 'Naja sagittifera'),
(228, 'Tolypocladium inflatum'),
(229, 'Mycobacterium bovis'),
(230, 'Geotrichum candidum'),
(231, 'Naja mossambica pallida'),
(232, 'Haemophilus influenzae'),
(233, 'Naja naja siamensis'),
(234, 'Viscum album'),
(239, 'Semiliki forest virus'),
(240, 'Tick-borne encephalitis virus'),
(241, 'Vespa xanthoptera'),
(242, 'Bovine viral diarrhea virus'),
(243, 'Caenorhabditis elegans'),
(244, 'Loxosceles laeta'),
(245, 'Leishmania major'),
(246, 'Streptoverticillium griseoverticillatum'),
(247, 'Desulfovibrio vulgaris'),
(248, 'Bordetella pertussis'),
(249, 'Geobacillus zalihae'),
(250, 'Serratia marcescens'),
(251, 'Pseudomonas mendocina'),
(252, 'Vipera nikolskii'),
(253, 'Arabidopsis thaliana'),
(254, 'Rhizobium loti'),
(255, 'Todarodes pacificus'),
(256, 'Plasmodium falciparum'),
(257, 'Ralstonia pickettii'),
(258, 'Pseudomonas putida'),
(259, 'Methanosarcina acetivorans'),
(260, 'Meleagris gallopavo'),
(261, 'Methylosinus trichosporium'),
(262, 'Vibrio parahaemolyticus'),
(263, 'Salinibacter ruber'),
(264, 'Parthenium argentatum'),
(265, 'Photbacterium lipolyticum'),
(266, 'Pseudomonas sp. MIS 38'),
(267, 'Mycobacterium liquefaciens'),
(268, 'Gloeobacter violaceus'),
(269, 'Corinebacterium glutamicum'),
(270, 'Nostoc sp.'),
(271, 'Burkholderia xenovorans'),
(272, 'Spodoptera frugiperda'),
(273, 'Shewanella loihica'),
(274, 'Squalus acanthias'),
(275, 'Squalus acanthias'),
(277, 'Pichia pastoris'),
(278, 'Salmonella enterica'),
(279, 'Shigella  dysenteriae'),
(280, 'Xanthomonas campestris'),
(281, 'Vespula lewisii'),
(282, 'Lactobacillus plantarum'),
(283, 'Clostridium novyi'),
(284, 'Clostridium difficile'),
(285, 'Clostridium sordellii'),
(286, 'Human respiratory syncytial virus'),
(287, 'Arenicola marina'),
(288, 'Mesobuthus martensii (Manchurian scorpion)'),
(289, 'Psalmopoeus cambridgei (Trinidad chevron tarantula)'),
(290, 'Anthopleura elegantissima (Sea anemone)'),
(291, 'Haplopelma schmidti (Chinese bird spider)'),
(293, 'Grammostola rosea (Chilean rose tarantula)'),
(295, 'Bothrops neuwiedi pauloensis'),
(296, 'Geobacillus thermocatenulatus'),
(297, 'Oryza sativa (Rice)'),
(298, 'Vipera ammodytes ammodytes'),
(299, 'Trypanosoma cruzi'),
(300, 'Enterobacteria phage p21'),
(301, 'Pseudomonas fluorescens'),
(302, 'Leishmania infantum'),
(303, 'Nostoc punctiforme'),
(304, 'Thermosynechococcus vulcanus'),
(305, 'Agrobacterium tumefaciens'),
(306, 'Staphylococcus epidermidis'),
(307, 'Pardachirus marmoratus'),
(308, 'Carnobacterium maltaromaticum'),
(309, 'Legionella pneumophila'),
(310, 'Yersinia pestis'),
(311, 'Morganella morganii'),
(312, 'Bacillus pseudofirmus'),
(313, 'Morone saxatilis'),
(314, 'Phyllomedusa distincta'),
(315, 'Proteus mirabilis'),
(316, 'Pyrococcus furiosus'),
(317, 'Cyanidoschyzon merolae'),
(318, 'Bacillus anthracis'),
(319, 'Streptococcus intermedius'),
(320, 'Daboia russellii siamensis'),
(321, 'Crotalus durissus terrificus'),
(323, 'Bothrops asper'),
(324, 'Atropoides nummifer'),
(325, 'Zhaoermia manqshanensis'),
(326, 'Naja naja'),
(327, 'Bacteriophage Pf1'),
(328, 'Bacteriophage Xf'),
(329, 'Bacteriophage IKe'),
(330, 'Shewanella oneidensis'),
(331, 'Neurospora crassa'),
(332, 'Rhodospirillum rubrum'),
(333, 'Pan troglodytes'),
(334, 'Mycobacterium phage D29'),
(335, 'Aspergillus oryzae'),
(336, 'Colletotrichum gloeosporioides'),
(337, 'Cryptococcus sp.'),
(338, 'Viola arvensis'),
(339, 'Hepatitis C virus'),
(340, 'Opisthacanthus madagascariensis'),
(341, 'Macaca mulatta'),
(342, 'Litoria aurea'),
(343, 'Manduca sexta'),
(344, 'Podisus maculiventris'),
(346, 'Penicillium expansum'),
(347, 'Yarrowia lipolytica'),
(348, 'Rhodococcus sp.'),
(349, 'Mycobacterium marinum'),
(350, 'Pseudomonas lemoignei'),
(351, 'Xanthomonas oryzae'),
(352, 'Vibrio harveyi'),
(353, 'Podospora anserina'),
(354, 'Zea mays'),
(355, 'Aedes aegypti (Yellowfever mosquito)'),
(356, 'Notechis scutatus scutatus (Mainland tiger snake)'),
(365, 'Arcobacter butzleri'),
(358, 'Campylobacter lari'),
(359, 'Solanum tuberosum'),
(360, 'Acetabularia acetabulum'),
(361, 'Ambystoma mexicanum (Axolotl)'),
(362, 'Coturnix coturnix japonica (Japanese quail)'),
(363, 'Dermatophagoides farinae (American house dust mite)'),
(364, 'Locusta migratoria (Migratory locust)');

-- --------------------------------------------------------

--
-- Table structure for table `subunits`
--

CREATE TABLE `subunits` (
  `id` int(4) NOT NULL auto_increment,
  `protein_id` varchar(4) NOT NULL default '',
  `pdbid` varchar(5) NOT NULL default '',
  `letter` char(2) NOT NULL default '',
  `tilt` int(3) NOT NULL default '0',
  `segment` text NOT NULL,
  PRIMARY KEY  (`id`),
  KEY `protein_id` (`protein_id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=1483 ;

--
-- Dumping data for table `subunits`
--

INSERT INTO `subunits` (`id`, `protein_id`, `pdbid`, `letter`, `tilt`, `segment`) VALUES
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(9, '93', '1afo', 'B', 20, '1(72-94)'),
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(13, '68', '1c17', 'B', 4, '1(8-32),2(53-75)'),
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(16, '68', '1c17', 'E', 8, '1(7-31),2(55-78)'),
(17, '68', '1c17', 'F', 8, '1(7-31),2(55-78)'),
(18, '68', '1c17', 'G', 8, '1(7-31),2(55-78)'),
(19, '68', '1c17', 'H', 7, '1(8-31),2(53-77)'),
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(21, '68', '1c17', 'J', 5, '1(8-32),2(52-75)'),
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(23, '68', '1c17', 'L', 4, '1(8-32),2(51-76)'),
(24, '68', '1c17', 'M', 10, '1(101-124),2(142-166),3(201-223),4(241-262)'),
(25, '77', '1e12', 'A', 13, '1(27-50),2(63-82),3(106-123),4(134-153),5(159-180),6(199-221),7(227-250)'),
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(32, '53', '1ehk', 'B', 9, '1(15-37)'),
(33, '53', '1ehk', 'C', 9, '1(8-29)'),
(34, '24', '1ek9', 'A', 51, '1(40-50),2(65-77),3(246-256),4(282-290)'),
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(36, '24', '1ek9', 'B', 51, '1(40-50),2(65-77),3(246-256),4(282-290)'),
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(39, '54', '1fft', 'B', 16, '1(45-65),2(89-109)'),
(40, '54', '1fft', 'C', 20, '1(25-45),2(67-85),3(96-116),4(141-165),5(176-197)'),
(41, '94', '1gzm', 'A', 11, '1(35-63),2(74-99),3(109-133),4(153-172),5(202-224),6(253-276),7(286-308)'),
(42, '76', '1h2s', 'A', 8, '1(3-24),2(38-57),3(70-87),4(98-117),5(122-141),6(163-180),7(190-211)'),
(43, '76', '1h2s', 'B', 3, '1(24-41),2(60-81)'),
(44, '76', '1h2s', 'C', 3, '1(24-41),2(60-81)'),
(45, '76', '1h2s', 'D', 8, '1(3-24),2(38-57),3(70-87),4(98-117),5(122-141),6(163-180),7(190-211)'),
(46, '169', '1h68', 'A', 14, '1(3-24),2(37-56),3(70-87),4(98-117),5(121-141),6(165-180),7(190-211)'),
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(48, '171', '1h6i', 'B', 8, '1(11-32),2(50-68),3(77-87),4(92-113),5(135-156),6(168-186),7(193-202),8(210-231)'),
(49, '171', '1h6i', 'C', 8, '1(11-32),2(50-68),3(77-87),4(92-113),5(135-156),6(168-186),7(193-202),8(210-231)'),
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(51, '194', '1hgz', 'A', 13, '1(13-35)'),
(52, '194', '1hgz', 'B', 18, '1(16-37)'),
(53, '194', '1hgz', 'C', 27, '1(16-37)'),
(54, '194', '1hgz', 'D', 29, '1(16-38)'),
(55, '194', '1hgz', 'E', 22, '1(17-41)'),
(56, '194', '1hgz', 'F', 13, '1(22-45)'),
(57, '194', '1hgz', 'G', 17, '1(27-45)'),
(58, '194', '1hgz', 'H', 27, '1(28-45)'),
(59, '194', '1hgz', 'I', 34, '1(27-45)'),
(60, '194', '1hgz', 'J', 31, '1(28-45)'),
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INSERT INTO `subunits` (`id`, `protein_id`, `pdbid`, `letter`, `tilt`, `segment`) VALUES
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-- --------------------------------------------------------

--
-- Table structure for table `superfamily`
--

CREATE TABLE `superfamily` (
  `id` smallint(4) NOT NULL auto_increment,
  `number` char(7) NOT NULL default '',
  `name` char(80) NOT NULL default '',
  `tcdb` char(20) NOT NULL default '',
  `comment` char(255) default NULL,
  `pfam` char(10) NOT NULL,
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=280 ;

