This following example has been heavily cut and truncated from the original file 1ABS.pdb. It will not work when loaded to a 3D display program. It was made shorter for the purpose of illustration of the PDB file format HEADER PDB mock file as an Example (from 1ABS.pdb) 28-JAN-97 short_name_here TITLE PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K COMPND MOL_ID: 1; COMPND 2 MOLECULE: MYOGLOBIN; COMPND 3 CHAIN: NULL; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: D122N; COMPND 6 BIOLOGICAL_UNIT: MONOMER; COMPND 7 OTHER_DETAILS: HEME BOUND TO HIS-93, PHOTOLYSED CO ATOP COMPND 8 HEME SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PHYSETER CATODON; SOURCE 3 ORGANISM_COMMON: SPERM WHALE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 OTHER_DETAILS: SYNTHETIC GENE KEYWDS OXYGEN STORAGE, INTERMEDIATE IN LIGAND BINDING, KEYWDS 2 RESPIRATORY PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR I.SCHLICHTING,J.BERENDZEN,G.N.PHILLIPS JUNIOR,R.M.SWEET REVDAT 1 01-APR-97 1ABS 0 JRNL AUTH I.SCHLICHTING,J.BERENDZEN,G.N.PHILLIPS JUNIOR, JRNL AUTH 2 R.M.SWEET JRNL TITL CRYSTAL STRUCTURE OF PHOTOLYSED JRNL TITL 2 CARBONMONOXY-MYOGLOBIN JRNL REF NATURE V. 371 808 1994 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.N.PHILLIPS JUNIOR,R.M.ARDUINI,B.A.SPRINGER, REMARK 1 AUTH 2 S.G.SLIGAR REMARK 1 TITL CRYSTAL STRUCTURE OF MYOGLOBIN FROM A SYNTHETIC REMARK 1 TITL 2 GENE REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 7 358 1990 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 0867 REMARK 2 REMARK 2 RESOLUTION. 1.5 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.5 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.0 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89. REMARK 3 NUMBER OF REFLECTIONS : 29798 REMARK 4 REMARK 4 1ABS COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: REMARK 280 PROTEIN WAS CRYSTALLIZED FROM 3.6 M AMMONIUM SULFATE. REMARK 280 CRYSTALS WER SOAKED FOR ~ 1 HOUR IN A THOROUGHLY DEGASSED REMARK 280 AND N2 - SATURATED CRYOPROTECTANT SOLUTION MADE BY ADDITION REMARK 280 OF 100 MG SUCROSE, 100 MG GLUCOSE AND 8 MG NA-DITHIONATE TO REMARK 280 1 ML OF 70% SATURATED AMMONIUM SULFATE WITH 50 MM TRIS. REMARK 280 HCL PH 9.0. THEN THE SOLUTION WAS EXCHANGED AGAINST A CO REMARK 280 SATURATED ONE. DISTINCT COLOR CHANGES ACCOMPANIED THE REMARK 280 FORMATION OF UNLIGATED MYOGLOBIN FROM MET-MB AND MBCO FROM REMARK 280 UNLIGATED MB. REMARK DBREF 1ABS 1 153 SWS P02185 MYG_PHYCA 1 153 SEQADV 1ABS ASN 122 SWS P02185 ASP 122 ENGINEERED SEQRES 1 154 MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS SEQRES 2 154 VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY SEQRES 3 154 GLN ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU SEQRES 4 154 THR LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR SEQRES 5 154 GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS SEQRES 6 154 GLY VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS SEQRES 7 154 LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA SEQRES 8 154 GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR HET HEM 154 43 HET CMO 155 2 HET SO4 156 5 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETNAM SO4 SULFATE ION HETSYN HEM HEME FORMUL 2 HEM C34 H32 N4 O4 FE1 FORMUL 3 CMO C1 O1 FORMUL 4 SO4 O4 S1 2- FORMUL 5 HOH *118(H2 O1) HELIX 1 A SER 3 GLU 18 1 16 HELIX 2 B ASP 20 SER 35 1 16 HELIX 3 C HIS 36 LYS 42 1 7 HELIX 4 D THR 51 ALA 57 1 7 HELIX 5 E SER 58 LYS 77 1 20 HELIX 6 F LEU 86 THR 95 1 10 HELIX 7 G PRO 100 ARG 118 1 19 HELIX 8 H GLY 124 LEU 149 1 26 LINK FE HEM 154 NE2 HIS 93 CRYST1 90.420 90.420 45.400 90.00 90.00 120.00 P 6 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011060 0.006385 0.000000 0.00000 SCALE2 0.000000 0.012770 0.000000 0.00000 SCALE3 0.000000 0.000000 0.022026 0.00000 ATOM 1 N MET 0 23.612 8.367 -9.458 1.00 26.59 N ATOM 2 CA MET 0 23.871 9.800 -9.365 1.00 25.47 C ATOM 3 C MET 0 25.258 10.146 -9.871 1.00 23.93 C ATOM 4 O MET 0 26.193 9.343 -9.767 1.00 24.76 O ATOM 5 CB MET 0 23.749 10.277 -7.931 1.00 26.67 C ATOM 6 CG MET 0 24.410 9.317 -6.955 1.00 27.31 C ATOM 7 SD MET 0 23.997 9.709 -5.244 1.00 27.80 S ATOM 8 CE MET 0 24.625 11.379 -5.216 1.00 25.33 C ATOM 9 N VAL 1 25.410 11.314 -10.492 1.00 21.05 N ATOM 10 CA VAL 1 26.714 11.686 -11.004 1.00 17.92 C ....Very long piece removed (more than a 1000 lines)... ATOM 1223 C GLY 153 22.545 -1.135 6.941 1.00 27.65 C ATOM 1224 O GLY 153 21.708 -0.362 7.402 1.00 26.72 O ATOM 1225 OXT GLY 153 23.329 -0.789 6.063 1.00 28.94 O TER 1226 GLY 153 HETATM 1227 FE HEM 154 34.801 4.074 10.439 1.00 4.64 FE HETATM 1228 CHA HEM 154 37.447 2.390 11.650 1.00 4.79 C HETATM 1229 CHB HEM 154 36.751 5.382 8.055 1.00 4.69 C HETATM 1230 CHC HEM 154 32.301 6.098 9.483 1.00 4.83 C HETATM 1231 CHD HEM 154 33.065 3.274 13.212 1.00 5.32 C HETATM 1232 N A HEM 154 36.704 3.923 9.957 1.00 4.98 N HETATM 1233 C1A HEM 154 37.648 3.136 10.495 1.00 4.90 C HETATM 1234 C2A HEM 154 38.828 3.106 9.758 1.00 5.21 C HETATM 1235 C3A HEM 154 38.610 3.968 8.707 1.00 4.99 C HETATM 1236 C4A HEM 154 37.331 4.460 8.897 1.00 4.92 C CONECT 748 746 747 1227 CONECT 1227 748 1232 1243 1251 CONECT 1227 1259 CONECT 1228 1233 1263 CONECT 1229 1236 1244 CONECT 1230 1247 1252 CONECT 1231 1255 1260 MASTER 226 0 3 8 0 0 0 6 1393 1 52 12 END