Here is a sample PDB file. This is Peanut Peroxidase,
PDB-ID: 1SCH (note: some sections were shortened):
TITLE SECTION
HEADER OXIDOREDUCTASE 23-JAN-96 1SCH
TITLE PEANUT PEROXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEANUT PEROXIDASE, MAJOR CATIONIC ISOZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PNP;
COMPND 5 EC: 1.11.1.7;
COMPND 6 OTHER_DETAILS: CARBOHYDRATE PRESENT. ONE N-ACETYL
COMPND 7 GLUCOSAMINE SUGAR RESIDUE MODELED AT ASN 144 OF CHAIN B.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARACHIS HYPOGAEA;
SOURCE 3 ORGANISM_COMMON: PEANUT;
SOURCE 4 CELLULAR_LOCATION: SECRETED, EXTRACELLULAR;
SOURCE 5 OTHER_DETAILS: CULTURED PEANUT CELLS
KEYWDS CALCIUM BINDING, GLYCOSYLATION, PEROXIDASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.SCHULLER,T.L.POULOS
REVDAT 1 11-JUL-96 1SCH 0
JRNL AUTH D.J.SCHULLER,N.BAN,R.B.VANHUYSTEE,A.MCPHERSON,
JRNL AUTH 2 T.L.POULOS
JRNL TITL THE CRYSTAL STRUCTURE OF PEANUT PEROXIDASE
JRNL REF STRUCTURE (LONDON) V. 4 311 1996
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.7 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) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.9
REMARK 3 NUMBER OF REFLECTIONS : 19414
REMARK 3
PRIMARY STRUCTURE SECTION
SEQRES 1 A 294 PCA LEU SER SER ASN PHE TYR ALA THR LYS CYS PRO ASN
SEQRES 2 A 294 ALA LEU SER THR ILE LYS SER ALA VAL ASN SER ALA VAL
SEQRES 3 A 294 ALA LYS GLU ALA ARG MET GLY ALA SER LEU LEU ARG LEU
SEQRES 4 A 294 HIS PHE HIS ASP CYS PHE VAL GLN GLY CYS ASP ALA SER
SEQRES 5 A 294 VAL LEU LEU ASP ASP THR SER ASN PHE THR GLY GLU LYS
SEQRES 6 A 294 THR ALA GLY PRO ASN ALA ASN SER ILE ARG GLY PHE GLU
SEQRES 7 A 294 VAL ILE ASP THR ILE LYS SER GLN VAL GLU SER LEU CYS
SEQRES 8 A 294 PRO GLY VAL VAL SER CYS ALA ASP ILE LEU ALA VAL ALA
SEQRES 9 A 294 ALA ARG ASP SER VAL VAL ALA LEU GLY GLY ALA SER TRP
SEQRES 10 A 294 ASN VAL LEU LEU GLY ARG ARG ASP SER THR THR ALA SER
SEQRES 11 A 294 LEU SER SER ALA ASN SER ASP LEU PRO ALA PRO PHE PHE
SEQRES 12 A 294 ASN LEU SER GLY LEU ILE SER ALA PHE SER ASN LYS GLY
SEQRES 13 A 294 PHE THR THR LYS GLU LEU VAL THR LEU SER GLY ALA HIS
SEQRES 14 A 294 THR ILE GLY GLN ALA GLN CYS THR ALA PHE ARG THR ARG
SEQRES 15 A 294 ILE TYR ASN GLU SER ASN ILE ASP PRO THR TYR ALA LYS
