Thesis (Index) <- Sean Forman <- You Are Here
This is a small portion of a protein data bank file. The header consists of the protein along with its date of submission to the Data Bank. The journal the protein structure was first presented in is displayed along with the authors and other references. Below that are comments on interesting features of the protein along with a list of the amino acid sequence. Then at the very end, the 3-D locations of the first four amino acids are included. The rest of the amino acids would normally follow below those.
A full description of the format of this file can be found here:
http://www.rcsb.org/pdb/docs/format/pdbguide2.2/Contents_Guide_21.html
HEADER HYDROLASE(ACID PROTEINASE ZYMOGEN) 03-SEP-91 3PSG 3PSG 2 COMPND PEPSINOGEN 3PSG 3 SOURCE PORCINE (SUS \$SCROFA) 3PSG 4 AUTHOR J.A.HARTSUCK,G.KOELSCH,S.J.REMINGTON 3PSG 5 REVDAT 1 15-JAN-93 3PSG 0 3PSG 6 SPRSDE 15-JAN-93 3PSG 1PSG 3PSG 7 JRNL AUTH J.A.HARTSUCK,G.KOELSCH,S.J.REMINGTON 3PSG 8 JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF PORCINE 3PSG 9 JRNL TITL 2 PEPSINOGEN 3PSG 10 JRNL REF PROTEINS.STRUCT.,FUNCT., V. 13 1 1992 3PSG 11 JRNL REF 2 GENET. 3PSG 12 JRNL REFN ASTM PSFGEY US ISSN 0887-3585 867 3PSG 13 REMARK 1 3PSG 14 REMARK 2 3PSG 15 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. 3PSG 16 REMARK 3 3PSG 17 REMARK 3 REFINEMENT. 3PSG 18 REMARK 3 PROGRAM TNT 3PSG 19 REMARK 3 AUTHORS TRONRUD,TEN EYCK & MATHEWS 3PSG 20 REMARK 3 R VALUE 0.173 3PSG 21 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 3PSG 22 REMARK 3 RMSD BOND ANGLES 2.60 DEGREES 3PSG 23 REMARK 4 3PSG 24 REMARK 4 THE ATOMIC COORDINATES IN THIS ENTRY ARE IDENTICAL TO THOSE 3PSG 25 REMARK 4 IN PROTEIN DATA BANK ENTRY 1PSG WHICH HAS BEEN WITHDRAWN. 3PSG 26 REMARK 4 THE RESIDUE NUMBERING HAS BEEN REVISED. 3PSG 27 REMARK 5 3PSG 28 REMARK 5 THE ELECTRON DENSITY IS VERY WEAK FOR RESIDUES 157 - 161. 3PSG 29 REMARK 5 COORDINATES FOR THESE RESIDUES ARE NOT INCLUDED IN THIS 3PSG 30 REMARK 5 MODEL. 3PSG 31 REMARK 6 3PSG 32 REMARK 6 RESIDUE SER 68 IS PHOSPHORYLATED BUT THE SIDE CHAIN 3PSG 33 REMARK 6 DENSITY IS SO WEAK THAT ONLY CB HAS BEEN INCLUDED. 3PSG 34 REMARK 7 3PSG 35 REMARK 7 PROPEPTIDE RESIDUES HAVE BEEN ASSIGNED INSERTION CODE P 3PSG 36 REMARK 7 AND NUMBERED FROM 1 TO 44. THE REMAINDER OF THE RESIDUES 3PSG 37 REMARK 7 ARE NUMBERED FROM 1 TO 326. 3PSG 38 REMARK 8 3PSG 39 REMARK 8 A NUMBER OF BETA TURNS ARE ALSO LISTED AS 3/10 HELICES, 3PSG 40 REMARK 8 WHERE APPROPRIATE. 