--
-- Dumping data for table `superfamily`
--

INSERT INTO `superfamily` (`id`, `number`, `name`, `tcdb`, `comment`, `pfam`) VALUES
(1, '1.1.03.', 'Light-harvesting complexes', '', NULL, ''),
(2, '1.1.02.', 'Photosynthetic reaction centers and photosystems', '3.E.2', NULL, ''),
(3, '1.1.04.', 'Transmembrane cytochrome b like', '', NULL, 'CL0328'),
(4, '1.1.05.', 'Cytochrome c oxidases', '3.D.4', NULL, 'PF00115'),
(5, '1.1.06.', 'Proton or Sodium translocating F-type, V-type and A-type ATPases', '3.A.2', NULL, ''),
(6, '1.1.01.', 'Rhodopsin-like proteins', '', NULL, 'CL0192'),
(7, '1.1.27.', 'Major Intrinsic Protein (MIP)/FNT superfamily', '', NULL, ''),
(8, '1.1.22.', 'Voltage-gated channel like', '', NULL, 'CL0030'),
(71, '1.3.13.', 'Nucleoside-specific channel-forming membrane porin (Tsx) (n=12,S=16)', '1.B.10', NULL, ''),
(10, '1.1.28.', 'Chloride transporter (ClC)', '2.A.49', NULL, ''),
(11, '1.1.24.', 'Small conductance mechanosensitive ion channel (MscS)', '1.A.23', NULL, 'PF05552'),
(12, '1.1.23.', 'Large conductance mechanosensitive ion channel (MscL)', '1.A.22', NULL, 'PF01741'),
(13, '1.1.19.', 'Ammonia and urea transporters', '', NULL, ''),
(14, '1.1.26.', 'Pentameric ligand-gated ion channels', '1.A.9', NULL, 'PF02932'),
(15, '1.1.14.', 'Major Facilitator Superfamily (MFS)', '2.A.1', NULL, 'CL0015'),
(16, '1.1.15.', 'Resistance-nodulation-cell division', '2.A.6', NULL, 'CL0322'),
(17, '1.1.09.', 'ABC transporters', '3.A.1', '', ''),
(232, '1.1.57.', 'Vitamin K epoxide reductase', '', NULL, 'PF07884'),
(19, '1.1.12.', 'General secretory pathway (Sec)', '3.A.5', NULL, ''),
(20, '1.1.16.', 'Dicarboxylate/amino acid:Cation Symporter (DAACS)', '2.A.23', NULL, ''),
(21, '1.1.13.', 'Mitochondrial Carrier (MC)', '2.A.29', NULL, ''),
(22, '1.1.08.', 'P-type ATPase (P-ATPase)', '3.A.3', '', 'PF00122'),
(23, '1.1.07.', 'Methane monooxygenase', '', NULL, 'PF02461'),
(24, '1.1.29.', 'Sulfatase', '', NULL, 'PF00884'),
(25, '1.2.07.', 'Glycophorin A', '', NULL, 'PF01102'),
(26, '1.3.01.', 'OmpA-OmpF porin family (n=8,S=10)', '1.B.6', NULL, ''),
(27, '1.3.07.', 'Omptin (n=10,S=12)', '1.B.1', NULL, 'PF01278'),
(28, '1.3.11.', 'Autotransporter (AT) (n=12,S=14)', '1.B.12', NULL, ''),
(29, '1.3.12.', 'OM phospholipase (n=12,S=16)', '', NULL, ''),
(30, '1.3.14.', 'FadL outer membrane protein (FadL) (n=14,S=14)', '1.B.9', NULL, ''),
(31, '1.3.16.', 'Trimeric porins (n=16,S=20)', '', NULL, ''),
(32, '1.3.18.', 'Sugar porins (n=18,S=22)', '1.B.3', NULL, ''),
(33, '1.3.20.', 'Ligand-gated protein channels (n=22,S=24)', '1.B.14', NULL, 'PF00593'),
(34, '1.3.24.', 'Outer Membrane Factor (OMF) (n=12,S=18) trimeric', '1.B.17', NULL, ''),
(35, '1.3.25.', 'Leukocidin-like', '', NULL, ''),
(37, '2.1.04.', 'Heme-dependent peroxidases', '', NULL, ''),
(38, '2.1.05.', 'Terpenoid cyclases/Protein prenyltransferases', '', NULL, 'CL0059'),
(39, '2.1.15.', 'ENTH/VHS domain', '', NULL, 'CL0009'),
(41, '1.2.17.', 'Cytochrome P450', '', NULL, 'PF00067'),
(42, '1.2.23.', 'Bcl-2 inhibitors of programmed cell death', '1.A.21', NULL, 'PF00452'),
(43, '2.1.18.', 'Annexins', '1.A.31', NULL, 'PF00191'),
(44, '2.1.21.', 'Influenza virus matrix protein M1', '', NULL, 'PF00598'),
(45, '2.1.17.', 'LEM domain', '', NULL, 'PF03020'),
(76, '3.1.06.', 'Peptaibol', '1.D.5', NULL, ''),
(47, '2.2.11.', 'C2 domain', '', NULL, 'CL0154'),
(48, '2.2.14.', 'Galactose-binding domain-like', '', NULL, 'CL0202'),
(180, '1.2.11.', 'Stannin', '', NULL, 'PF09049'),
(179, '1.3.23.', 'Trimeric autotransporter (n=12,S=12)', '1.B.40', NULL, 'CL0327'),
(51, '2.2.20.', 'PH domain-like', '', NULL, 'CL0266'),
(52, '2.2.06.', 'Lipocalins', '8.A.33', NULL, 'CL0116'),
(53, '2.2.38.', 'Cloacin translocation domain', '', NULL, 'PF03515'),
(54, '2.2.17.', 'Cystine-knot cytokines', '', NULL, 'CL0079'),
(55, '2.2.39.', 'Snake toxin-like', '1.C.74', NULL, 'CL0117'),
(56, '2.2.41.', 'Defensin-like', '', NULL, 'CL0075'),
(58, '1.2.22.', 'Amidase signature (AS) enzymes', '', NULL, 'PF01425'),
(59, '2.3.03.', 'FMN-linked oxidoreductases', '', NULL, 'PF01180'),
(60, '2.4.07.', 'PX domain', '', NULL, 'PF00787'),
(61, '2.2.37.', 'Scorpion toxin-like', '', NULL, 'CL0054'),
(62, '2.2.26.', 'FYVE/PHD zinc finger', '', NULL, 'CL0390'),
(63, '2.2.27.', 'C1 domain', '', NULL, 'CL0006'),
(64, '2.2.36.', 'Cyclotides', '', NULL, 'PF03784'),
(70, '1.2.09.', 'Single-helix ATPase regulators', '', NULL, ''),
(66, '1.1.17.', 'Monovalent cation/proton antiporter (CPA)', '2.A.33', NULL, 'CL0064'),
(67, '1.1.18.', 'Ligand/cation symporters', '', NULL, 'CL0062'),
(68, '3.1.05.', 'Magainin', '1.C.16', NULL, ''),
(69, '3.3.01.', 'Gramicidin A channel', '1.D.1', NULL, ''),
(72, '1.1.25.', 'CorA Metal Ion Transporters (MIT)', '1.A.35', NULL, 'PF01544'),
(73, '1.2.12.', 'Inovirus (filamentous phage) major coat protein', '', NULL, 'CL0371'),
(74, '1.2.13.', 'Pili subunits', '', NULL, ''),
(75, '1.2.10.', 'Pulmonary surfactant-associated protein', '', NULL, 'PF08999'),
(77, '1.1.20.', 'Drug/Metabolite Transporter (DMT)', '2.A.7', NULL, ''),
(78, '2.1.08.', 'Cytochrome c', '', '', 'CL0318'),
(79, '2.1.11.', 'Spectrin repeat', '', '', 'PF00435'),
(80, '2.1.12.', 'Outer surface protein C', '', '', 'PF01441'),
(81, '2.1.23.', 'Ectatomin subunits', '', '', 'PF06457'),
(82, '2.1.13.', 'Crustacean CHH/MIH/GIH neurohormone', '', '', 'PF01147'),
(83, '2.1.24.', 'Saposin', '1.C.35', '', ''),
(84, '2.1.25.', 'Bacteriocin AS-48', '1.C.28', '', 'PF09221'),
(85, '2.1.09.', 'Uteroglobin-like', '', '', 'CL0370'),
(86, '2.1.14.', 'TPR-like', '', '', ''),
(87, '2.1.02.', 'Lipoxygenase', '', '', ''),
(88, '2.1.03.', 'Phospholipase C/P1 nuclease', '', '', 'CL0368'),
(89, '2.1.06.', 'Terpenoid synthases', '', '', ''),
(90, '2.1.01.', 'Secretory phospholipase A2', '', '', ''),
(183, '2.3.18.', 'CoA-dependent acyltransferases', '', NULL, 'CL0149'),
(92, '2.1.10.', 'Glycolipid transfer protein', '', '', 'PF08718'),
(93, '2.1.26.', 'Colicin pore forming domain', '1.C.1', '', 'PF01024'),
(182, '2.3.17.', 'ClpP/Crotonase', '', NULL, 'CL0127'),
(95, '2.1.27.', 'delta-Endotoxin', '1.C.2', '', 'PF03945'),
(96, '2.1.28.', 'Heat-stable enterotoxin B', '', '', 'PF09075'),
(97, '2.1.20.', 'GLA-domain', '', '', 'PF00594'),
(98, '2.1.22.', 'Virus ectodomain', '', '', 'PF00517'),
(99, '2.2.12.', 'E set domains', '', '', 'CL0159'),
(100, '2.2.13.', 'Clathrin adaptor appendage domain', '', '', ''),
(101, '2.2.05.', 'Cupredoxins', '', '', 'CL0026'),
(174, '3.4.05.', 'Cyclosporin', '', NULL, 'PF00160'),
(103, '2.2.32.', 'Anemone pore-forming cytolysin', '1.C.38', '', 'PF06369'),
(104, '2.2.22.', 'Hydrophobin', '', '', 'PF06766'),
(274, '1.2.25.', 'Oligosaccaryltransferase', '', NULL, 'PF10215'),
(106, '2.2.21.', 'Actin cross-linking proteins', '', '', 'CL0066'),
(107, '2.2.02.', 'Trypsin-like serine proteases', '', '', 'PF00089'),
(108, '2.2.03.', 'Acid proteases', '', '', ''),
(109, '2.2.07.', 'Streptavidin-like', '', '', ''),
(181, '1.3.15.', 'OmpG porin (n=14,S=16)', '1.B.21', NULL, ''),
(111, '2.2.04.', 'Retinal pigment epithelial membrane protein', '', '', 'PF03055'),
(177, '2.4.03.', 'Transcriptional factor tubby, C-terminal domain', '', NULL, 'PF01167'),
(113, '2.2.24.', 'Vitelline membrane outer protein-I', '', '', 'PF03762'),
(114, '2.2.09.', 'Ganglioside GM2 activator', '', '', ''),
(115, '2.2.19.', 'Adsorption protein p2', '', '', 'PF09214'),
(116, '2.2.35.', 'Cholesterol-dependent cytolysin', '', '', 'CL0293'),
(117, '1.2.19.', 'Viral glycoprotein', '1.G.3', '', 'PF01589'),
(118, '2.2.28.', 'Gurmarin-like', '', '', ''),
(119, '2.2.29.', 'Agouti-related protein', '', '', 'PF05039'),
(120, '2.2.34.', 'Omega conotoxin-like', '', '', 'CL0083'),
(121, '2.2.30.', 'Elafin-like', '', '', ''),
(122, '2.2.40.', 'Neurotoxin III', '', '', 'PF08098'),
(123, '2.2.31.', 'Kringle-like', '', '', ''),
(124, '2.2.10.', 'High potential iron protein', '', '', 'PF01355'),
(125, '2.3.01.', 'Transglycosidases', '', '', 'CL0058'),
(126, '2.3.02.', 'PLC-like phosphodiesterases', '', '', 'CL0384'),
(127, '1.2.21.', 'Proteins with NAD(P)-binding Rossmann-fold domains', '', '', ''),
(128, '2.3.05.', 'FAD/NAD(P)-binding domain', '', 'Combines FAD-binding proteins with additional membrane-anchoring helices', 'CL0063'),
(129, '2.3.14.', 'CRAL/TRIO domain', '', '', 'PF00650'),
(130, '2.3.15.', 'Adenine nucleotide alpha hydrolases-like', '', '', 'CL0039'),
(131, '2.4.10.', 'PreATP-grasp domain', '', '', ''),
(132, '2.3.16.', 'P-loop containing nucleoside triphosphate hydrolases', '', '', 'CL0023'),
(275, '1.1.31.', 'Vitamin uptake transporter', '2.A.88', NULL, 'PF09515'),
(134, '2.3.08.', 'FabD/lysophospholipase-like', '', '', 'CL0323'),
(135, '2.3.06.', 'Alpha/beta-hydrolases', '', '', 'CL0028'),
(136, '2.3.10.', 'UDP-Glycosyltransferase/glycogen phosphorylase', '', '', 'CL0113'),
(137, '2.3.11.', 'Chelatase', '', '', 'CL0043'),
(176, '2.3.12.', 'Phosphotyrosine protein phosphatases II', '', NULL, ''),
(139, '2.3.13.', 'Thioredoxin-like', '', '', 'CL0172'),
(140, '2.4.01.', 'FAD-linked reductases, C-terminal domain', '', '', ''),
(141, '2.4.02.', 'NTF2-like', '', '', 'CL0051'),
(260, '3.1.19.', 'Membrane-binding domain of phosphotransferase IIA component', '', NULL, 'PF00358'),
(143, '2.2.25.', 'SH2 domain', '', '', ''),
(144, '2.4.05.', 'Sterol carrier protein', '', '', 'PF00515'),
(145, '2.4.09.', 'SNARE-like', '', '', 'CL0212'),
(178, '2.2.01.', 'Peptidase SF', '', NULL, 'CL0299'),
(147, '2.4.06.', 'Bet v1-like', '', '', 'CL0209'),
(148, '2.4.04.', 'DNase I-like', '', '', ''),
(149, '2.4.11.', 'Crambin-like', '1.C.44', '', 'PF00321'),
(150, '2.4.12.', 'Leucocin-like bacteriocin', '1.C.24', '', 'PF01721'),
(151, '3.1.07.', 'Moricin', '1.C.17', '', 'PF06451'),
(152, '3.1.08.', 'Tachykinin peptides', '', '', 'PF02202'),
(153, '3.1.09.', 'Antimicrobial peptide HP', '', '', ''),
(154, '3.1.01.', 'Peptide hormones', '', '', ''),
(155, '3.1.10.', 'Insect toxins', '', '', 'PF08117'),
(156, '3.1.02.', 'Endothelin-like', '', '', 'PF00322'),
(157, '3.1.11.', 'Alpha-conotoxins', '', '', ''),
(158, '3.1.03.', 'Major surface glycoprotein G', '', '', 'PF00802'),
(159, '3.1.04.', 'Synuclein', '1.C.77', '', 'PF01387'),
(160, '3.1.12.', 'Cecropin-like', '', '', ''),
(161, '3.2.02.', 'Lactoferricin B', '', '', 'PF00405'),
(162, '3.2.03.', 'Hepcidin', '', '', 'PF06446'),
(163, '3.2.04.', 'Cyclic trypsin inhibitor', '', '', ''),
(164, '3.2.05.', 'Macrocyclic bacteriocins', '', '', ''),
(165, '3.2.06.', 'PSP1-like', '', '', 'PF02425'),
(166, '3.2.07.', 'Tricyclic peptide RP71935', '', '', ''),
(167, '3.2.01.', 'Octreotide', '', '', ''),
(185, '3.1.13.', 'Membrane-binding domain of viral polyproteins', '', NULL, ''),
(169, '3.4.01.', 'Gramicidin S', '', '', ''),
(170, '3.4.02.', 'Lantibiotic peptides', '1.C.20', '', ''),
(171, '3.4.03.', 'Heat-stable enterotoxin', '', '', ''),
(172, '3.4.04.', 'Cyclic lipopeptide antibiotics', '', NULL, ''),
(173, '2.4.13.', 'OSBP-related proteins', '', NULL, 'PF01237'),
(186, '1.1.30.', 'Rhomboid proteins', '', NULL, 'CL0207'),
(187, '1.2.02.', 'T cell receptor transmembrane dimerization domain', '', NULL, 'PF11628'),
(188, '1.2.16.', 'Outer membrane auxiliary proteins', '1.B.18', NULL, ''),
(189, '2.2.08.', 'Osmotin, thaumatin-like protein', '', NULL, 'PF00314'),
(190, '2.2.15.', ' Methuselah ectodomain', '', NULL, ''),
(191, '2.1.16.', 'Extracellular domain of amyloid beta A4 protein', '', NULL, ''),
(192, '2.2.16.', 'Lipoprotein localization factors', '', NULL, ''),
(193, '2.1.29.', 'Apolipoprotein', '', NULL, 'PF01442'),
(194, '1.1.33.', 'Disulfide bond oxidoreductase-B (DsbB)', '5.A.2', NULL, 'PF02600'),
(195, '3.1.14.', 'Designed alpha-helical peptides', '', NULL, ''),
(196, '1.2.08.', 'Multi-heme cytochromes', '', NULL, 'CL0317'),
(197, '1.2.04.', 'Integrin transmembrane dimer', '', NULL, ''),
(231, '1.1.10.', 'Glutamate-gated Ion Channel (GIC) superfamily', '1.A.10.', NULL, ''),
(199, '1.1.40.', 'MAPEG (Eicosanoid and Glutathione metabolism proteins)', '', NULL, ''),
(200, '1.3.17.', 'Omp85-TpsB transporters (n=16,S=20)', '1.B.20', NULL, 'CL0191'),
(201, '1.1.41.', 'Magnesium ion transporter-E (MgtE)', '9.A.19', NULL, 'PF03448'),
(202, '1.1.42.', 'ENaC/P2X', '', NULL, ''),
(203, '1.3.19.', 'OprD/AlgE superfamily (n=18,S=22)', '', NULL, ''),
(204, '1.1.43.', 'Cation diffusion facilitator', '2.A.4', NULL, 'CL0184'),
(205, '1.1.44.', 'Peptidase M50', '', NULL, ''),
(206, '1.2.14.', 'Viral channel proteins', '1.A.19', NULL, ''),
(207, '1.2.01.', 'Protein tyrosine kinase', '', NULL, ''),
(208, '1.3.21.', 'Fimbrial usher porin (n=24,S=26)', '1.B.11', NULL, ''),
(209, '1.1.47.', 'Prokaryotic molybdopterin-containing oxidoreductases', '5.A.3', NULL, ''),
(210, '1.3.22.', 'Mitochondrial and plastid porins (n=19,S=20)', '1.B.8', NULL, ''),
(221, '2.1.38.', 'Corynebacterial porin B', '1.B.41', NULL, 'PF11565'),
(212, '1.3.09.', 'Lipid A deacylase (n=12, S=14)', '', NULL, ''),
(213, '1.2.06.', 'BNip3 protein family', '1.A.20', NULL, ''),
(230, '1.2.03.', 'Immunoglobulin', '', NULL, ''),
(215, '1.1.52.', 'Gap junction-forming connexin', '1.A.24', NULL, ''),
(216, '1.2.18.', 'Lysozyme-like', '', NULL, 'CL0037'),
(217, '1.1.53.', 'Prokaryotic diacylglycerol kinase', '', NULL, 'PF01219'),
(218, '1.2.05.', 'SNARE complex', '', NULL, 'PF00835'),
(219, '1.1.55.', 'Pore-forming haemolysin E', '1.C.10', NULL, 'PF06109'),
(222, '2.3.19.', 'Nucleotide-diphospho-sugar transferases', '', NULL, 'CL0110'),
(223, '2.2.42.', 'Pneumovirus matrix protein', '', NULL, 'PF03393'),
(224, '2.1.31.', 'Colicin M', '', NULL, ''),
(225, '2.2.43.', 'Galactose mutarotase-like', '', NULL, ''),
(226, '3.2.08.', 'BRICHOS domain', '', NULL, ''),
(227, '3.2.09.', 'Ksi conotoxins', '8.B.4', NULL, ''),
(228, '2.3.20.', 'CheY-like', '', NULL, 'PF01058'),
(229, '1.3.10.', 'Oligogalactoronate-specific porin (KdgM) (n=12,S=14)', '1.B.35', NULL, ''),
(233, '1.1.58.', 'Signal transduction histidine kinase', '', NULL, ''),
(234, '3.1.15.', 'FATC domain', '', NULL, 'PF02260'),
(235, '3.1.16.', 'Pardaxin', '', NULL, 'PF07425'),
(236, '3.1.17.', 'Cathelicidin', '1.C.33', NULL, 'PF00666'),
(237, '2.1.32.', 'Carnocyclin A', '1.C.90.', NULL, ''),
(238, '3.4.06.', 'Cathelicidin', '1.C.33.', NULL, 'PF12153'),
(239, '3.4.07.', 'Designed nonregular peptides', '', NULL, ''),
(240, '1.1.11.', 'Tellurite-resistance/Dicarboxylate transporter', '2.A.16', NULL, 'PF03595'),
(242, '2.1.33.', 'DrrA protein', '', NULL, ''),
(244, '2.4.14.', 'Type IV (VirB) secretory pathway family', '3.A.7', NULL, ''),
(245, '2.1.34.', 'DivIVA protein', '', NULL, 'PF05103'),
(246, '2.1.35.', 'PASCIN (protein kinase C and casein kinase substrate)', '', NULL, 'PF00611'),
(247, '1.1.59.', 'MerTCFH', '9.A.7', NULL, ''),
(248, '3.1.18.', 'Lactococcin', '1.C.22', NULL, ''),
(249, '1.1.60.', 'Multidrug/Oligosaccharidyl-lipid superfamily', '2.A.66', NULL, 'PF01554'),
(250, '2.2.44.', 'PLAT domain', '', 'Also present in liopxygenases, pancreatic lipases and  alpha-toxin', 'CL0321'),
(251, '2.1.36.', 'Endoplasmic reticulum oxidoreductin', '', NULL, 'PF04137'),
(252, '1.2.15.', 'TYROBP', '', NULL, ''),
(253, '1.1.62.', 'Bile/arsenite/riboflavin transporter (BART)', '', NULL, ''),
(254, '1.2.24.', 'Fst toxin', '1.C.64', NULL, ''),
(255, '1.1.63.', 'Phosphotransferase-GFL (Glc, Fru, Lac) superfamily', '', NULL, ''),
(256, '1.2.20.', 'Peptidase MA', '', NULL, 'CL0126'),
(257, '2.1.37.', 'DBL (Duffy-binding like)', '', NULL, 'CL0195'),
(258, '3.1.20.', 'Delta lysin', '', NULL, 'PF05372'),
(259, '3.1.21.', 'Envelope glycoprotein E1', '', NULL, 'PF01539'),
(261, '2.3.09.', 'Flavokinase-like nucleotidyl transferase', '', NULL, 'CL0119'),
(262, '3.1.22.', 'Scorpion NDBP 5 family', '', NULL, ''),
(263, '3.1.23.', 'Antifreeze protein, type I', '', NULL, ''),
(264, '3.1.24.', 'Aurein', '', NULL, 'PF08256'),
(265, '3.2.10.', 'Thanatin', '', NULL, ''),
(266, '1.3.02.', 'Opacity porins (n=8,S=10)', '', NULL, 'PF02462'),
(267, '1.3.03.', 'Outer membrane protein W (OmpW) family (n=8,S=10)', '1.B.39', NULL, 'PF03922'),
(268, '1.3.04.', 'Lipid A acylation (n=8,S=10)', '', NULL, 'PF07017'),
(269, '1.3.05.', 'Lipid A 3-O-deacylase (PagL) (n=8,S=10)', '', NULL, 'PF09411'),
(270, '1.3.06.', 'Major OMP (n=8,S=10)', '', NULL, ''),
(271, '1.3.08.', 'OM adhesion protein (n=10,S=12)', '', NULL, 'PF07239'),
(272, '2.1.07.', 'Multiheme cytochrome', '', NULL, 'CL0317'),
(273, '1.1.21.', 'Oligosaccharyltransferase', '', NULL, ''),
(276, '3.1.25.', 'Amylin family', '1.C.49', NULL, 'PF00214'),
(277, '1.1.32.', 'Peptidase AD', '', NULL, 'CL0130'),
(278, '2.2.18.', 'Second domain of Mu2 adaptin subunit', '', NULL, 'CL0448'),
(279, '1.1.34.', 'NADH dehydrogenase I', '3.D.1', NULL, 'CL0425');

