Header list of 1zxf.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 08-JUN-05 1ZXF TITLE SOLUTION STRUCTURE OF A SELF-SACRIFICING RESISTANCE PROTEIN, CALC FROM TITLE 2 MICROMONOSPORA ECHINOSPORA COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALC; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA ECHINOSPORA; SOURCE 3 ORGANISM_TAXID: 1877; SOURCE 4 GENE: CALC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11B KEYWDS SELF-SACRIFICING RESISTANCE PROTEIN, STRUCTURAL GENOMICS, PSI, KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL KEYWDS 3 GENOMICS, CESG, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.SINGH,M.H.HAGER,C.ZHANG,B.R.GRIFFITH,M.S.LEE,K.HALLENGA, AUTHOR 2 J.L.MARKLEY,J.S.THORSON,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS AUTHOR 3 (CESG) REVDAT 6 02-MAR-22 1ZXF 1 REMARK REVDAT 5 24-FEB-09 1ZXF 1 VERSN REVDAT 4 20-MAY-08 1ZXF 1 JRNL REVDAT 3 22-AUG-06 1ZXF 1 JRNL REVDAT 2 10-JAN-06 1ZXF 1 REMARK REVDAT 1 13-DEC-05 1ZXF 0 JRNL AUTH S.SINGH,M.H.HAGER,C.ZHANG,B.R.GRIFFITH,M.S.LEE,K.HALLENGA, JRNL AUTH 2 J.L.MARKLEY,J.S.THORSON JRNL TITL STRUCTURAL INSIGHT INTO THE SELF-SACRIFICE MECHANISM OF JRNL TITL 2 ENEDIYNE RESISTANCE. JRNL REF ACS CHEM.BIOL. V. 1 451 2006 JRNL REFN ISSN 1554-8929 JRNL PMID 17168523 JRNL DOI 10.1021/CB6002898 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.B.BIGGINS,K.C.ONWUEME,J.S.THORSON REMARK 1 TITL RESISTANCE TO ENEDIYNE ANTITUMOR ANTIBIOTICS BY CALC REMARK 1 TITL 2 SELF-SACRIFICE. REMARK 1 REF SCIENCE V. 301 1537 2003 REMARK 1 REFN ISSN 0036-8075 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.AHLERT,E.SHEPARD,N.LOMOVSKAYA,E.ZAZOPOULOS,A.STAFFA, REMARK 1 AUTH 2 B.O.BACHMANN,K.HUANG,L.FONSTEIN,A.CZISNY,R.E.WHITWAM, REMARK 1 AUTH 3 C.M.FARNET,J.S.THORSON REMARK 1 TITL THE CALICHEAMICIN GENE CLUSTER AND ITS ITERATIVE TYPE I REMARK 1 TITL 2 ENEDIYNE PKS. REMARK 1 REF SCIENCE V. 297 1173 2002 REMARK 1 REFN ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.2, ARIA 1.2 REMARK 3 AUTHORS : F. DELAGLIO (NMRPIPE), MICHAEL NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 3042 RESTRAINTS, 2766 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 176 DIHEDRAL ANGLE RESTRAINTS,100 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1ZXF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033231. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 293 REMARK 210 PH : 7.3; 7.3 REMARK 210 IONIC STRENGTH : 150 MM NACL; 150 MM NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM CALC U-15N,13C; 10MM REMARK 210 PHOSPHATE BUFFER, 150 MM NACL, REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, CNS 1.1, ARIA 1.2 REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NOESY MIXING TIME = 100 MS REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HB2 ALA A 42 HB3 GLU A 55 1.24 REMARK 500 HB2 PRO A 32 HD13 ILE A 140 1.30 REMARK 500 OE2 GLU A 55 HH22 ARG A 82 1.