3PSG 41 REMARK 9 3PSG 42 REMARK 9 ONE OF THE SHEETS IN THIS ENTRY (SHEET S2), CONTAINING SIX 3PSG 43 REMARK 9 STRANDS, IS A BETA BARREL CONTAINING AN EXTENSION COMPRISED 3PSG 44 REMARK 9 OF RESIDUES 65 - 90 WHICH FORMS A SECOND HYDROPHOBIC CORE 3PSG 45 REMARK 9 WITH THE SURFACE OF THE BARREL. THIS IS REPRESENTED IN 3PSG 46 REMARK 9 THIS ENTRY BY A SEVEN-STRANDED SHEET IN WHICH THE FIRST AND 3PSG 47 REMARK 9 LAST STRANDS ARE IDENTICAL. ADDITIONALLY, THE THIRD STRAND 3PSG 48 REMARK 9 IS COMPOSED OF THREE NONCONTIGUOUS FRAGMENTS (RESIDUES 3PSG 49 REMARK 9 16 - 20, 65 - 67, AND 69 - 75). THIS IS REPRESENTED BY 3PSG 50 REMARK 9 DESCRIBING THE SHEET THREE TIMES (SHEETS *S2A*, *S2B*, AND 3PSG 51 REMARK 9 *S2C* BELOW) WITH DIFFERENT THIRD STRANDS. REGISTRATION 3PSG 52 REMARK 9 INFORMATION IS NOT INCLUDED WHEN TWO ADJACENT STRANDS DO 3PSG 53 REMARK 9 NOT INTERACT. 3PSG 54 REMARK 10 3PSG 55 REMARK 10 LYS 23P MISSING CD CE NZ 3PSG 56 REMARK 10 LYS 27P MISSING CG CD CE NZ 3PSG 57 REMARK 10 LYS 30P MISSING CD CE NZ 3PSG 58 REMARK 10 GLU 40P MISSING CG CD OE1 NE2 3PSG 59 REMARK 10 ALA 42P MISSING CB 3PSG 60 REMARK 10 ALA 43P MISSING CB 3PSG 61 REMARK 10 LEU 44P MISSING CB CG CD1 CD2 3PSG 62 REMARK 10 ILE 1 MISSING CB CG1 CD1 CG2 3PSG 63 REMARK 10 SER 68 MISSING OG 3PSG 64 REMARK 10 GLU 70 MISSING CG CD OE1 NE2 3PSG 65 REMARK 10 SER 163 MISSING CB OG 3PSG 66 REMARK 10 GLU 239 MISSING CG CD OE1 NE2 3PSG 67 REMARK 10 SER 241 MISSING OG 3PSG 68 REMARK 10 ASP 242 MISSING CG OD1 OD2 3PSG 69 REMARK 10 ASP 253 MISSING OD1 OD2 3PSG 70 REMARK 10 ASP 278 MISSING CB CG OD1 OD2 3PSG 71 REMARK 10 ASP 279 MISSING CG OD1 OD2 3PSG 72 REMARK 10 ASP 280 MISSING CB CG OD1 OD2 3PSG 73 REMARK 10 SER 281 MISSING CB OG 3PSG 74 REMARK 10 THR 293 MISSING OG1 CG2 3PSG 75 SEQRES 1 370 LEU VAL LYS VAL PRO LEU VAL ARG LYS LYS SER LEU ARG 3PSG 76 SEQRES 2 370 GLN ASN LEU ILE LYS ASP GLY LYS LEU LYS ASP PHE LEU 3PSG 77 SEQRES 3 370 LYS THR HIS LYS HIS ASN PRO ALA SER LYS TYR PHE PRO 3PSG 78 SEQRES 4 370 GLU ALA ALA ALA LEU ILE GLY ASP GLU PRO LEU GLU ASN 3PSG 79 SEQRES 5 370 TYR LEU ASP THR GLU TYR PHE GLY THR ILE GLY ILE GLY 3PSG 80 SEQRES 6 370 THR PRO ALA GLN ASP PHE THR VAL ILE PHE ASP THR GLY 3PSG 81 SEQRES 7 370 SER SER ASN LEU TRP VAL PRO SER VAL TYR CYS SER SER 3PSG 82 SEQRES 8 370 LEU ALA CYS SER ASP HIS ASN GLN PHE ASN PRO ASP ASP 3PSG 83 SEQRES 9 370 SER SER THR PHE GLU ALA THR SER GLN GLU LEU SER ILE 3PSG 84 SEQRES 10 370 THR TYR GLY THR GLY SER MET THR GLY ILE LEU GLY TYR 3PSG 85 SEQRES 11 370 ASP THR VAL GLN VAL GLY GLY ILE SER ASP THR ASN GLN 3PSG 86 SEQRES 12 370 ILE PHE GLY LEU SER GLU THR GLU PRO GLY SER PHE LEU 3PSG 87 SEQRES 13 370 TYR TYR ALA PRO PHE ASP GLY ILE LEU GLY LEU ALA TYR 3PSG 88 SEQRES 14 370 PRO SER ILE SER ALA SER GLY ALA THR PRO VAL PHE ASP 3PSG 89 SEQRES 15 370 ASN LEU TRP ASP GLN GLY LEU VAL SER GLN ASP LEU PHE 3PSG 90 SEQRES 16 370 SER VAL TYR LEU SER SER ASN ASP ASP SER GLY SER VAL 3PSG 91 SEQRES 17 370 VAL LEU LEU GLY GLY ILE ASP SER SER TYR TYR THR GLY 3PSG 92 SEQRES 18 370 SER LEU ASN TRP VAL PRO VAL SER VAL GLU GLY TYR TRP 3PSG 93 SEQRES 19 370 GLN ILE THR LEU ASP SER ILE THR MET ASP GLY GLU THR 3PSG 94 SEQRES 20 370 ILE ALA CYS SER GLY GLY CYS GLN ALA ILE VAL ASP THR 3PSG 95 SEQRES 21 370 GLY THR SER LEU LEU THR GLY