-- --------------------------------------------------------

--
-- Table structure for table `temp_pfam`
--

CREATE TABLE `temp_pfam` (
  `name` varchar(255) NOT NULL,
  `pfam` varchar(10) NOT NULL
) ENGINE=MyISAM DEFAULT CHARSET=latin1;

--
-- Dumping data for table `temp_pfam`
--

INSERT INTO `temp_pfam` (`name`, `pfam`) VALUES
('ADP/ATP carrier', 'PF00153'),
('ATP-gated cation channel', 'PF00864'),
('Acetylcholinesterase-like', 'PF00135'),
('Acid-sensing ion channels', 'PF00858'),
('Adsorption protein p2', 'PF09214'),
('Agouti-related protein', 'PF05039'),
('Albumin 1', 'PF08027'),
('Alpha-Hemolysin (alphaHL) channel-forming toxin (n=14,S=14)', 'PF07968'),
('Alpha-conotoxin', 'PF07365'),
('Amidase signature (AS) enzymes', 'PF01425'),
('Amino acid-Polyamine-Organocation (APC) family', 'PF00324'),
('Ammonia transporter Amt', 'PF00909'),
('Anemone pore-forming cytolysin', 'PF06369'),
('Animal lipoxygenases', 'PF00305'),
('Annexins', 'PF00191'),
('Apolipoprotein', 'PF01442'),
('ArsA ATPase', 'PF02374'),
('Autotransporter-2 (AT-2)', 'PF05662'),
('Autotransporters of N-terminal passenger domain', 'PF03797'),
('BNip3 (BCL2/Adenovirus E1B-interacting protein 3)', 'PF06553'),
('Bacterial PLC', 'PF00388'),
('Bacterial conjugation TrbI-like', 'PF03743'),
('Bacterial lipase', 'PF00561'),
('Bacterial phospholipase C', 'PF00882'),
('Bacterial zinc transporters', 'PF01545'),
('Bacteriocin AS-48', 'PF09221'),
('Bcl-2 inhibitors of programmed cell death', 'PF00452'),
('Beta-glycanases', 'PF02055'),
('Betaine/carnitine/choline transporters', 'PF02028'),
('Brucella-Rhizobium Porin (BRP)', 'PF00593'),
('C-terminal domain of adrenodoxin reductase-like', 'PF07992'),
('CD4', 'PF12104'),
('CRAL/TRIO domain', 'PF00650'),
('Calcium ATPase regulators', 'PF04272'),
('Caspase catalytic domain', 'PF00656'),
('Cathelicidin', 'PF12153'),
('CheY-like', 'PF01058'),
('Chloride channel', 'PF00654'),
('Choline/carnitine  O-acyltransferases', 'PF00755'),
('Circulin A', 'PF03784'),
('Cloacin translocation domain', 'PF03515'),
('Clostridium neurotoxins', 'PF07952'),
('ClpP protease', 'PF00574'),
('Colicin A', 'PF01024'),
('Connexin', 'PF00029'),
('Conotoxin', 'PF02950'),
('CorA Metal Ion Transporters (MIT)', 'PF01544'),
('Corynebacterial porin B', 'PF11565'),
('Crambin-like', 'PF00321'),
('Crustacean CHH/MIH/GIH neurohormone', 'PF01147'),
('Cutinase-like', 'PF01083'),
('Cyclosporin', 'PF00160'),
('Cycloviolacin O1', 'PF03784'),
('Cytochrome P450', 'PF00067'),
('Cytochrome bc1 and b6f complexes', 'PF00033'),
('Cytochrome c of nitrite reductase', 'PF03264'),
('Cytochrome c oxidases', 'PF00115'),
('Defensin', 'PF00323'),
('Dendroaspin', 'PF00087'),
('Dermaseptin', 'PF12121'),
('Discoidin domain', 'PF00754'),
('Disulfide bond oxidoreductase-B (DsbB)', 'PF02600'),
('DivIVA protein', 'PF05103'),
('Drug/proton antiporter', 'PF07690'),
('Dynamin', 'PF00350'),
('ENTH domain', 'PF01417'),
('ETFP subunits', 'PF01012'),
('Ectatomin subunits', 'PF06457'),
('Endothelin-like', 'PF00322'),
('Epoxide Hydrolase', 'PF07858'),
('Eukaryotic proteases', 'PF00089'),
('FAD-linked reductases, N-terminal domain', 'PF01593'),
('FATC domain', 'PF02260'),
('FMN-linked oxidoreductases', 'PF01180'),
('FXYD regulators', 'PF02038'),
('FYVE, a phosphatidylinositol-3-phosphate binding domain', 'PF01363'),
('Family 1 of glycosyl hydrolase', 'PF00232'),
('Fatty acid binding protein-like', 'PF00061'),
('Fatty acid transporter FadL family', 'PF03349'),
('Ferrochelatase', 'PF00762'),
('Fibronectin type II module', 'PF00040'),
('Fimbrial usher porin', 'PF00577'),
('Formate dehydrogenase', 'PF00033'),
('Formate/Nitrite transporter (FNT) family', 'PF01226'),
('Fumarate reductase respiratory complex', 'PF01127'),
('Fungal lipases', 'PF03893'),
('G-protein coupled receptors', 'PF00001'),
('G-proteins', 'PF00503'),
('GDI-like N domain', 'PF00996'),
('GLA-domain', 'PF00594'),
('GMC oxidoreductases', 'PF00732'),
('Gamma-adaptin C-terminal appendage domain-like', 'PF02883'),
('Gastric lipase', 'PF04083'),
('General Bacterial Porin (GBP)', 'PF00267'),
('Glucagon', 'PF00123'),
('Glutamate-gated Ion Channel (GIC) family', 'PF00060'),
('Glutathione S-transferase', 'PF00462'),
('Glycerol-3-phosphate transporter', 'PF07690'),
('Glycolipid transfer protein', 'PF08718'),
('Glycophorin A', 'PF01102'),
('Glycosylating toxin', 'PF04488'),
('Glycosyltransferase family 28', 'PF03033'),
('Glycosyltransferase family 9', 'PF01075'),
('Gonadodropin/Follitropin', 'PF00236'),
('Heat-stable enterotoxin B', 'PF09075'),
('Hepcidin', 'PF06446'),
('High potential iron protein', 'PF01355'),
('Histidine-rich actin-binding protein', 'PF06268'),
('Hydrophobin', 'PF06766'),
('IPT/TIG domains', 'PF00071'),
('IPT/TIG domains', 'PF01833'),
('Influenza virus matrix protein 2', 'PF04772'),
('Influenza virus matrix protein M1', 'PF00598'),
('Insect defensins', 'PF01097'),
('Insect secretory phospholipase A2', 'PF05826'),
('Insect toxins', 'PF08117'),
('Integrin transmembrane domain', 'PF08725'),
('Inward rectifier potassium channels', 'PF01007'),
('Ion-translocating microbial rhodopsin', 'PF01036'),
('Isoprenyl diphosphate synthases', 'PF00348'),
('Kalata B1', 'PF03784'),
('Kunitz (STI inhibitors)', 'PF00197'),
('LEM domain', 'PF03020'),
('LacY-like proton/sugar symporter', 'PF01306'),
('Lactoferricin B', 'PF00405'),
('Large conductance mechanosensitive ion channel (MscL)', 'PF01741'),
('Leucocin-like bacteriocin', 'PF01721'),
('Ligand-gated ion channel of neurotransmitter receptors', 'PF02932'),
('Light-harvesting complexes from bacteria', 'PF00556'),
('Light-harvesting complexes from chloroplasts', 'PF00504'),
('Lipase', 'PF03403'),
('Lipid A acylation', 'PF09411'),
('Lipid A deacylase', 'PF09982'),
('Lipid/drug exporters', 'PF00664'),
('Lipoproteins of Mycobacteria', 'PF07161'),
('Long-chain scorpion toxins', 'PF00537'),
('Lysophospholipase', 'PF01735'),
('Lysophospholipase', 'PF01734'),
('MAPEG domain', 'PF01124'),
('MHC antigen-recognition domain', 'PF07654'),
('ML domain', 'PF02221'),
('Magnesium ion transporter-E (MgtE)', 'PF03448'),
('Major coat protein, symmetry class I', 'PF05371'),
('Major intrinsic protein (MIP) family', 'PF00230'),
('Major surface glycoprotein G', 'PF00802'),
('Malptoporin-like proteins', 'PF02264'),
('Maltose uptake transporter', 'PF00005'),
('Mammalian PLC', 'PF09279'),
('Mastoparan family', 'PF08249'),
('Melittin', 'PF01372'),
('MerF Mercuric ion uptake family', 'PF11431'),
('Methane monooxygenase', 'PF02461'),
('Methionine uptake transporter', 'PF00005'),
('Methuselah ectodomain', 'PF06652'),
('Monodomain cytochrome c', 'PF00034'),
('Moricin', 'PF06451'),
('Motilin', 'PF04644'),
('Multidrug efflux transporter', 'PF00873'),
('Multidrug resistance exporter (MDR)', 'PF00005'),
('Mycobacterial Porin (MBP) (n=16,S=16)', 'PF09203'),
('Mycobacterial antigens', 'PF00756'),
('Myeloperoxidase-like', 'PF03098'),
('Myotubularin-like phosphatases', 'PF02893'),
('NK-lysin-like', 'PF05184'),
('Neuropeptide Y', 'PF00159'),
('Neurotoxin III', 'PF08098'),
('Neurotransmitter: sodium symporter', 'PF00209'),
('Neutral sphingomyelinases', 'PF03372'),
('Nisin', 'PF02052'),
('Nonstructural protein 5a, anchor domain', 'PF01506'),
('Nucleoside transporter Tsx', 'PF03502'),
('OM adhesion protein OpcA', 'PF07239'),
('OM phospholipase A, OmpLA', 'PF02253'),
('OM protease OMPT', 'PF01278'),
('OMA polysaccharide transporter', 'PF02563'),
('OMPA-like proteins', 'PF03922'),
('OSBP-related proteins', 'PF01237'),
('Oligogalactoronate-specific porin (KdgM)', 'PF06178'),
('OmpG porin', 'PF09381'),
('Orexin', 'PF02072'),
('Osmotin, thaumatin-like protein', 'PF00314'),
('Outer Membrane Receptor (OMR)', 'PF00593'),
('Outer membrane porin (Opr)', 'PF03573'),
('Outer membrane protein insertion porin (OmpIP)', 'PF08479'),
('Outer surface protein C', 'PF01441'),
('P-ATPase', 'P-ATPas'),
('PASCIN (protein kinase C and casein kinase substrate)', 'PF00611'),
('PLC-like (P variant)', 'PF00168'),
('PSP1-like', 'PF02425'),
('PX domain', 'PF00787'),
('Palicourein', 'PF03784'),
('Pancreatic lipase', 'PF00151'),
('Pardaxin', 'PF07425'),
('Pepsin-like', 'PF00026'),
('Perfringolysin', 'PF01289'),
('Phage lysozyme', 'PF00959'),
('Phosducin', 'PF02114'),
('Phosphatidylinositol transfer protein (PITP)', 'PF02121'),
('Phosphoinositide-binding clathrin adaptor, N-terminal domain', 'PF07651'),
('Phosphotyrosine-binding domain', 'PF00640'),
('Photosystem II', 'PF00124'),
('Photosystem II', 'PF02533'),
('Photosystem II', 'PF00421'),
('Photosystem I', 'PF00223'),
('Pilin', 'PF07963'),
('Plant defensins', 'PF00304'),
('Plastocyanin/azurin-like', 'PF00127'),
('Platelet-activating factor acetylhydrolase', 'PF03403'),
('Pleckstrin-homology domain', 'PF00169'),
('Pleckstrin-homology domain', 'PF00621'),
('Pleurocidin', 'PF08107'),
('Pneumovirus matrix protein', 'PF03393'),
('Polyisoprenoid-binding protein', 'PF04264'),
('Polysulfide reductase', 'PF00037'),
('Polysulfide reductase', 'PF04879'),
('Pore-forming haemolysin E', 'PF06109'),
('Porins O and P', 'PF07396'),
('Prokaryotic diacylglycerol kinase', 'PF01219'),
('Prokaryotic pentameric ligand-gated ion channels', 'PF02931'),
('Prokaryotic phospholipase A2', 'PF09056'),
('Prokaryotic proteases', 'PF00089'),
('Protein kinase C1 domain', 'PF00130'),
('Protein translocase SecY', 'PF00344'),
('Proton glutamate symport protein', 'PF00375'),
('Pulmonary surfactant-associated protein', 'PF08999'),
('Respiratory nitrate reductase', 'PF02665'),
('Retinal pigment epithelial membrane protein', 'PF03055'),
('Retinol binding protein-like', 'PF00061'),
('RhoGDI-like', 'PF00025'),
('Rhomboid proteases', 'PF01694'),
('SNARE complex', 'PF00835'),
('STAR domain', 'PF01852'),
('Saposin B', 'PF03489'),
('Sea anemone sodium channel inhibitory toxin', 'PF00706'),
('Sedlin', 'PF04628'),
('Shikimate kinase', 'PF01202'),
('Short-chain scorpion toxins', 'PF00451'),
('Site-2 protease', 'PF02163'),
('Small conductance mechanosensitive ion channel (MscS)', 'PF05552'),
('Snake venom toxins', 'PF00087'),
('Sodium/Proton antiporter 1', 'PF06965'),
('Solute:sodium symporter', 'PF00474'),
('Spectrin repeat', 'PF00435'),
('Spider toxins', 'PF02819'),
('SpoIIaa-like protein', 'PF11964'),
('Srx domain of the signal recognition particle receptor alpha-subunit', 'PF09201'),
('Stannin', 'PF09049'),
('Sterol carrier protein', 'PF02036'),
('Sterol carrier protein', 'PF00515'),
('Subtilosin A', 'PF11420'),
('Succinate dehydrogenase/fumarate reductase', 'PF02300'),
('Synapsin domain', 'PF02078'),
('Synaptotagmin-like (S variant)', 'PF00168'),
('Synatpobrevin N-terminal domain', 'PF00957'),
('Synuclein', 'PF01387'),
('T cell receptor transmembrane dimerization domain', 'PF11628'),
('Tachykinin peptides', 'PF02202'),
('Tandem RecA ATPase-like', 'PF07517'),
('Tellurite-resistance/Dicarboxylate transporter', 'PF03595'),
('Terpene synthases', 'PF00432'),
('Tetratricopeptide repeat', 'PF01733'),
('Thioesterases', 'PF02089'),
('Third domain of FERM', 'PF09379'),
('TolC-like proteins', 'PF02321'),
('Transcriptional factor tubby, C-terminal domain', 'PF01167'),
('Transglycosylase of penicillin-binding proteins', 'PF00912'),
('Two-domain cytochrome c', 'PF00034'),
('Type 1 signal peptidase', 'PF10502'),
('Tyrosine-dependent oxidoreductases', 'PF00106'),
('Urea transporter', 'PF03253'),
('Uteroglobin', 'PF09252'),
('V-type and F-type ATPases', 'PF00137'),
('VHS domain', 'PF00790'),
('Vertebrate secretory phospholipase A2', 'PF00068'),
('Viral glycoprotein', 'PF01589'),
('Viral proteases', 'PF02907'),
('Virus ectodomain', 'PF00517'),
('Vitamin K epoxide reductase', 'PF07884'),
('Vitamine B&lt;sub&gt;12&lt;/sub&gt; transporter-like ABC transporters', 'PF01032'),
('Vitelline membrane outer protein-I', 'PF03762'),
('Voltage-dependent anion channel (VDAC) porin', 'PF01459'),
('Voltage-gated ion channels', 'PF07885'),
('delta-Endotoxin', 'PF03945');

