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PROTEIN ENTRY:

Sample Input (hypothetical entry designed to test all sections of PDB):

HEADER IMAGINARY FIBER PROTEIN 30-JUN-99 1QT2 OBSLTE 31-JAN-94 1MBP 2MBP TITLE BUNDLE FORMING PILIN OF IMAGINARY E. COLI CAVEAT 1ABC IMAGINARY CAVEAT: THE CRYSTAL TRANSFORMATION IS IN CAVEAT 2 1ABC ERROR BUT IS UNCORRECTABLE AT THIS TIME COMPND MOL_ID: 1; COMPND 2 MOLECULE: FIBER-FORMING PROTEIN PILIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FIMBRIAE; COMPND 5 BIOLOGICAL_UNIT: MONOMER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROPATHOGENIC ESCHERICHIA COLI KEYWDS TYPE 4B PILIN, FIBER FORMING PROTEIN, BUNDLE FORMING PILIN, KEYWDS 2 ENTEROPATHOGENIC ESCHERICHIA COLI, ADHESION, FIBER-FORMING KEYWDS 3 PROTEIN EXPDTA THEORETICAL MODEL AUTHOR R.CHATTOPADHYAYA,A.C.GHOSE REVDAT 1 12-JUL-99 1QT2 0 SPRSDE 17-JUL-84 4HHB 1HHB SPRSDE 27-FEB-95 1GDJ 1LH4 2LH4 JRNL AUTH R.CHATTOPADHYAYA,A.C.GHOSE JRNL TITL MODEL OF BUNDLE FORMING PILUS PROTEIN OF JRNL TITL 2 ENTEROPATHOGENIC ESCHERICHIA COLI JRNL REF TO BE PUBLISHED JRNL REFN 0353 JRNL AUTH G.FERMI,M.F.PERUTZ,B.SHAANAN,R.FOURME JRNL EDIT S.GREGORIO,M.CHANGHO,M.G.TORRES JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT JRNL TITL 2 1.74 A RESOLUTION JRNL REF J.MOL.BIOL. V. 175 159 1984 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.A.GIRON,A.S.Y.HO,G.K.SCHOOLNIK REMARK 1 TITL AN INDUCIBLE BUNDLE FORMING PILUS OF PATHOGENIC REMARK 1 TITL 2 ESCHERICHIA COLI REMARK 1 REF SCIENCE V. 254 710 1991 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.S.STROM,S.LORY REMARK 1 TITL STRUCTURE-FUNCTION AND BIOGENESIS OF TYPE IV PILI REMARK 1 REF ANNU.REV.MICROBIOL. V. 47 565 1993 REMARK 1 REFN US ISSN 0066-4227 DBREF 1QT2 A 1 180 SWS P33553 BFPA_ECOLI 14 193 SEQADV 1ABC ASN A 100A SWS P10725 ASP 100 1994-300-1200-0070 SEQADV 2ABC ASN A 100A SWS P10725 ASP 100 PDB: 1ABC SEQADV 3ABC MET A -1 SWS P10725 CLONING ARTIFACT SEQADV 3ABC GLY A 50 SWS P10725 VAL 50 ENGINEERED SEQRES 1 A 180 LEU SER LEU ILE GLU SER ALA MET VAL LEU ALA LEU ALA SEQRES 2 A 180 ALA THR VAL THR ALA GLY VAL MET PHE TYR TYR GLN SER SEQRES 3 A 180 ALA SER ASP GLY ASN LYS SER GLN ASN ALA ILE SER GLU SEQRES 4 A 180 VAL MET SER ALA THR SER ALA ILE ASN GLY LEU TYR ILE SEQRES 5 A 180 GLY GLN THR SER TYR SER GLY LEU ASP SER THR