SEQRES 16 A 294 SER LEU GLN ALA ASN CYS PRO SER VAL GLY GLY ASP THR
SEQRES 17 A 294 ASN LEU SER PRO PHE ASP VAL THR THR PRO ASN LYS PHE
SEQRES 18 A 294 ASP ASN ALA TYR TYR ILE ASN LEU ARG ASN LYS LYS GLY
SEQRES 19 A 294 LEU LEU HIS SER ASP GLN GLN LEU PHE ASN GLY VAL SER
SEQRES 20 A 294 THR ASP SER GLN VAL THR ALA TYR SER ASN ASN ALA ALA
SEQRES 21 A 294 THR PHE ASN THR ASP PHE GLY ASN ALA MET ILE LYS MET
SEQRES 22 A 294 GLY ASN LEU SER PRO LEU THR GLY THR SER GLY GLN ILE
SEQRES 23 A 294 ARG THR ASN CYS ARG LYS THR ASN
SEQRES 1 B 294 PCA LEU SER SER ASN PHE TYR ALA THR LYS CYS PRO ASN
SEQRES 2 B 294 ALA LEU SER THR ILE LYS SER ALA VAL ASN SER ALA VAL
SEQRES 3 B 294 ALA LYS GLU ALA ARG MET GLY ALA SER LEU LEU ARG LEU
SEQRES 4 B 294 HIS PHE HIS ASP CYS PHE VAL GLN GLY CYS ASP ALA SER
SEQRES 5 B 294 VAL LEU LEU ASP ASP THR SER ASN PHE THR GLY GLU LYS
SEQRES 6 B 294 THR ALA GLY PRO ASN ALA ASN SER ILE ARG GLY PHE GLU
SEQRES 7 B 294 VAL ILE ASP THR ILE LYS SER GLN VAL GLU SER LEU CYS
SEQRES 8 B 294 PRO GLY VAL VAL SER CYS ALA ASP ILE LEU ALA VAL ALA
SEQRES 9 B 294 ALA ARG ASP SER VAL VAL ALA LEU GLY GLY ALA SER TRP
SEQRES 10 B 294 ASN VAL LEU LEU GLY ARG ARG ASP SER THR THR ALA SER
SEQRES 11 B 294 LEU SER SER ALA ASN SER ASP LEU PRO ALA PRO PHE PHE
SEQRES 12 B 294 ASN LEU SER GLY LEU ILE SER ALA PHE SER ASN LYS GLY
SEQRES 13 B 294 PHE THR THR LYS GLU LEU VAL THR LEU SER GLY ALA HIS
SEQRES 14 B 294 THR ILE GLY GLN ALA GLN CYS THR ALA PHE ARG THR ARG
SEQRES 15 B 294 ILE TYR ASN GLU SER ASN ILE ASP PRO THR TYR ALA LYS
SEQRES 16 B 294 SER LEU GLN ALA ASN CYS PRO SER VAL GLY GLY ASP THR
SEQRES 17 B 294 ASN LEU SER PRO PHE ASP VAL THR THR PRO ASN LYS PHE
SEQRES 18 B 294 ASP ASN ALA TYR TYR ILE ASN LEU ARG ASN LYS LYS GLY
SEQRES 19 B 294 LEU LEU HIS SER ASP GLN GLN LEU PHE ASN GLY VAL SER
SEQRES 20 B 294 THR ASP SER GLN VAL THR ALA TYR SER ASN ASN ALA ALA
SEQRES 21 B 294 THR PHE ASN THR ASP PHE GLY ASN ALA MET ILE LYS MET
SEQRES 22 B 294 GLY ASN LEU SER PRO LEU THR GLY THR SER GLY GLN ILE
SEQRES 23 B 294 ARG THR ASN CYS ARG LYS THR ASN
HET PCA A 1 8
HET HEM A 300 43 PROTOPORPHYRIN IX CONTAINS FE(II)
HET CA A 301 1
HET CA A 302 1
HET PCA B 1 8
HETNAM PCA PYROGLUTAMIC ACID
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN HEM HEME
SECONDARY STRUCTURE SECTION