-- --------------------------------------------------------

--
-- Table structure for table `temp_protein`
--

CREATE TABLE `temp_protein` (
  `pdbid` varchar(5) NOT NULL,
  `thickness` decimal(4,1) NOT NULL,
  `thicknesserror` decimal(4,1) NOT NULL,
  `tilt` smallint(3) NOT NULL,
  `tilterror` smallint(3) NOT NULL,
  `gibbs` decimal(5,1) NOT NULL
) ENGINE=MyISAM DEFAULT CHARSET=latin1;

--
-- Dumping data for table `temp_protein`
--

INSERT INTO `temp_protein` (`pdbid`, `thickness`, `thicknesserror`, `tilt`, `tilterror`, `gibbs`) VALUES
('1a0r', 2.3, 1.0, 50, 4, -7.4),
('1a0s', 23.8, 1.1, 0, 0, -103.5),
('1a25', 3.1, 1.0, 44, 18, -2.8),
('1a8a', 2.1, 1.1, 89, 10, -8.9),
('1a8c', 2.7, 1.0, 80, 11, -4.7),
('1a91', 36.1, 6.7, 21, 3, -21.4),
('1aa7', 2.6, 0.8, 89, 4, -5.6),
('1ae7', 4.7, 0.6, 84, 9, -6.2),
('1af6', 25.1, 0.7, 0, 0, -117.9),
('1afo', 31.9, 2.8, 5, 6, -43.5),
('1agg', 2.5, 1.4, 57, 17, -5.0),
('1ahl', 3.7, 1.2, 86, 11, -7.3),
('1akg', 4.2, 1.4, 42, 19, -5.9),
('1akn', 3.8, 1.5, 77, 15, -6.7),
('1ann', 2.2, 1.0, 77, 3, -6.0),
('1ans', 3.3, 1.4, 50, 15, -4.7),
('1aod', 7.4, 1.0, 79, 10, -9.2),
('1apf', 6.4, 1.3, 78, 19, -7.1),
('1aqb', 4.1, 1.1, 75, 14, -4.4),
('1aql', 5.7, 1.1, 78, 7, -9.6),
('1ar1', 31.9, 1.5, 7, 0, -108.4),
('1atx', 4.5, 1.7, 63, 12, -6.1),
('1aua', 8.8, 1.1, 75, 10, -14.3),
('1aun', 5.8, 1.0, 85, 11, -6.7),
('1auv', 1.9, 1.1, 86, 11, -5.2),
('1avc', 4.4, 1.0, 83, 1, -8.1),
('1avw', 6.6, 1.5, 75, 10, -6.7),
('1axn', 2.7, 0.8, 77, 11, -5.7),
('1ayj', 11.0, 1.9, 39, 19, -7.4),
('1b12', 5.4, 1.8, 88, 7, -5.1),
('1b3i', 2.8, 1.4, 43, 18, -4.4),
('1b4v', 5.4, 0.6, 39, 4, -8.4),
('1b56', 2.5, 2.0, 56, 18, -3.5),
('1b5n', 3.1, 1.2, 87, 16, -3.7),
('1b9x', 1.0, 1.6, 49, 12, -3.9),
('1bds', 5.6, 0.8, 83, 9, -9.6),
('1bdy', 1.5, 1.4, 84, 16, -3.2),
('1bg1', 2.4, 10.4, 90, 10, -8.2),
('1bh4', 3.9, 1.2, 60, 18, -6.6),
('1bhp', 2.9, 2.0, 56, 19, -4.8),
('1bjj', 2.6, 0.7, 86, 5, -8.4),
('1bk9', 7.3, 0.3, 87, 3, -11.4),
('1bnb', 6.0, 1.6, 88, 15, -10.8),
('1brv', 2.6, 1.6, 40, 19, -4.0),
('1bu8', 3.5, 1.3, 87, 10, -6.1),
('1bwy', 4.8, 1.3, 71, 12, -6.6),
('1bxv', 2.0, 1.6, 36, 19, -2.6),
('1byn', 3.8, 1.6, 32, 19, -4.7),
('1c17', 34.6, 1.2, 4, 0, -149.9),
('1c44', 3.7, 1.2, 74, 17, -4.8),
('1c4e', 5.2, 1.3, 17, 17, -4.8),
('1c6s', 0.4, 1.7, 89, 16, -1.3),
('1c8z', 2.8, 0.9, 89, 13, -5.8),
('1ca1', 2.9, 1.0, 89, 4, -9.3),
('1cbr', 6.5, 1.1, 45, 11, -5.4),
('1cbs', 7.1, 1.9, 41, 13, -5.9),
('1cdt', 4.2, 1.0, 46, 14, -6.9),
('1cjy', 5.8, 1.0, 70, 9, -9.9),
('1cle', 10.2, 0.0, 83, 0, -24.7),
('1cn2', 2.9, 1.6, 81, 16, -5.1),
('1co6', 1.4, 0.7, 78, 10, -3.3),
('1col', 1.8, 1.0, 43, 11, -3.2),
('1cor', 2.6, 1.1, 73, 12, -6.1),
('1coy', 4.4, 1.1, 43, 10, -6.8),
('1crb', 2.4, 1.7, 52, 19, -5.3),
('1ctx', 2.8, 1.7, 29, 18, -4.6),
('1cuo', 1.4, 1.6, 69, 15, -4.3),
('1cvl', 9.9, 1.0, 53, 9, -8.7),
('1cw6', 3.6, 1.1, 90, 16, -6.2),
('1cx2', 9.7, 0.4, 89, 3, -37.4),
('1cxa', 2.0, 1.2, 88, 13, -4.3),
('1czs', 3.4, 1.6, 13, 15, -6.2),
('1d1h', 3.4, 1.7, 68, 15, -4.2),
('1d3h', 3.4, 0.8, 55, 6, -10.1),
('1d5r', 2.9, 0.8, 83, 1, -4.5),
('1d5t', 2.8, 2.0, 19, 18, -3.8),
('1d6g', 7.0, 0.2, 89, 2, -11.6),
('1d7n', 6.5, 1.7, 82, 16, -7.5),
('1d7p', 4.8, 2.0, 28, 10, -8.8),
('1dan', 3.9, 2.0, 30, 19, -5.2),
('1dbh', 2.7, 2.8, 28, 19, -4.2),
('1df4', 6.3, 0.9, 0, 10, -6.7),
('1df6', 4.1, 1.2, 63, 19, -5.9),
('1dfn', 1.4, 1.3, 87, 15, -3.9),
('1dg2', 5.1, 1.7, 89, 16, -4.9),
('1djt', 3.8, 0.9, 90, 15, -6.9),
('1djx', 4.1, 0.9, 68, 5, -7.2),
('1dk5', 3.5, 1.3, 76, 18, -4.4),
('1dm5', 2.7, 1.0, 90, 7, -10.2),
('1doa', 1.1, 1.3, 87, 4, -3.1),
('1dq7', 5.9, 1.8, 88, 18, -8.1),
('1dqv', 1.6, 1.2, 86, 13, -3.7),
('1dqz', 4.6, 0.8, 36, 6, -9.3),
('1drs', 3.3, 1.5, 87, 12, -6.5),
('1ds6', 2.8, 1.0, 82, 6, -5.5),
('1dt5', 5.1, 0.9, 79, 13, -5.9),
('1dt6', 7.3, 1.0, 13, 7, -8.8),
('1dvp', 3.0, 0.0, 89, 0, -6.6),
('1dy9', 8.4, 1.1, 58, 14, -9.6),
('1dyn', 4.1, 1.2, 88, 15, -9.7),
('1e12', 31.8, 1.4, 0, 1, -126.7),
('1e4r', 2.8, 1.1, 74, 19, -5.5),
('1e4t', 3.6, 1.4, 13, 19, -5.2),
('1e54', 25.4, 0.5, 0, 0, -138.8),
('1e6c', 2.6, 1.8, 90, 12, -5.8),
('1e6e', 2.3, 1.0, 11, 2, -4.1),
('1ea5', 1.8, 1.1, 34, 5, -4.7),
('1eaz', 1.7, 1.6, 87, 14, -3.0),
('1eci', 5.3, 1.8, 58, 15, -5.2),
('1efp', 4.3, 1.1, 90, 13, -4.8),
('1efv', 4.6, 1.3, 79, 12, -4.6),
('1eh5', 5.3, 0.9, 59, 6, -8.1),
('1ehk', 31.3, 1.2, 8, 0, -114.6),
('1ehs', 1.4, 1.1, 64, 11, -6.0),
('1ein', 8.1, 0.8, 63, 4, -14.5),
('1ejg', 4.0, 1.7, 79, 15, -7.0),
('1ek9', 24.6, 1.4, 0, 2, -56.1),
('1em2', 2.0, 1.1, 82, 12, -5.0),
('1epw', 3.3, 2.0, 28, 6, -6.4),
('1eth', 13.6, 0.2, 90, 3, -13.3),
('1etn', 3.3, 1.1, 45, 18, -1.9),
('1ews', 4.7, 1.1, 18, 17, -4.4),
('1ex9', 11.0, 1.0, 52, 5, -30.0),
('1f0k', 5.3, 1.2, 55, 7, -8.6),
('1f0n', 3.7, 0.9, 33, 7, -7.4),
('1f1f', 4.8, 1.6, 80, 15, -3.5),
('1f3k', 2.8, 1.4, 57, 18, -4.5),
('1f56', 1.4, 1.5, 11, 15, -2.0),
('1f6w', 1.8, 0.5, 81, 10, -5.1),
('1f76', 3.7, 0.8, 24, 8, -8.7),
('1f8u', 2.6, 1.0, 60, 9, -7.3),
('1fao', 2.4, 2.0, 59, 19, -3.9),
('1faq', 4.8, 1.1, 30, 14, -7.3),
('1fd3', 5.2, 1.2, 80, 12, -9.1),
('1fdq', 3.1, 1.4, 51, 15, -4.9),
('1fep', 24.3, 1.1, 1, 0, -77.2),
('1ffj', 7.9, 0.8, 56, 5, -13.7),
('1fft', 29.5, 0.6, 12, 0, -82.3),
('1fh3', 3.6, 1.5, 83, 16, -5.2),
('1fho', 2.3, 1.2, 25, 14, -4.3),
('1fjr', 1.8, 1.5, 56, 13, -4.3),
('1fl7', 2.0, 1.6, 74, 9, -5.3),
('1fle', 4.4, 2.0, 52, 11, -6.3),
('1foe', 4.5, 1.1, 64, 7, -6.7),
('1fon', 2.1, 0.3, 85, 7, -9.0),
('1ftp', 4.5, 1.0, 53, 11, -5.2),
('1fu3', 6.5, 1.8, 25, 18, -8.3),
('1fyg', 2.9, 1.1, 76, 18, -3.5),
('1g1z', 6.5, 1.9, 72, 18, -8.7),
('1g2x', 3.8, 1.5, 84, 10, -5.4),
('1g4i', 1.9, 0.5, 87, 4, -7.4),
('1g5m', 4.2, 1.4, 33, 11, -6.6),
('1g5z', 3.6, 0.6, 2, 8, -7.0),
('1g7n', 2.7, 2.0, 49, 18, -4.3),
('1gcn', 5.3, 1.0, 78, 12, -6.6),
('1ggl', 3.3, 1.9, 53, 16, -4.9),
('1gmi', 2.9, 1.2, 46, 15, -5.9),
('1gmz', 3.8, 1.5, 88, 10, -6.7),
('1god', 3.0, 0.8, 80, 8, -7.4),
('1got', 4.9, 1.2, 61, 8, -7.0),
('1gox', 4.1, 0.0, 90, 0, -18.5),
('1gp7', 4.6, 1.0, 84, 12, -5.8),
('1gpl', 5.8, 1.0, 86, 9, -7.8),
('1gwy', 3.4, 1.9, 35, 15, -5.0),
('1gyg', 6.1, 2.0, 75, 6, -5.9),
('1gym', 4.9, 1.0, 67, 11, -7.2),
('1gz7', 4.8, 1.3, 87, 10, -8.5),
('1gzm', 32.2, 1.5, 11, 1, -75.6),
('1h0j', 7.1, 0.9, 59, 7, -11.3),
('1h2s', 30.5, 1.1, 0, 0, -123.4),
('1h3q', 3.3, 0.8, 14, 11, -6.3),
('1h68', 30.3, 1.5, 15, 2, -60.0),
('1h6h', 3.9, 2.0, 55, 14, -6.0),