ILE LEU SEQRES 6 A 180 LEU ASN THR SER ALA ILE PRO ASP ASN TYR LYS ASP THR SEQRES 7 A 180 THR ASN LYS LYS ILE THR ASN PRO PHE GLY GLY GLU LEU SEQRES 8 A 180 ASN VAL GLY PRO ALA ASN ASN ASN THR ALA PHE GLY TYR SEQRES 9 A 180 TYR LEU THR LEU THR ARG LEU ASP LYS ALA ALA CYS VAL SEQRES 10 A 180 SER LEU ALA THR LEU ASN LEU GLY THR SER ALA LYS GLY SEQRES 11 A 180 TYR GLY VAL ASN ILE SER GLY GLU ASN ASN ILE THR SER SEQRES 12 A 180 PHE GLY ASN SER ALA ASP GLN ALA ALA LYS SER THR ALA SEQRES 13 A 180 ILE THR PRO ALA GLU ALA ALA THR ALA CYS LYS ASN THR SEQRES 14 A 180 ASP SER THR ASN LYS VAL THR TYR PHE MET LYS MODRES 1ABC ASN A 22A ASN GLYCOSYLATION SITE MODRES 2ABC TTQ A 50A TRP POST-TRANSLATIONAL MODIFICATION MODRES 3ABC DAL A 32 ALA POST-TRANSLATIONAL MODIFICATION,D-ALANINE MODRES 3ABC DAL B 32 ALA POST-TRANSLATIONAL MODIFICATION,D-ALANINE HET FUC Y 1 10 PART_OF: NONOATE COMPLEX; L-FUCOSE HET GAL Y 2 11 PART_OF: NONOATE COMPLEX HET NAG Y 3 15 PART_OF: NONOATE COMPLEX HET FUC Y 4 10 PART_OF: NONOATE COMPLEX HET NON Y 5 12 PART_OF: NONOATE COMPLEX HETNAM GLC GLUCOSE HETNAM SAD BETA-METHYLENE SELENAZOLE-4-CARBOXAMIDE ADENINE HETNAM 2 SAD DINUCLEOTIDE HETSYN NAD NICOTINAMIDE ADENINE DINUCLEOTIDE HETSYN COA COA HETSYN CMP CYCLIC AMP; CYCLIC ADENOSINE MONOPHOSPHATE HETSYN TRS TRIS BUFFER; TRISAMINE; HETSYN 2 TRS TRIS(HYDROXYMETHYL)AMINOMETHANE; TRIMETHYLOL HETSYN 3 TRS AMINOMETHANE FORMUL 2 SO4 2(O4 S1 2-) FORMUL 3 GLC C6 H12 O6 FORMUL 3 FOL 2(C19 H17 N7 FORMUL 3 FOL 1 O6 2-) FORMUL 4 CL 2(CL1 1-) FORMUL 5 CA CA1 2+ FORMUL 6 HOH *429(H2 O1) HELIX 1 1 SER A 2 ALA A 43 1 42 HELIX 2 2 ALA A 43 GLY A 53 1 11 HELIX 3 3 ASP A 149 ALA A 162 1 14 SHEET 1 A 3 ASN A 85 GLY A 88 0 SHEET 2 A 3 PHE A 102 THR A 109 -1 O GLY A 103 N PHE A 87 SHEET 3 A 3 LYS A 113 SER A 118 -1 N ALA A 114 O LEU A 108 SHEET 1 B 2 THR A 121 GLY A 125 0 SHEET 2 B 2 ALA A 128 TYR A 131 -1 O ALA A 128 N GLY A 125 TURN 1 S1A GLY A 16 GLN A 18 SURFACE TURN 2 FLA ILE A 50 GLY A 52 FLAP TURN 3 S2A ILE A 66 HIS A 69 SURFACE TURN 4 S1B GLY B 16 GLN B 18 SURFACE TURN 5 FLB ILE B 50 GLY B 52 FLAP TURN 6 S2B ILE B 66 HIS B 69 SURFACE SSBOND 1 CYS A 116 CYS A 166 LINK O1 DDA 1 C3 DDL 2 LINK MN MN 391 OE2 GLU 217 2565 HYDBND N 1LEU 10 AO3* NDP 501 HYDBND NH2ZARG 111 OD1 ASP 149 1555 SLTBRG O QGLU 1 10Z NZ LYS 115 SLTBRG O RGLU 2 10X NZ LYS 