HELIX 1 A ALA A 14 LYS A 28 1 15
HELIX 2 B ARG A 31 PHE A 45 1 15
HELIX 3 C PHE A 77 LEU A 90 1 14
HELIX 4 D ALA A 98 LEU A 112 1 15
HELIX 5 D' LEU A 131 ASP A 137 1 7
HELIX 6 E SER A 146 ASN A 154 1 9
HELIX 7 F THR A 159 SER A 166 1 8
HELIX 8 F' PHE A 179 ASN A 185 1 7
HELIX 9 F" THR A 192 ASN A 200 1 9
HELIX 10 G ALA A 224 ARG A 230 1 7
HELIX 11 H HIS A 237 GLN A 241 1 5
HELIX 12 I ASP A 249 ASN A 257 1 9
HELIX 13 J ALA A 259 MET A 273 1 15
HELIX 14 A ALA B 14 LYS B 28 1 15
HELIX 15 B ARG B 31 PHE B 45 1 15
HELIX 16 C PHE B 77 LEU B 90 1 14
HELIX 17 D ALA B 98 LEU B 112 1 15
HELIX 18 D' LEU B 131 ASP B 137 1 7
HELIX 19 E SER B 146 ASN B 154 1 9
HELIX 20 F THR B 159 SER B 166 1 8
HELIX 21 F' PHE B 179 ASN B 185 1 7
HELIX 22 F" THR B 192 ASN B 200 1 9
HELIX 23 G ALA B 224 ARG B 230 1 7
HELIX 24 H HIS B 237 GLN B 241 1 5
HELIX 25 I ASP B 249 ASN B 257 1 9
HELIX 26 J ALA B 259 MET B 273 1 15
SHEET 1 A 2 GLN A 173 GLN A 175 0
SHEET 2 A 2 LEU A 210 PRO A 212 -1 N SER A 211 O ALA A 174
SHEET 1 B 2 GLN B 173 GLN B 175 0
SHEET 2 B 2 LEU B 210 PRO B 212 -1 N SER B 211 O ALA B 174
CONNECTIVITY ANNOTATION SECTION
SSBOND 1 CYS A 11 CYS A 91
SSBOND 2 CYS A 44 CYS A 49
SSBOND 3 CYS A 97 CYS A 290
SSBOND 4 CYS A 176 CYS A 201
SSBOND 5 CYS B 11 CYS B 91
SSBOND 6 CYS B 44 CYS B 49
SSBOND 7 CYS B 97 CYS B 290
SSBOND 8 CYS B 176 CYS B 201
LINK C PCA A 1 N LEU A 2
LINK FE HEM A 300 NE2 HIS A 169
LINK CA CA A 301 O THR A 170
LINK CA CA A 301 OG1 THR A 170
LINK CA CA A 301 O THR A 217
LINK CA CA A 301 O LYS A 220
LINK CA CA A 302 O ASP A 43
LINK CA CA A 302 O VAL A 46
LINK CA CA A 302 O GLY A 48
LINK C PCA B 1 N LEU B 2
LINK FE HEM B 300 NE2 HIS B 169
LINK CA CA B 301 O THR B 170
LINK CA CA B 301 O THR B 217
LINK CA CA B 301 OG1 THR B 217
LINK CA CA B 301 O LYS B 220
LINK CA CA B 302 O ASP B 43
LINK CA CA B 302 O VAL B 46
LINK CA CA B 302 O GLY B 48
LINK CA CA B 302 OG SER B 52
LINK C1 NAG B 303 ND2 ASN B 144
MISCELLANEOUS FEATURES SECTION
SITE 1 APC 5 THR A 170 ASP A 214 THR A 217 LYS A 220
SITE 2 APC 5 ASP A 222
SITE 1 ADC 6 ASP A 43 VAL A 46 GLY A 48 ASP A 50
SITE 2 ADC 6 SER A 52 GLU A 64
SITE 1 ADH 4 HIS A 42 ARG A 38 PHE A 41 ASN A 70
SITE 1 APH 3 HIS A 169 PHE A 213 ASP A 239
SITE 1 BPC 5 THR B 170 ASP B 214 THR B 217 LYS B 220