('1h6i', 30.8, 1.1, 0, 0, -135.6),
('1h8p', 10.5, 0.9, 87, 7, -16.6),
('1h9f', 1.4, 1.1, 64, 16, -3.6),
('1hc9', 2.2, 1.5, 70, 16, -5.0),
('1hce', 3.5, 1.1, 60, 15, -1.6),
('1hci', 0.4, 0.7, 90, 12, -5.1),
('1hgz', 29.2, 2.3, 8, 7, -46.5),
('1hh4', 4.0, 0.6, 88, 6, -7.2),
('1hlg', 3.2, 1.4, 6, 12, -5.6),
('1hm6', 2.1, 0.9, 88, 7, -5.6),
('1hmt', 4.3, 1.6, 49, 12, -5.0),
('1hpi', 2.7, 1.0, 89, 12, -4.4),
('1hpl', 3.8, 0.3, 80, 5, -8.1),
('1hrc', 2.1, 1.0, 80, 16, -2.6),
('1hrk', 2.7, 0.1, 90, 0, -9.9),
('1hvf', 2.3, 1.5, 79, 10, -5.4),
('1hxi', 3.7, 1.0, 71, 5, -8.1),
('1hxx', 25.1, 1.0, 0, 0, -139.8),
('1hyi', 3.0, 2.0, 24, 17, -3.5),
('1i4a', 2.5, 1.1, 89, 3, -7.7),
('1i5p', 3.4, 1.2, 16, 12, -7.0),
('1i78', 26.5, 1.6, 5, 6, -46.9),
('1i7e', 3.8, 1.9, 75, 13, -4.7),
('1iaz', 3.0, 1.2, 44, 9, -5.1),
('1icm', 3.5, 1.5, 51, 18, -4.3),
('1icy', 6.4, 1.1, 73, 9, -8.2),
('1id2', 4.2, 1.3, 52, 8, -4.9),
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('3emo', 22.8, 1.9, 4, 0, -40.1),
('3eqm', 6.1, 1.2, 58, 8, -12.4),
('3f00', 1.4, 1.5, 29, 18, -3.3),
('3f5w', 29.2, 0.7, 0, 0, -83.5),
('3f7v', 30.1, 1.1, 0, 0, -95.2),
('3f7y', 31.3, 1.3, 0, 0, -82.3),
('3fb5', 33.7, 0.9, 0, 0, -115.9),
('3fdw', 3.0, 2.0, 71, 17, -3.6),
('3fg1', 3.5, 1.7, 87, 14, -9.5),
('3fh6', 29.9, 0.6, 3, 1, -97.8),
('3fhh', 24.6, 0.9, 5, 0, -70.7),
('3fid', 25.6, 2.0, 24, 0, -58.6),
('3fog', 3.4, 1.0, 69, 12, -4.9),
('3fsn', 7.8, 1.0, 73, 10, -10.3),
('3fwm', 29.9, 4.6, 23, 4, -18.9),
('3g1q', 8.1, 1.5, 62, 12, -10.8),
('3g49', 7.0, 0.5, 90, 1, -15.9),
('3g5u', 31.8, 1.2, 4, 0, -100.6),
('3g8g', 4.1, 0.9, 80, 6, -11.0),
('3g8h', 4.1, 1.1, 81, 8, -9.7),
('3gd8', 29.8, 1.1, 0, 1, -122.9),
('3gia', 29.9, 1.4, 11, 2, -92.1),
('3gp6', 24.7, 1.5, 40, 1, -32.5),
('3h1j', 28.2, 0.6, 0, 0, -184.8),
('3h28', 2.4, 0.1, 90, 0, -19.4),
('3h5m', 29.0, 0.8, 0, 0, -128.9),
('3h90', 29.6, 0.8, 0, 2, -83.9),
('3h9v', 27.6, 1.3, 0, 1, -61.3),
('3hd6', 31.8, 0.7, 0, 0, -174.1),
('3hd7', 28.5, 1.9, 3, 7, -29.3),
('3hde', 1.8, 1.4, 55, 10, -4.7),
('3hfx', 29.8, 0.8, 0, 0, -203.5),
('3hgc', 24.1, 0.7, 0, 0, -37.9),
('3hqk', 29.8, 1.0, 0, 0, -124.6),
('3hzq', 20.8, 1.2, 89, 0, -56.9),
('3hzs', 7.0, 1.1, 54, 9, -14.6),
('3i03', 2.5, 0.5, 76, 5, -10.6),
('3i65', 5.1, 1.0, 47, 6, -13.6),
('3i9v', 5.1, 14.0, 34, 10, -11.6),
('3jql', 6.2, 1.0, 85, 5, -7.0),
('3jqo', 8.3, 1.0, 82, 0, -6.3),
('3jty', 24.2, 1.2, 1, 0, -59.8),
('3jyc', 30.5, 1.4, 0, 1, -119.9),
('3k07', 27.4, 1.2, 0, 0, -166.7),
('3k3f', 29.4, 0.8, 0, 0, -124.4),
('3k9v', 6.6, 1.0, 49, 6, -9.6),
('3kbc', 28.1, 0.9, 0, 1, -158.8),
('3kcu', 29.9, 0.7, 0, 0, -160.9),
('3kdp', 31.4, 1.4, 7, 0, -95.3),
('3kg2', 31.8, 2.0, 0, 0, -93.0),
('3kly', 31.4, 0.5, 1, 0, -188.2),
('3kp9', 29.8, 1.6, 0, 0, -45.1),
('3kss', 28.8, 0.5, 0, 0, -147.7),
('3kvn', 24.4, 1.5, 4, 2, -48.7),
('3kwu', 3.3, 1.9, 67, 16, -3.6),
('3l1l', 28.8, 1.4, 2, 2, -132.0),
('3l4d', 8.4, 1.8, 66, 9, -12.6),
('3l7l', 6.9, 2.0, 35, 15, -10.8),
('3ld6', 8.9, 0.6, 57, 2, -16.8),
('3ldc', 29.8, 0.8, 0, 0, -72.4),
('3lll', 1.9, 0.4, 88, 1, -5.4),
('3llq', 29.8, 0.6, 0, 0, -134.5),
('3lnm', 31.1, 0.9, 0, 0, -260.7),
('3lut', 25.1, 0.5, 0, 0, -153.1),
('3m31', 1.9, 1.2, 27, 9, -6.2),
('3m73', 29.1, 1.4, 0, 0, -157.4),
('3m8d', 23.3, 0.8, 6, 1, -70.5),
('3mdm', 3.8, 1.3, 51, 8, -5.9),
('3mk7', 32.8, 1.2, 4, 4, -119.2),
('3mkt', 29.8, 1.1, 9, 0, -74.0),
('3mp7', 30.1, 1.0, 5, 6, -94.0),
('3n6o', 5.1, 1.4, 56, 10, -4.9),
('3ne2', 31.2, 1.3, 0, 0, -143.5),
('3nsj', 3.1, 1.0, 34, 11, -3.3),
('3nxu', 9.3, 1.0, 52, 12, -17.5),
('3ny8', 31.7, 1.2, 2, 3, -69.9),
('3o7q', 30.7, 1.3, 6, 0, -85.3),
('3odu', 31.2, 1.1, 0, 0, -129.5),
('3oe0', 32.2, 2.0, 5, 6, -133.2),
('3oe6', 35.3, 2.5, 8, 7, -79.7),
('3ohm', 7.5, 2.0, 39, 5, -6.9),
('3org', 28.7, 1.3, 0, 2, -140.4),
('3pbl', 33.0, 1.8, 8, 1, -56.6),
('3prn', 23.2, 0.5, 0, 0, -127.6),
('3tgl', 2.7, 1.1, 39, 7, -5.8),
('451c', 1.4, 0.9, 85, 10, -5.4),
('4p2p', 3.3, 0.8, 89, 7, -8.6),
('4tgl', 8.8, 0.9, 64, 11, -18.2),
('5lip', 9.0, 1.0, 46, 2, -30.6),
('5p2p', 1.6, 1.0, 89, 6, -7.7),
('7ahl', 23.5, 0.9, 0, 1, -49.3),
('9pcy', 1.8, 1.6, 18, 19, -1.9),
('3lbw', 31.1, 1.7, 7, 10, -50.5),
('1nl2', 8.9, 1.9, 5, 19, -8.8),
('1mic', 23.2, 3.8, 32, 7, -19.9),
('2xdc', 22.2, 3.0, 36, 3, -27.2),
('2izq', 23.8, 4.5, 24, 9, -18.1),
('1grm', 23.2, 1.7, 11, 11, -27.4),
('1aj1', 3.0, 1.3, 90, 16, -5.6),
('1amt', 30.0, 5.2, 71, 11, -16.7),
('1cwa', 10.3, 1.2, 84, 18, -8.1),
('1d6x', 9.8, 1.1, 78, 19, -7.8),
('1edn', 4.3, 1.2, 72, 15, -5.4),
('1ee7', 9.6, 1.5, 82, 17, -12.8),
('1etn', 2.9, 2.0, 37, 18, -2.1),
('1g92', 10.1, 0.5, 54, 5, -11.0),
('1grm', 23.2, 1.7, 11, 11, -27.4),
('1ih9', 11.4, 1.3, 89, 13, -11.8),
('1joh', 10.3, 1.9, 87, 19, -11.0),
('1mqx', 2.1, 1.4, 87, 16, -3.0),
('1mqy', 5.2, 1.2, 89, 19, -6.1),
('1mqz', 3.9, 1.9, 83, 19, -4.3),
('1ob4', 15.3, 1.8, 56, 19, -14.0),
('1ob6', 15.0, 1.6, 48, 16, -14.6),
('1ob7', 31.1, 4.7, 53, 13, -13.0),
('1p0l', 5.2, 0.8, 79, 10, -10.0),
('1pxq', 7.5, 0.9, 87, 10, -9.3),
('1q71', 3.7, 1.6, 74, 16, -5.3),
('1qow', 3.1, 1.5, 72, 18, -5.5),
('1qvl', 4.2, 1.4, 84, 18, -6.4),
('1qx9', 6.4, 1.2, 47, 11, -7.5),
('1rpb', 4.1, 1.3, 86, 14, -8.4),
('1s7p', 4.7, 1.2, 83, 18, -5.7),
('1soc', 8.5, 1.8, 76, 19, -6.9),
('1t5m', 2.9, 1.1, 32, 11, -7.9),
('1t5n', 8.6, 2.0, 22, 16, -8.8),
('1tk2', 6.9, 1.9, 88, 19, -8.4),
('1w3m', 8.2, 1.9, 69, 12, -9.1),
('1wco', 7.1, 1.4, 90, 11, -6.5),
('1x22', 3.5, 0.9, 69, 8, -9.5),
('1xt7', 9.3, 1.8, 15, 15, -6.3),
('2dde', 3.6, 1.6, 30, 19, -5.5),
('3cay', 14.5, 1.1, 77, 15, -16.0),
('1btn', 13.7, 1.6, 57, 19, -17.3),
('1bwn', 15.3, 0.5, 90, 10, -33.3),
('1fhx', 15.0, 1.2, 18, 15, -16.4),
('1gc6', 15.4, 1.8, 17, 12, -17.9),
('1hfa', 14.2, 2.0, 44, 14, -17.9),
('1joc', 15.0, 0.4, 2, 11, -34.0),
('1mai', 15.0, 1.8, 22, 14, -17.8),
('1nu2', 14.8, 1.1, 46, 12, -17.6),
('1o7k', 15.2, 1.7, 60, 15, -18.4),
('1ocu', 15.3, 0.8, 88, 6, -34.9),
('1dsy', 0.9, 1.5, 18, 16, -3.0),
('1h0a', 3.2, 1.1, 39, 19, -5.3),
('1eys', 31.6, 1.0, 2, 0, -116.0),
('1rzh', 31.4, 0.7, 3, 0, -127.9),
('1dxr', 31.8, 0.7, 5, 0, -121.8),
('1jb0', 31.4, 0.4, 1, 0, -285.7),
('2o01', 26.9, 0.0, 3, 0, -269.9),
('3bz1', 31.6, 0.4, 0, 0, -409.7),
('3a0b', 31.8, 0.4, 0, 0, -397.1),
('1nkz', 31.8, 0.6, 0, 0, -193.5),
('1ijd', 29.8, 0.7, 0, 0, -174.6),
('1lgh', 29.7, 0.5, 0, 0, -163.4),
('1rwt', 30.0, 0.7, 0, 0, -154.0),
('2bhw', 29.4, 1.0, 0, 0, -123.2),
('3kzi', 31.8, 0.5, 0, 0, -310.1);