115 3654 CISPEP 1 GLY A 116 GLY A 117 0 18.50 CISPEP 2 THR D 92 PRO D 93 0 359.80 SITE 1 DTA 3 ASP A 25 THR A 26 GLY A 27 SITE 1 DTB 3 ASP B 25 THR B 26 GLY B 27 SITE 1 A 4 U A 44 C A 46 G A 61 U A 118 SITE 1 ZN1 5 CYS A 97 CYS A 100 CYS A 103 CYS 1 111 SITE 2 ZN1 5 ZN A 375 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 4.00000 ORIGX2 0.000000 2.000000 0.000000 5.00000 ORIGX3 0.000000 0.000000 3.000000 6.12000 SCALE1 1.000000 0.000000 0.000000 7.00000 SCALE2 0.000000 1.000000 0.000000 8.00000 SCALE3 0.000000 0.000000 1.000000 9.87000 MTRIX1 1 -1.000000 0.000000 -0.000000 0.00001 1 MTRIX2 1 -0.000000 1.000000 0.000000 0.00002 1 MTRIX3 1 0.000000 -0.000000 -1.000000 0.00002 1 TVECT 1 0.00000 0.00000 28.30000 ATOM 1 N LEU A 1 61.225 -19.114 -3.625 1.00 0.00 N ATOM 2 CA LEU A 1 61.334 -17.752 -4.207 1.00 0.00 C ATOM 3 C LEU A 1 60.139 -16.862 -3.718 1.00 0.00 C ATOM 4 O LEU A 1 59.079 -16.789 -4.353 1.00 0.00 O ATOM 5 CB LEU A 1 61.444 -17.848 -5.761 1.00 0.00 C ATOM 6 CG LEU A 1 62.766 -18.307 -6.443 1.00 0.00 C ATOM 7 CD1 LEU A 1 63.952 -17.372 -6.149 1.00 0.00 C ATOM 8 CD2 LEU A 1 63.160 -19.763 -6.147 1.00 0.00 C ATOM 9 N SER A 2 60.298 -16.179 -2.572 1.00 0.00 N ATOM 10 CA SER A 2 59.179 -15.477 -1.885 1.00 0.00 C ATOM 11 C SER A 2 58.892 -14.015 -2.380 1.00 0.00 C ATOM 230 N PRO 15 20.860 29.640 13.460 1.00 12.20 N SIGATM 230 N PRO 15 0.040 0.030 0.030 0.00 0.00 N ATOM 231 CA PRO 15 22.180 29.010 12.960 1.00 14.70 C SIGATM 231 CA PRO 15 0.060 0.040 0.050 0.00 0.00 C ATOM 232 C PRO 15 23.170 30.090 12.670 1.00 19.10 C SIGATM 232 C PRO 15 0.080 0.070 0.060 0.00 0.00 C ATOM 233 O PRO 15 24.360 29.860 12.670 1.00 17.50 O SIGATM 233 O PRO 15 0.040 0.030 0.030 0.00 0.00 O ATOM 12 O SER A 2 59.330 -13.033 -1.771 1.00 0.00 O ATOM 13 CB SER A 2 59.422 -15.586 -0.354 1.00 0.00 C ATOM 14 OG SER A 2 60.657 -14.985 0.052 1.00 0.00 O ATOM 15 N LEU A 3 58.022 -13.863 -3.414 0.00 0.00 N ATOM 16 CA LEU A 3 57.442 -12.611 -3.767 0.00 0.00 C ATOM 17 C LEU A 3 56.308 -12.410 -2.773 0.00 0.00 C ATOM 18 O LEU A 3 56.251 -11.386 -2.113 0.00 0.00 O ATOM 19 CB LEU A 3 57.035 -12.628 -5.269 0.00 0.00 C ATOM 20 CG LEU A 3 56.385 -11.332 -5.823 0.00 0.00 C TER 1312 LYS A 180 CONECT 855 1194 CONECT 1194 855 MASTER 194 0 0 3 5 0 0 6 1311 1 2 14 END

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