SITE 2 BPC 5 ASP B 222
SITE 1 BDC 6 ASP B 43 VAL B 46 GLY B 48 ASP B 50
SITE 2 BDC 6 SER B 52 GLU B 64
SITE 1 BDH 4 HIS B 42 ARG B 38 PHE B 41 ASN B 70
SITE 1 BPH 3 HIS B 169 PHE B 213 ASP B 239
CRYSTALLOGRAPHIC AND COORDINATE TRANSFORMATION SECTION
CRYST1 48.100 97.200 146.200 90.00 90.00 90.00 P 21 21 21 8
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 0.020790 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010288 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006840 0.00000
MTRIX1 1 0.438990 0.642420 -0.628160 19.31394 1
MTRIX2 1 0.657570 0.246710 0.711850 -23.03639 1
MTRIX3 1 0.612280 -0.725560 -0.314130 48.73469 1
COORDINATE SECTION
HETATM 1 N PCA A 1 21.053 53.031 41.428 1.00 64.66 N
HETATM 2 CA PCA A 1 21.281 54.416 41.795 1.00 64.66 C
HETATM 3 C PCA A 1 21.512 54.618 43.296 1.00 64.66 C
HETATM 4 O PCA A 1 21.449 55.742 43.797 1.00 97.31 O
HETATM 5 CB PCA A 1 19.978 55.081 41.329 1.00 97.31 C
HETATM 6 CG PCA A 1 18.952 53.983 41.455 1.00 97.31 C
HETATM 7 CD PCA A 1 19.776 52.710 41.396 1.00 97.31 C
HETATM 8 OE PCA A 1 19.322 51.556 41.252 1.00 97.31 O
ATOM 9 N LEU A 2 21.768 53.526 44.010 1.00 16.90 N
ATOM 10 CA LEU A 2 22.014 53.594 45.444 1.00 16.90 C
ATOM 11 C LEU A 2 23.393 54.216 45.651 1.00 16.90 C
ATOM 12 O LEU A 2 24.329 53.888 44.922 1.00 8.12 O
ATOM 13 CB LEU A 2 21.986 52.182 46.044 1.00 8.12 C
ATOM 14 CG LEU A 2 20.821 51.253 45.684 1.00 8.12 C
ATOM 15 CD1 LEU A 2 20.926 49.982 46.501 1.00 8.12 C
ATOM 16 CD2 LEU A 2 19.487 51.927 45.939 1.00 8.12 C
ATOM 17 N SER A 3 23.523 55.114 46.621 1.00 5.95 N
ATOM 18 CA SER A 3 24.804 55.760 46.897 1.00 5.95 C
ATOM 19 C SER A 3 25.108 55.755 48.394 1.00 5.95 C
ATOM 20 O SER A 3 24.192 55.755 49.224 1.00 18.79 O
ATOM 21 CB SER A 3 24.803 57.195 46.357 1.00 18.79 C
ATOM 22 OG SER A 3 23.704 57.943 46.853 1.00 18.79 O
ATOM 23 N SER A 4 26.394 55.771 48.738 1.00 6.04 N
ATOM 24 CA SER A 4 26.831 55.756 50.131 1.00 6.04 C
ATOM 25 C SER A 4 26.546 57.062 50.876 1.00 6.04 C
CONNECTIVITY SECTION
CONECT 1 2 7
CONECT 1 2 7
CONECT 2 1 3 5
CONECT 2 1 3 5
CONECT 3 2 4 9
CONECT 7 1 6 8
CONECT 8 7
CONECT 8 7
CONECT 9 3 10
CONECT 86 85 677
CONECT 320 319 2234
CONECT 330 329 367
CONECT 345 344 2234
BOOKEEPING SECTION
MASTER 252 0 9 26 4 0 12 9 4579 2 174 46
END