-- --------------------------------------------------------

--
-- Table structure for table `temp_subunits`
--

CREATE TABLE `temp_subunits` (
  `pdbid` varchar(4) NOT NULL,
  `letter` char(2) NOT NULL,
  `tilt` int(3) NOT NULL,
  `segment` text NOT NULL
) ENGINE=MyISAM DEFAULT CHARSET=latin1;

--
-- Dumping data for table `temp_subunits`
--

INSERT INTO `temp_subunits` (`pdbid`, `letter`, `tilt`, `segment`) VALUES
('1a0s', 'P', 1, '1(75-86),2(116-124),3(136-145),4(162-167),5(181-186),6(208-213),7(223-230),8(244-253),9(256-263),10(287-296),11(306-314),12(336-344),13(351-360),14(374-383),15(389-398),16(417-426),17(438-447),18(473-482)'),
('1a0s', 'Q', 2, '1(75-86),2(116-124),3(136-145),4(158-167),5(182-186),6(208-213),7(223-230),8(243-253),9(256-263),10(287-296),11(306-314),12(336-344),13(351-360),14(374-383),15(389-398),16(417-426),17(438-447),18(473-482)'),
('1a0s', 'R', 1, '1(75-86),2(116-124),3(136-145),4(162-167),5(181-186),6(208-213),7(223-230),8(244-253),9(256-263),10(287-296),11(306-314),12(336-345),13(351-360),14(374-383),15(389-398),16(417-426),17(438-447),18(473-482)'),
('1a91', 'A', 21, '1(8-36),2(51-75)'),
('1af6', 'A', 2, '1(2-13),2(39-48),3(58-68),4(75-88),5(98-103),6(125-132),7(138-146),8(170-179),9(185-194),10(213-221),11(227-235),12(269-278),13(284-293),14(305-314),15(320-329),16(343-352),17(361-370),18(411-420)'),
('1af6', 'B', 2, '1(2-13),2(39-48),3(58-68),4(75-88),5(98-103),6(125-132),7(138-146),8(170-179),9(185-194),10(213-221),11(227-235),12(269-278),13(284-293),14(305-314),15(320-329),16(343-352),17(361-370),18(411-420)'),
('1af6', 'C', 2, '1(2-13),2(39-48),3(58-68),4(75-88),5(98-103),6(125-132),7(138-146),8(170-179),9(185-194),10(213-221),11(227-235),12(269-278),13(284-293),14(305-314),15(320-329),16(343-352),17(361-370),18(411-420)'),
('1afo', 'A', 19, '1(72-93)'),
('1afo', 'B', 20, '1(72-94)'),
('1ar1', 'A', 7, '1(31-55),2(90-113),3(129-151),4(178-202),5(219-247),6(269-294),7(305-326),8(338-363),9(371-394),10(407-429),11(443-464),12(488-512)'),
('1ar1', 'B', 14, '1(37-60),2(75-94)'),
('1c17', 'A', 3, '1(8-32),2(52-75)'),
('1c17', 'B', 4, '1(8-32),2(53-75)'),
('1c17', 'C', 6, '1(8-31),2(53-75)'),
('1c17', 'D', 8, '1(8-31),2(55-77)'),
('1c17', 'E', 8, '1(7-31),2(55-78)'),
('1c17', 'F', 8, '1(7-31),2(55-78)'),
('1c17', 'G', 8, '1(7-31),2(55-78)'),
('1c17', 'H', 7, '1(8-31),2(53-77)'),
('1c17', 'I', 7, '1(8-32),2(53-75)'),
('1c17', 'J', 5, '1(8-32),2(52-75)'),
('1c17', 'K', 3, '1(8-32),2(52-75)'),
('1c17', 'L', 4, '1(8-32),2(51-76)'),
('1c17', 'M', 10, '1(101-124),2(142-166),3(201-223),4(241-262)'),
('1e12', 'A', 13, '1(27-50),2(63-82),3(106-123),4(134-153),5(159-180),6(199-221),7(227-250)'),
('1e12', 'B', 13, '1(27-50),2(63-82),3(106-123),4(134-153),5(159-180),6(199-221),7(227-250)'),
('1e12', 'C', 13, '1(27-50),2(63-82),3(106-123),4(134-153),5(159-180),6(199-221),7(227-250)'),
('1e54', 'A', 5, '1(6-17),2(27-31),3(37-43),4(53-62),5(76-82),6(136-143),7(148-156),8(171-179),9(183-192),10(205-213),11(217-225),12(240-249),13(253-262),14(273-281),15(286-294),16(322-331)'),
('1e54', 'C', 5, '1(6-17),2(27-31),3(37-43),4(53-62),5(76-82),6(136-143),7(148-156),8(171-179),9(183-192),10(205-213),11(217-225),12(240-249),13(253-262),14(273-281),15(286-294),16(322-331)'),
('1e54', 'E', 5, '1(6-17),2(27-31),3(37-43),4(53-62),5(76-82),6(136-143),7(148-156),8(171-179),9(183-192),10(205-213),11(217-225),12(240-249),13(253-262),14(273-281),15(286-294),16(322-331)'),
('1ehk', 'A', 7, '1(20-47),2(67-90),3(104-125),4(143-164),5(186-210),6(223-248),7(267-280),8(292-314),9(347-367),10(379-402),11(419-444),12(465-493),13(527-550)'),
('1ehk', 'B', 9, '1(15-37)'),
('1ehk', 'C', 9, '1(8-29)'),
('1ek9', 'A', 51, '1(40-50),2(65-77),3(246-256),4(282-290)'),
('1ek9', 'C', 51, '1(40-50),2(65-77),3(246-256),4(282-290)'),
('1ek9', 'B', 51, '1(40-50),2(65-77),3(246-256),4(282-290)'),
('1fep', 'A', 0, '1(153-163),2(172-183),3(187-196),4(231-240),5(245-254),6(288-295),7(302-309),8(345-353),9(361-369),10(410-418),11(424-433),12(442-451),13(456-465),14(509-517),15(521-529),16(565-574),17(578-586),18(606-615),19(619-627),20(655-664),21(669-676),22(715-723)'),
('1fft', 'A', 6, '1(57-80),2(103-124),3(140-161),4(189-210),5(231-252),6(277-298),7(318-325),8(344-367),9(382-402),10(414-436),11(451-473),12(497-518)'),
('1fft', 'B', 16, '1(45-65),2(89-109)'),
('1fft', 'C', 20, '1(25-45),2(67-85),3(96-116),4(141-165),5(176-197)'),
('1gzm', 'A', 11, '1(35-63),2(74-99),3(109-133),4(153-172),5(202-224),6(253-276),7(286-308)'),
('1h2s', 'A', 8, '1(3-24),2(38-57),3(70-87),4(98-117),5(122-141),6(163-180),7(190-211)'),
('1h2s', 'B', 3, '1(24-41),2(60-81)'),
('1h2s', 'C', 3, '1(24-41),2(60-81)'),
('1h2s', 'D', 8, '1(3-24),2(38-57),3(70-87),4(98-117),5(122-141),6(163-180),7(190-211)'),
('1h68', 'A', 14, '1(3-24),2(37-56),3(70-87),4(98-117),5(121-141),6(165-180),7(190-211)'),
('1h6i', 'A', 8, '1(11-32),2(50-68),3(77-87),4(92-113),5(135-156),6(168-186),7(193-202),8(210-231)'),
('1h6i', 'B', 8, '1(11-32),2(50-68),3(77-87),4(92-113),5(135-156),6(168-186),7(193-202),8(210-231)'),
('1h6i', 'C', 8, '1(11-32),2(50-68),3(77-87),4(92-113),5(135-156),6(168-186),7(193-202),8(210-231)'),
('1h6i', 'D', 8, '1(11-32),2(50-68),3(77-87),4(92-113),5(135-156),6(168-186),7(193-202),8(210-231)'),
('1hgz', 'A', 13, '1(13-35)'),
('1hgz', 'B', 18, '1(16-37)'),
('1hgz', 'C', 27, '1(16-37)'),
('1hgz', 'D', 29, '1(16-38)'),
('1hgz', 'E', 22, '1(17-41)'),
('1hgz', 'F', 13, '1(22-45)'),
('1hgz', 'G', 17, '1(27-45)'),
('1hgz', 'H', 27, '1(28-45)'),
('1hgz', 'I', 34, '1(27-45)'),
('1hgz', 'J', 31, '1(28-45)'),
('1hgz', 'K', 18, '1(32-45)'),
('1hgz', 'L', 16, '1(36-45)'),
('1hgz', 'M', 18, '1(38-45)'),
('1hgz', 'N', 27, '1(38-45)'),
('1hgz', 'O', 32, '1(39-45)'),
('1hxx', 'A', 3, '1(11-23),2(39-49),3(55-66),4(79-90),5(94-99),6(135-142),7(151-158),8(173-182),9(185-192),10(214-222),11(225-232),12(257-265),13(269-276),14(294-302),15(307-315),16(332-339)'),
('1hxx', 'B', 3, '1(11-23),2(39-49),3(55-66),4(79-90),5(94-99),6(135-142),7(151-158),8(173-182),9(185-192),10(214-222),11(225-232),12(257-265),13(269-276),14(294-302),15(307-315),16(332-339)'),
('1hxx', 'C', 3, '1(11-23),2(39-49),3(55-66),4(79-90),5(94-99),6(135-142),7(151-158),8(173-182),9(185-192),10(214-222),11(225-232),12(257-265),13(269-276),14(294-302),15(307-315),16(332-339)'),
('1i78', 'A', 3, '1(11-20),2(50-61),3(64-72),4(111-121),5(126-136),6(178-187),7(192-201),8(230-240),9(245-254),10(287-296)'),
('1ifi', 'A', 20, '1(18-44)'),
('1ifi', 'B', 20, '1(18-44)'),
('1ifi', 'C', 20, '1(18-44)'),
('1ifi', 'D', 20, '1(18-44)'),
('1ifi', 'E', 20, '1(18-44)'),
('1ifi', 'F', 19, '1(30-49)'),
('1ifi', 'G', 19, '1(30-49)'),
('1ifi', 'H', 19, '1(30-49)'),
('1ifi', 'I', 19, '1(30-49)'),
('1ifi', 'J', 19, '1(30-49)'),
('1ifi', 'K', 18, '1(41-49)'),
('1ifi', 'L', 18, '1(41-49)'),
('1ifi', 'M', 18, '1(41-49)'),
('1ifi', 'N', 18, '1(41-49)'),
('1ifi', 'O', 18, '1(41-49)'),
('1ifk', 'A', 20, '1(19-41)'),
('1ifk', 'B', 20, '1(19-41)'),
('1ifk', 'C', 20, '1(19-41)'),
('1ifk', 'D', 20, '1(19-41)'),
('1ifk', 'E', 20, '1(19-41)'),
('1ifk', 'F', 20, '1(31-50)'),
('1ifk', 'G', 20, '1(31-50)'),
('1ifk', 'H', 20, '1(31-50)'),
('1ifk', 'I', 20, '1(31-50)'),
('1ifk', 'J', 20, '1(31-50)'),
('1ifk', 'K', 21, '1(42-50)'),
('1ifk', 'L', 21, '1(42-50)'),
('1ifk', 'M', 21, '1(42-50)'),
('1ifk', 'N', 21, '1(42-50)'),
('1ifk', 'O', 21, '1(42-50)'),
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('2r6g', 'F', 18, '1(17-35),2(40-57),3(65-88),4(277-306),5(314-326),6(366-391),7(424-439),8(489-503)'),
('2r6g', 'G', 18, '1(14-36),2(81-107),3(118-130),4(159-178),5(214-228),6(264-282)'),
('2r9r', 'B', 20, '1(160-184),2(221-243),3(254-272),4(287-306),5(320-346),6(357-369),7(381-403)'),
('2r9r', 'D', 20, '1(160-184),2(221-243),3(254-272),4(287-306),5(320-346),6(357-369),7(381-403)'),
('2r9r', 'F', 20, '1(160-184),2(221-243),3(254-272),4(287-306),5(320-346),6(357-369),7(381-403)'),
('2r9r', 'H', 21, '1(160-184),2(221-243),3(254-272),4(287-306),5(320-346),6(357-369),7(381-403)'),
('2rdd', 'A', 5, '1(10-26),2(340-358),3(363-382),4(397-414),5(438-456),6(471-493),7(539-556),8(875-892),9(896-918),10(927-947),11(971-991),12(1003-1026)'),
('2rdd', 'B', 5, '1(10-26),2(340-358),3(363-382),4(397-414),5(438-456),6(471-493),7(539-556),8(875-892),9(896-918),10(927-947),11(971-991),12(1003-1026)'),
('2rdd', 'C', 5, '1(10-26),2(340-358),3(363-382),4(397-414),5(438-456),6(471-493),7(539-556),8(875-892),9(896-918),10(927-947),11(971-991),12(1003-1026)'),
('2rdd', 'D', 60, '1(21-51)'),
('2rdd', 'E', 61, '1(21-51)'),
('2rdd', 'F', 60, '1(21-51)'),
('2rh1', 'C', 5, '1(31-56),2(70-92),3(104-129),4(150-171),5(198-220),6(275-298),7(306-327)'),
('2rh1', 'D', 5, '1(31-56),2(70-92),3(104-129),4(150-171),5(198-220),6(275-298),7(306-327)'),
('2rlf', 'A', 33, '1(25-46)'),
('2rlf', 'B', 25, '1(25-46)'),
('2rlf', 'C', 1, '1(25-45)'),
('2rlf', 'D', 21, '1(25-46)'),
('2uuh', 'A', 19, '1(4-24),2(56-73),3(76-92),4(107-131)'),
('2uuh', 'B', 19, '1(4-24),2(56-73),3(76-92),4(107-131)'),
('2uuh', 'C', 19, '1(4-24),2(56-73),3(76-92),4(107-131)'),
('2v50', 'A', 2, '1(9-28),2(340-359),3(362-386),4(394-412),5(440-458),6(467-490),7(539-557),8(873-891),9(895-918),10(926-944),11(972-988),12(998-1020)'),
('2v50', 'B', 4, '1(9-27),2(340-358),3(362-383),4(397-414),5(438-456),6(471-493),7(539-557),8(873-891),9(895-917),10(926-946),11(969-988),12(1001-1024)'),
('2v50', 'C', 3, '1(10-28),2(341-359),3(362-386),4(394-413),5(439-458),6(470-490),7(539-556),8(873-891),9(895-918),10(926-946),11(970-988),12(1001-1024)'),