PRO THR SER ALA ILE ALA 3PSG 96 SEQRES 22 370 ASN ILE GLN SER ASP ILE GLY ALA SER GLU ASN SER ASP 3PSG 97 SEQRES 23 370 GLY GLU MET VAL ILE SER CYS SER SER ILE ASP SER LEU 3PSG 98 SEQRES 24 370 PRO ASP ILE VAL PHE THR ILE ASP GLY VAL GLN TYR PRO 3PSG 99 SEQRES 25 370 LEU SER PRO SER ALA TYR ILE LEU GLN ASP ASP ASP SER 3PSG 100 SEQRES 26 370 CYS THR SER GLY PHE GLU GLY MET ASP VAL PRO THR SER 3PSG 101 SEQRES 27 370 SER GLY GLU LEU TRP ILE LEU GLY ASP VAL PHE ILE ARG 3PSG 102 SEQRES 28 370 GLN TYR TYR THR VAL PHE ASP ARG ALA ASN ASN LYS VAL 3PSG 103 SEQRES 29 370 GLY LEU ALA PRO VAL ALA 3PSG 104 FTNOTE 1 3PSG 105 FTNOTE 1 RESIDUE PRO 23 IS A CIS PROLINE. 3PSG 106 FORMUL 2 HOH *180(H2 O1) 3PSG 107 CRYST1 106.100 43.700 88.900 90.00 91.40 90.00 C 2 4 3PSG 108 ORIGX1 1.000000 0.000000 0.000000 0.00000 3PSG 109 ORIGX2 0.000000 1.000000 0.000000 0.00000 3PSG 110 ORIGX3 0.000000 0.000000 1.000000 0.00000 3PSG 111 SCALE1 0.009425 0.000000 0.000230 0.00000 3PSG 112 SCALE2 0.000000 0.022883 0.000000 0.00000 3PSG 113 SCALE3 0.000000 0.000000 0.011252 0.00000 3PSG 114 ATOM 1 N LEU 1P 57.364 -9.595 2.554 1.00 21.58 3PSG 115 ATOM 2 CA LEU 1P 56.687 -8.586 3.371 1.00 22.68 3PSG 116 ATOM 3 C LEU 1P 57.052 -8.758 4.847 1.00 16.32 3PSG 117 ATOM 4 O LEU 1P 57.270 -9.875 5.293 1.00 26.09 3PSG 118 ATOM 5 CB LEU 1P 55.129 -8.641 3.226 1.00 36.56 3PSG 119 ATOM 6 CG LEU 1P 54.503 -8.303 1.850 1.00 32.34 3PSG 120 ATOM 7 CD1 LEU 1P 52.977 -8.461 1.892 1.00 37.73 3PSG 121 ATOM 8 CD2 LEU 1P 54.798 -6.861 1.453 1.00 30.91 3PSG 122 ATOM 9 N VAL 2P 57.149 -7.672 5.627 1.00 17.11 3PSG 123 ATOM 10 CA VAL 2P 57.472 -7.872 7.047 1.00 15.32 3PSG 124 ATOM 11 C VAL 2P 56.176 -8.087 7.837 1.00 20.03 3PSG 125 ATOM 12 O VAL 2P 55.370 -7.164 7.985 1.00 18.54 3PSG 126 ATOM 13 CB VAL 2P 58.309 -6.750 7.618 1.00 21.11 3PSG 127 ATOM 14 CG1 VAL 2P 58.642 -7.031 9.089 1.00 15.95 3PSG 128 ATOM 15 CG2 VAL 2P 59.574 -6.617 6.758 1.00 23.35 3PSG 129 ATOM 16 N LYS 3P 55.959 -9.331 8.243 1.00 23.38 3PSG 130 ATOM 17 CA LYS 3P 54.761 -9.726 8.949 1.00 23.08 3PSG 131 ATOM 18 C LYS 3P 55.009 -10.146 10.384 1.00 33.87 3PSG 132 ATOM 19 O LYS 3P 55.870 -10.952 10.608 1.00 29.24 3PSG 133 ATOM 20 CB LYS 3P 54.070 -10.868 8.201 1.00 17.80 3PSG 134 ATOM 21 CG LYS 3P 53.558 -10.466 6.812 1.00 30.12 3PSG 135 ATOM 22 CD LYS 3P 52.365 -11.275 6.276 1.00 53.77 3PSG 136 ATOM 23 CE LYS 3P 52.307 -11.408 4.730 1.00 64.96 3PSG 137 ATOM 24 NZ LYS 3P 51.094 -10.845 4.035 1.00 36.57 3PSG 138 ATOM 25 N VAL 4P 54.260 -9.631 11.356 1.00 18.70 3PSG 139 ATOM 26 CA VAL 4P 54.376 -10.099 12.733 1.00 8.89 3PSG 140 ATOM 27 C VAL 4P 53.073 -10.866 13.011 1.00 16.65 3PSG 141 ATOM 28 O VAL 4P 52.010 -10.269 12.976 1.00 23.14 3PSG 142 ATOM 29 CB VAL 4P 54.499 -8.923 13.697 1.00 16.83 3PSG 143 ATOM 30 CG1 VAL 4P 54.656 -9.422 15.142 1.00 21.44 3PSG 144 ATOM 31 CG2 VAL 4P 55.655 -7.981 13.323 1.00 25.67 3PSG 145 ... ...