('2vl0', 'A', 10, '1(204-223),2(228-249),3(260-281),4(299-315)'),
('2vl0', 'B', 10, '1(204-223),2(228-249),3(260-281),4(299-315)'),
('2vl0', 'C', 10, '1(203-223),2(228-249),3(260-281),4(299-315)'),
('2vl0', 'D', 10, '1(203-223),2(229-249),3(260-281),4(299-315)'),
('2vl0', 'E', 10, '1(204-223),2(228-249),3(260-281),4(299-315)'),
('2vpz', 'C', 11, '1(16-37),2(49-67),3(88-108),4(114-136),5(146-167),6(173-193),7(208-221),8(226-244)'),
('2vpz', 'G', 13, '1(15-39),2(48-66),3(87-107),4(113-135),5(145-166),6(172-192),7(207-220),8(224-243)'),
('2vqi', 'A', 1, '1(148-155),2(168-177),3(181-189),4(206-216),5(222-228),6(242-248),7(336-343),8(357-366),9(370-378),10(384-392),11(398-404),12(420-428),13(436-442),14(470-478),15(484-492),16(503-512),17(520-527),18(538-545),19(550-558),20(564-573),21(578-586),22(597-606),23(609-617),24(624-634)'),
('2vt4', 'B', 4, '1(42-64),2(78-103),3(112-137),4(158-179),5(205-228),6(292-315),7(323-344)'),
('2vv5', 'A', 28, '1(26-52),2(73-89),3(94-101)'),
('2vv5', 'B', 28, '1(26-52),2(73-89),3(94-101)'),
('2vv5', 'C', 28, '1(26-52),2(73-90),3(94-101)'),
('2vv5', 'D', 28, '1(26-52),2(73-89),3(94-101)'),
('2vv5', 'E', 28, '1(26-52),2(73-89),3(94-101)'),
('2vv5', 'F', 28, '1(26-52),2(73-89),3(94-101)'),
('2vv5', 'G', 28, '1(26-52),2(73-89),3(94-101)'),
('2w2e', 'A', 9, '1(44-66),2(86-105),3(113-122),4(127-148),5(171-191),6(197-216),7(225-234),8(242-266)'),
('2w2e', 'B', 9, '1(44-66),2(86-105),3(113-122),4(127-148),5(171-191),6(197-216),7(225-234),8(242-266)'),
('2w2e', 'C', 9, '1(44-66),2(86-105),3(113-122),4(127-148),5(171-191),6(197-216),7(225-234),8(242-266)'),
('2w2e', 'D', 9, '1(44-66),2(86-105),3(113-122),4(127-148),5(171-191),6(197-216),7(225-234),8(242-266)'),
('2w5j', 'A', 3, '1(12-32),2(53-77)');
INSERT INTO `temp_subunits` (`pdbid`, `letter`, `tilt`, `segment`) VALUES
('2w5j', 'B', 3, '1(12-32),2(53-77)'),
('2w5j', 'C', 3, '1(12-32),2(53-77)'),
('2w5j', 'D', 3, '1(12-32),2(53-77)'),
('2w5j', 'E', 3, '1(12-32),2(53-77)'),
('2w5j', 'F', 3, '1(12-32),2(53-77)'),
('2w5j', 'G', 3, '1(12-32),2(53-77)'),
('2w5j', 'H', 3, '1(12-32),2(53-77)'),
('2w5j', 'I', 3, '1(12-32),2(53-77)'),
('2w5j', 'J', 3, '1(12-32),2(53-77)'),
('2w5j', 'K', 3, '1(12-32),2(53-77)'),
('2w5j', 'L', 3, '1(12-32),2(53-77)'),
('2w5j', 'M', 3, '1(12-32),2(53-77)'),
('2w5j', 'V', 3, '1(12-32),2(53-77)'),
('2w8a', 'A', 10, '1(60-78),2(100-118),3(142-149),4(152-162),5(178-201),6(236-262),7(280-296),8(301-323),9(362-385),10(397-419),11(452-480),12(489-509),13(515-538)'),
('2w8a', 'B', 10, '1(60-78),2(100-118),3(142-149),4(152-162),5(178-201),6(236-262),7(280-296),8(301-323),9(362-385),10(397-419),11(452-480),12(489-509),13(517-538)'),
('2w8a', 'C', 10, '1(60-78),2(100-118),3(142-149),4(152-162),5(178-201),6(236-262),7(280-296),8(301-323),9(362-385),10(397-419),11(452-480),12(489-509),13(517-538)'),
('2wcd', 'A', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'B', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'C', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'D', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'E', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'F', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'G', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'H', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'I', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'J', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'K', 15, '1(10-35),2(175-186),3(189-202)'),
('2wcd', 'L', 15, '1(10-35),2(175-186),3(189-202)'),
('2wie', 'A', 5, '1(12-33),2(54-77)'),
('2wie', 'B', 5, '1(12-33),2(54-77)'),
('2wie', 'C', 5, '1(12-33),2(54-77)'),
('2wie', 'D', 5, '1(12-33),2(54-77)'),
('2wie', 'E', 5, '1(12-33),2(54-77)'),
('2wie', 'F', 5, '1(12-33),2(54-77)'),
('2wie', 'G', 5, '1(12-33),2(54-77)'),
('2wie', 'H', 5, '1(12-33),2(54-77)'),
('2wie', 'I', 5, '1(12-33),2(54-77)'),
('2wie', 'J', 5, '1(12-33),2(54-77)'),
('2wie', 'K', 5, '1(12-33),2(54-77)'),
('2wie', 'L', 5, '1(12-33),2(54-77)'),
('2wie', 'M', 5, '1(12-33),2(54-77)'),
('2wie', 'N', 5, '1(12-33),2(54-77)'),
('2wie', 'O', 5, '1(12-33),2(54-77)'),
('2wjr', 'A', 3, '1(3-9),2(17-26),3(30-38),4(54-63),5(69-79),6(85-94),7(100-109),8(129-136),9(142-150),10(168-177),11(181-189),12(206-213)'),
('2wlh', 'A', 37, '1(46-71),2(108-131)'),
('2wlh', 'C', 37, '1(46-71),2(108-131)'),
('2wlh', 'E', 37, '1(46-71),2(108-131)'),
('2wlh', 'G', 37, '1(46-71),2(108-131)'),
('2wlj', 'A', 36, '1(46-71),2(107-131)'),
('2wlj', 'F', 36, '1(46-71),2(108-131)'),
('2wlj', 'G', 36, '1(46-71),2(108-131)'),
('2wlj', 'L', 36, '1(46-71),2(108-131)'),
('2wlk', 'A', 36, '1(46-71),2(107-131)'),
('2wlk', 'D', 36, '1(46-71),2(107-131)'),
('2wlk', 'E', 36, '1(46-71),2(107-131)'),
('2wlk', 'H', 36, '1(46-71),2(107-131)'),
('2wll', 'A', 36, '1(60-84),2(121-145)'),
('2wll', 'D', 36, '1(60-84),2(121-145)'),
('2wll', 'E', 36, '1(60-84),2(121-145)'),
('2wll', 'H', 36, '1(60-84),2(121-145)'),
('2wpd', 'J', 3, '1(11-34),2(48-74)'),
('2wpd', 'K', 4, '1(11-34),2(48-74)'),
('2wpd', 'L', 4, '1(11-34),2(48-74)'),
('2wpd', 'M', 4, '1(11-34),2(47-74)'),
('2wpd', 'N', 4, '1(11-34),2(48-74)'),
('2wpd', 'O', 4, '1(11-34),2(48-74)'),
('2wpd', 'P', 4, '1(11-34),2(48-74)'),
('2wpd', 'Q', 4, '1(11-34),2(47-74)'),
('2wpd', 'R', 5, '1(11-34),2(47-74)'),
('2wpd', 'S', 4, '1(11-34),2(47-74)'),
('2wsw', 'A', 14, '1(13-30),2(52-67),3(92-98),4(102-112),5(132-142),6(144-154),7(187-216),8(231-248),9(254-277),10(312-335),11(348-370),12(404-433),13(447-464),14(469-492)'),
('2wsw', 'B', 14, '1(13-30),2(52-67),3(92-98),4(102-112),5(132-142),6(144-154),7(187-216),8(231-248),9(254-277),10(312-335),11(348-370),12(404-433),13(447-464),14(469-492)'),
('2wsw', 'C', 13, '1(13-30),2(52-67),3(92-98),4(102-112),5(132-142),6(144-154),7(187-216),8(231-248),9(254-277),10(312-335),11(348-370),12(404-433),13(447-464),14(469-492)'),
('2wsx', 'A', 22, '1(12-30),2(42-67),3(92-99),4(102-112),5(132-142),6(144-151),7(187-216),8(231-277),9(279-302),10(312-335),11(350-369),12(406-434),13(446-464),14(471-491)'),
('2wsx', 'C', 13, '1(12-30),2(42-67),3(92-99),4(102-112),5(132-142),6(144-151),7(187-216),8(232-277),9(279-302),10(312-335),11(350-369),12(406-434),13(446-464),14(471-491)'),
('2wsx', 'B', 13, '1(12-30),2(42-67),3(92-99),4(102-112),5(132-142),6(144-151),7(187-216),8(232-277),9(279-302),10(312-335),11(350-369),12(406-434),13(446-464),14(471-491)'),
('2x2v', 'A', 5, '1(4-26),2(46-68)'),
('2x2v', 'B', 4, '1(4-26),2(46-68)'),
('2x2v', 'C', 5, '1(4-26),2(46-68)'),
('2x2v', 'D', 4, '1(4-26),2(46-68)'),
('2x2v', 'E', 4, '1(3-26),2(46-68)'),
('2x2v', 'F', 4, '1(3-26),2(46-68)'),
('2x2v', 'G', 4, '1(3-26),2(46-68)'),
('2x2v', 'H', 4, '1(3-26),2(46-68)'),
('2x2v', 'I', 4, '1(3-26),2(46-68)'),
('2x2v', 'J', 4, '1(3-26),2(46-68)'),
('2x2v', 'K', 5, '1(4-26),2(46-68)'),
('2x2v', 'L', 5, '1(4-26),2(46-68)'),
('2x2v', 'M', 5, '1(4-26),2(46-68)'),
('2x55', 'A', 2, '1(13-22),2(51-60),3(65-73),4(111-121),5(126-136),6(174-183),7(188-197),8(224-235),9(239-248),10(282-292)'),
('2x79', 'A', 14, '1(30-40),2(58-80),3(102-133),4(143-158),5(161-185),6(209-227),7(252-274),8(297-326),9(336-349),10(360-379),11(409-423),12(429-444)'),
('2xok', 'K', 5, '1(12-35),2(47-71)'),
('2xok', 'S', 6, '1(12-35),2(47-70)'),
('2xok', 'T', 5, '1(12-35),2(48-70)'),
('2xok', 'L', 4, '1(12-34),2(48-71)'),
('2xok', 'M', 4, '1(12-34),2(48-71)'),
('2xok', 'N', 4, '1(12-35),2(48-71)'),
('2xok', 'O', 4, '1(12-35),2(48-71)'),
('2xok', 'P', 4, '1(12-35),2(48-71)'),
('2xok', 'Q', 4, '1(12-35),2(47-71)'),
('2xok', 'R', 6, '1(12-35),2(47-70)'),
('2xow', 'A', 15, '1(95-114),2(148-166),3(171-192),4(201-214),5(228-242),6(252-269)'),
('2xqu', 'A', 5, '1(12-33),2(54-77)'),
('2xqu', 'B', 5, '1(12-33),2(54-77)'),
('2xqu', 'C', 5, '1(12-33),2(54-77)'),
('2xqu', 'E', 5, '1(12-33),2(54-77)'),
('2xqu', 'D', 5, '1(12-33),2(54-77)'),
('2xqu', 'F', 5, '1(12-33),2(54-77)'),
('2xqu', 'G', 5, '1(12-33),2(54-77)'),
('2xqu', 'H', 5, '1(12-33),2(54-77)'),
('2xqu', 'I', 5, '1(12-33),2(54-77)'),
('2xqu', 'J', 5, '1(12-33),2(54-77)'),
('2xqu', 'K', 5, '1(12-33),2(54-77)'),
('2xqu', 'L', 5, '1(12-33),2(54-77)'),
('2xqu', 'M', 5, '1(12-33),2(54-77)'),
('2xqu', 'N', 5, '1(12-33),2(54-77)'),
('2xqu', 'O', 5, '1(12-33),2(54-77)'),
('2ysu', 'A', 2, '1(136-146),2(149-158),3(164-173),4(199-208),5(214-223),6(248-257),7(261-270),8(296-304),9(309-317),10(338-348),11(351-359),12(370-378),13(383-391),14(417-426),15(429-436),16(463-472),17(475-483),18(502-510),19(514-522),20(545-554),21(559-566),22(585-593)'),
('2yvx', 'A', 19, '1(277-306),2(319-336),3(355-381),4(388-412),5(424-443)'),
('2yvx', 'B', 19, '1(277-306),2(319-336),3(355-381),4(388-412),5(424-443)'),
('2yxr', 'A', 5, '1(28-42),2(77-88),3(110-129),4(140-161),5(169-187),6(209-228),7(255-276),8(313-331),9(381-395),10(401-411)'),
('2yxr', 'B', 44, '1(33-62)'),
('2yxr', 'C', 4, '1(30-48)'),
('2z73', 'A', 4, '1(32-57),2(72-97),3(106-131),4(152-172),5(197-221),6(262-286),7(295-317)'),
('2z73', 'B', 4, '1(32-57),2(72-97),3(106-131),4(152-172),5(197-221),6(262-286),7(295-317)'),
('2ziy', 'A', 9, '1(32-57),2(71-97),3(106-131),4(152-172),5(198-221),6(262-286),7(295-316)'),
('2zjs', 'Y', 3, '1(18-33),2(77-90),3(113-135),4(151-175),5(183-204),6(214-235),7(272-290),8(309-326),9(369-388),10(398-412)'),
('2zjs', 'E', 53, '1(27-56)'),
('2zt9', 'A', 23, '1(32-53),2(84-107),3(115-134),4(185-207)'),
('2zt9', 'B', 3, '1(35-57),2(95-115),3(127-146)'),
('2zt9', 'C', 2, '1(256-276)'),
('2zt9', 'D', 25, '1(17-39)'),
('2zt9', 'G', 12, '1(5-26)'),
('2zt9', 'H', 12, '1(5-26)'),
('2zt9', 'F', 33, '1(5-29)'),
('2zt9', 'E', 34, '1(2-25)'),
('2zt9', 'I', 23, '1(32-53),2(84-107),3(115-134),4(185-207)'),
('2zt9', 'J', 2, '1(35-57),2(95-116),3(127-146)'),
('2zt9', 'K', 25, '1(18-40)'),
('2zt9', 'L', 3, '1(256-276)'),
('2zt9', 'M', 13, '1(5-26)'),
('2zt9', 'N', 12, '1(5-26)'),
('2zt9', 'O', 32, '1(5-29)'),
('2zt9', 'P', 33, '1(2-25)'),
('2zup', 'B', 6, '1(15-27),2(49-63),3(71-85)'),
('2zup', 'C', 8, '1(148-161)'),
('2zuq', 'A', 26, '1(12-32),2(47-62),3(68-86),4(144-161)'),
('2zw3', 'A', 19, '1(22-45),2(73-93),3(136-157),4(187-212)'),
('2zw3', 'B', 18, '1(22-45),2(73-93),3(136-157),4(187-211)'),
('2zw3', 'C', 18, '1(22-45),2(73-93),3(136-157),4(187-211)'),
('2zw3', 'D', 18, '1(22-45),2(73-93),3(136-157),4(187-211)'),
('2zw3', 'E', 18, '1(22-45),2(73-93),3(136-157),4(187-211)'),
('2zw3', 'F', 18, '1(22-45),2(73-93),3(136-157),4(187-211)'),
('2zxe', 'A', 13, '1(99-115),2(128-149),3(291-313),4(319-331),5(334-343),6(774-795),7(804-822),8(849-872),9(917-938),10(952-970),11(985-1005)'),
('2zxe', 'B', 36, '1(33-61)'),
('2zxe', 'G', 11, '1(21-39)'),
('2zz9', 'A', 5, '1(34-56),2(70-90),3(98-107),4(112-133),5(156-177),6(189-204),7(231-252)'),
('2zz9', 'G', 5, '1(34-56),2(70-90),3(98-107),4(112-136),5(156-177),6(189-204),7(231-252)'),
('2zz9', 'M', 5, '1(34-56),2(70-90),3(98-107),4(112-133),5(156-177),6(189-204),7(231-252)'),
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('3jyc', 'D', 31, '1(82-107),2(130-141),3(156-177)'),
('3k07', 'A', 2, '1(13-32),2(339-357),3(360-381),4(394-411),5(447-465),6(479-501),7(874-891),8(894-918),9(927-946),10(983-1000),11(1012-1031)'),
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('3k07', 'C', 1, '1(12-32),2(339-357),3(360-381),4(394-411),5(447-465),6(479-501),7(874-891),8(894-918),9(927-946),10(983-1000),11(1012-1031)'),
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('3k3f', 'U', 10, '1(31-44),2(46-66),3(77-92),4(97-117),5(131-144),6(194-207),7(209-229),8(240-254),9(261-286),10(295-307)'),
('3kbc', 'A', 16, '1(12-29),2(42-71),3(86-106),4(151-165),5(186-217),6(224-250),7(312-326),8(335-351),9(358-370),10(379-401)'),
('3kbc', 'B', 17, '1(12-29),2(42-71),3(86-106),4(151-165),5(186-217),6(224-250),7(312-326),8(335-351),9(358-370),10(379-401)'),
('3kbc', 'C', 16, '1(12-29),2(42-71),3(86-106),4(151-165),5(186-217),6(224-250),7(312-326),8(335-351),9(358-370),10(379-401)'),
('3kcu', 'A', 8, '1(31-56),2(65-85),3(113-135),4(161-181),5(188-205),6(210-219),7(250-276)'),
('3kcu', 'B', 8, '1(31-56),2(65-85),3(113-135),4(161-181),5(188-205),6(210-219),7(250-276)'),
('3kcu', 'C', 8, '1(31-56),2(65-85),3(113-135),4(161-181),5(188-205),6(210-219),7(250-275)'),
('3kcu', 'D', 9, '1(31-56),2(65-85),3(113-135),4(161-181),5(188-205),6(210-219),7(250-273)'),
('3kcu', 'E', 8, '1(31-56),2(65-85),3(113-135),4(161-181),5(188-205),6(210-219),7(250-276)'),
('3kdp', 'A', 11, '1(92-107),2(121-142),3(284-306),4(313-336),5(767-788),6(797-815),7(842-864),8(911-931),9(945-963),10(984-998)'),
('3kdp', 'B', 35, '1(33-57)'),
('3kdp', 'G', 12, '1(28-47)'),
('3kg2', 'A', 20, '1(523-543),2(572-583),3(596-617),4(791-813)'),
('3kg2', 'B', 19, '1(523-543),2(572-583),3(596-617),4(791-813)'),
('3kg2', 'C', 20, '1(523-543),2(572-583),3(596-617),4(791-813)'),
('3kg2', 'D', 20, '1(523-543),2(572-583),3(596-617),4(791-813)'),
('3kly', 'A', 10, '1(33-55),2(64-84),3(109-134),4(160-182),5(187-204),6(209-222),7(246-272)'),
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('3kss', 'A', 3, '1(13-31),2(338-357),3(360-380),4(394-412),5(446-465),6(478-500),7(872-891),8(894-918),9(926-945),10(980-1000),11(1012-1031)'),
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('3kvn', 'A', 8, '1(347-356),2(374-382),3(388-397),4(414-424),5(428-437),6(466-475),7(484-494),8(523-532),9(538-547),10(581-589),11(595-604),12(613-620)'),
('3l1l', 'A', 4, '1(13-24),2(43-61),3(87-112),4(125-142),5(144-171),6(195-207),7(227-247),8(278-301),9(324-340),10(353-370),11(389-404),12(408-426)'),
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('3ldc', 'A', 30, '1(23-42),2(70-92)'),
('3ldc', 'B', 30, '1(23-42),2(70-92)'),
('3ldc', 'C', 30, '1(23-42),2(70-92)'),
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('3llq', 'A', 9, '1(5-25),2(36-55),3(64-73),4(80-103),5(129-150),6(159-175),7(185-195),8(199-221)'),
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('3lnm', 'I', 21, '1(160-184),2(221-242),3(254-275),4(287-306),5(321-345),6(357-369),7(381-403)'),
('3lnm', 'U', 21, '1(160-184),2(221-242),3(254-272),4(287-306),5(321-345),6(357-369),7(381-403)'),
('3lnm', 'B', 21, '1(160-184),2(221-242),3(254-275),4(287-306),5(321-345),6(357-369),7(381-403)'),
('3lnm', 'S', 21, '1(160-184),2(221-242),3(254-272),4(287-306),5(321-345),6(357-369),7(381-403)'),
('3lut', 'I', 18, '1(164-182),2(222-241),3(254-270),4(294-310),5(328-346),6(386-406)'),
('3lut', 'J', 18, '1(164-182),2(222-241),3(254-270),4(294-310),5(328-346),6(386-406)'),
('3lut', 'K', 18, '1(164-182),2(222-241),3(254-270),4(294-310),5(328-346),6(386-406)'),
('3lut', 'L', 18, '1(164-182),2(222-241),3(254-270),4(294-310),5(328-346),6(386-406)'),
('3m73', 'A', 1, '1(12-30),2(37-60),3(80-100),4(102-125),5(140-160),6(163-185),7(199-218),8(225-246),9(255-274),10(281-307)'),
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('3mk7', 'A', 6, '1(16-40),2(53-78),3(93-115),4(128-146),5(160-179),6(197-223),7(239-258),8(267-288),9(309-328),10(330-338),11(340-363),12(383-408),13(429-456)'),
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('3mk7', 'C', 20, '1(4-27),2(57-75)'),
('3mkt', 'A', 8, '1(15-38),2(53-73),3(95-116),4(127-149),5(161-178),6(195-215),7(244-266),8(276-297),9(321-339),10(357-380),11(391-415),12(421-440)'),
('3mp7', 'A', 7, '1(30-45),2(78-89),3(115-131),4(147-169),5(176-194),6(241-258),7(286-306),8(345-366),9(411-427),10(434-444)'),
('3mp7', 'B', 38, '1(33-59)'),
('3ne2', 'A', 4, '1(5-28),2(53-77),3(98-122),4(144-167),5(175-192),6(222-243)'),
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('3oe0', 'A', 5, '1(39-62),2(76-98),3(107-132),4(151-173),5(197-220),6(241-264),7(282-302)'),
('3oe0', 'B', 8, '1(39-61),2(76-98),3(106-132),4(155-174),5(197-221),6(240-261),7(283-302)'),
('3oe6', 'A', 8, '1(36-61),2(75-99),3(106-132),4(151-174),5(195-221),6(241-264),7(279-302)'),
('3org', 'A', 12, '1(92-128),2(135-157),3(189-203),4(210-221),5(245-256),6(259-270),7(276-294),8(321-345),9(358-372),10(405-422),11(430-445),12(460-474),13(477-487),14(494-510)'),
('3org', 'D', 13, '1(92-128),2(135-157),3(189-203),4(210-221),5(245-256),6(259-270),7(276-294),8(321-345),9(358-372),10(405-422),11(430-445),12(460-474),13(477-487),14(494-510)'),
('3pbl', 'A', 8, '1(34-52),2(67-91),3(101-126),4(150-170),5(187-209),6(330-351),7(363-386)'),
('3prn', 'A', 3, '1(2-13),2(27-39),3(45-57),4(63-75),5(78-83),6(130-139),7(142-149),8(164-171),9(175-182),10(194-202),11(206-213),12(223-232),13(235-242),14(252-260),15(265-272),16(280-288)'),
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('7ahl', 'A', 33, '1(119-126),2(132-140)'),
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('7ahl', 'C', 34, '1(119-126),2(132-140)'),
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('7ahl', 'G', 34, '1(119-126),2(132-140)'),
('3lbw', 'A', 27, '1(26-43)'),
('3lbw', 'B', 18, '1(26-43)'),
('3lbw', 'C', 22, '1(26-46)'),
('3lbw', 'D', 29, '1(26-46)'),
('1mic', 'A', 36, '1(1-15)'),
('1mic', 'B', 34, '1(2-13)'),
('2xdc', 'A', 37, '1(2-14)'),
('2xdc', 'B', 36, '1(2-14)'),
('2izq', 'A', 32, '1(2-15)'),
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('1grm', 'A', 27, '1(2-14)'),
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('1grm', 'A', 27, '1(2-14)'),
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('1jb0', 'A', 2, '1(72-93),2(159-179),3(193-216),4(298-314),5(354-374),6(392-413),7(439-464),8(536-557),9(591-613),10(674-691),11(725-745)'),
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('1jb0', 'F', 22, '1(60-84)'),
('1jb0', 'I', 17, '1(9-32)'),
('1jb0', 'J', 22, '1(11-30)'),
('1jb0', 'K', 11, '1(21-32),2(57-76)'),
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('1jb0', 'X', 5, '1(11-31)'),
('2o01', 'A', 5, '1(80-99),2(165-181),3(201-221),4(302-315),5(358-376),6(394-412),7(443-463),8(539-557),9(598-614),10(678-694),11(730-748)'),
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('2o01', '3', 17, '1(63-76),2(118-128),3(190-204)'),
('2o01', '4', 0, '1(42-60),2(90-106),3(155-171)'),
('3bz1', 'A', 7, '1(32-53),2(113-134),3(142-160),4(196-218),5(270-293)'),
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('3bz1', 'D', 11, '1(32-54),2(109-132),3(140-162),4(195-217),5(266-288)'),
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('3bz1', 'F', 29, '1(18-42)'),
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('3bz1', 'M', 3, '1(7-28)'),
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-- --------------------------------------------------------

--
-- Table structure for table `type`
--

CREATE TABLE `type` (
  `id` smallint(4) NOT NULL auto_increment,
  `number` char(2) NOT NULL default '',
  `name` char(80) NOT NULL default '',
  `description` char(100) NOT NULL default '',
  PRIMARY KEY  (`id`)
) ENGINE=MyISAM  DEFAULT CHARSET=latin1 AUTO_INCREMENT=5 ;

--
-- Dumping data for table `type`
--

INSERT INTO `type` (`id`, `number`, `name`, `description`) VALUES
(1, '1.', 'Transmembrane', ''),
(2, '2.', 'Monotopic/peripheral', ''),
(3, '3.', 'Peptides', '');