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 2 TYR A 54 CE1 TYR A 54 CZ -0.099 REMARK 500 2 TYR A 54 CZ TYR A 54 CE2 0.099 REMARK 500 3 TYR A 54 CE1 TYR A 54 CZ -0.082 REMARK 500 3 TYR A 54 CZ TYR A 54 CE2 0.078 REMARK 500 10 TYR A 54 CE1 TYR A 54 CZ -0.104 REMARK 500 10 TYR A 54 CZ TYR A 54 CE2 0.104 REMARK 500 19 TYR A 2 CE1 TYR A 2 CZ 0.086 REMARK 500 19 TYR A 2 CZ TYR A 2 CE2 -0.094 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 TYR A 2 -40.78 69.87 REMARK 500 1 ALA A 14 47.09 -156.03 REMARK 500 1 ASP A 15 163.17 75.07 REMARK 500 1 TRP A 30 -155.87 -90.60 REMARK 500 1 PRO A 32 -140.74 -88.32 REMARK 500 1 THR A 38 8.16 57.06 REMARK 500 1 LYS A 39 -73.53 -91.48 REMARK 500 1 VAL A 40 18.32 -147.08 REMARK 500 1 PRO A 43 62.44 -65.01 REMARK 500 1 LEU A 44 -91.13 -170.51 REMARK 500 1 GLU A 73 -172.93 49.43 REMARK 500 1 PRO A 74 77.33 -63.48 REMARK 500 1 ASP A 75 -68.37 -159.72 REMARK 500 1 ARG A 82 -78.34 -125.43 REMARK 500 1 LEU A 83 146.95 172.00 REMARK 500 1 ASN A 93 -80.68 -141.87 REMARK 500 1 SER A 94 -125.89 -78.41 REMARK 500 1 SER A 95 -75.29 70.85 REMARK 500 1 GLU A 96 116.37 60.40 REMARK 500 1 GLN A 106 39.50 -85.12 REMARK 500 1 HIS A 117 -69.21 -178.98 REMARK 500 1 ALA A 153 13.65 -144.19 REMARK 500 2 TYR A 2 -30.64 169.96 REMARK 500 2 PRO A 4 -68.02 -91.23 REMARK 500 2 ALA A 14 31.04 -148.23 REMARK 500 2 ASP A 15 167.26 72.32 REMARK 500 2 PRO A 32 -123.88 -71.54 REMARK 500 2 LYS A 39 -59.67 -127.48 REMARK 500 2 VAL A 40 28.26 -157.72 REMARK 500 2 PRO A 43 -5.12 -50.05 REMARK 500 2 LEU A 44 -85.31 -105.33 REMARK 500 2 GLU A 61 74.56 57.35 REMARK 500 2 PHE A 65 -58.43 -146.93 REMARK 500 2 LYS A 70 108.96 -165.79 REMARK 500 2 GLU A 73 -170.69 47.15 REMARK 500 2 PRO A 74 78.26 -64.71 REMARK 500 2 ASP A 75 -67.31 -161.76 REMARK 500 2 ARG A 82 23.16 -148.54 REMARK 500 2 LEU A 83 145.48 78.48 REMARK 500 2 ASN A 84 48.47 -77.85 REMARK 500 2 ASP A 92 -6.59 70.06 REMARK 500 2 ASN A 93 -64.69 -137.89 REMARK 500 2 HIS A 117 -78.13 99.22 REMARK 500 2 MET A 121 25.14 -78.08 REMARK 500 2 ALA A 153 81.48 -173.25 REMARK 500 2 LYS A 154 85.48 -163.13 REMARK 500 3 TYR A 2 -80.54 86.67 REMARK 500 3 ALA A 14 33.10 -153.74 REMARK 500 3 ASP A 15 165.67 73.43 REMARK 500 3 GLU A 25 33.70 -98.89 REMARK 500 REMARK 500 THIS ENTRY HAS 480 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.79751 RELATED DB: TARGETDB DBREF 1ZXF A 1 155 UNP Q8KNF0 Q8KNF0_MICEC 27 181 SEQRES 1 A 155 ASN TYR ASP PRO PHE VAL ARG HIS SER VAL THR VAL LYS SEQRES 2 A 155 ALA ASP ARG LYS THR ALA PHE LYS THR PHE LEU GLU GLY SEQRES 3 A 155 PHE PRO GLU TRP TRP PRO ASN ASN PHE ARG THR THR LYS SEQRES 4 A 155 VAL GLY ALA PRO LEU GLY VAL ASP LYS LYS GLY GLY ARG SEQRES 5 A 155 TRP TYR GLU ILE ASP GLU GLN GLY GLU GLU HIS THR PHE SEQRES 6 A 155 GLY LEU ILE ARG LYS VAL ASP GLU PRO ASP THR LEU VAL SEQRES 7 A 155 ILE GLY TRP ARG LEU ASN GLY PHE GLY ARG ILE ASP PRO SEQRES 8 A 155 ASP ASN SER SER GLU PHE THR VAL THR PHE VAL ALA ASP SEQRES 9 A 155 GLY GLN LYS LYS THR ARG VAL ASP VAL GLU HIS THR HIS SEQRES 10 A 155 PHE ASP ARG MET GLY THR LYS HIS ALA LYS ARG VAL ARG SEQRES 11 A 155 ASN GLY MET ASP LYS GLY TRP PRO THR ILE LEU GLN SER SEQRES 12 A 155 PHE GLN ASP LYS ILE ASP GLU GLU GLY ALA LYS LYS HELIX 1 1 ALA A 14 LEU A 24 1 11 HELIX 2 2 PRO A 32 ARG A 36 5 5 HELIX 3 3 GLY A 122 ASP A 134 1 13 HELIX 4 4 GLY A 136 ALA A 153 1 18 SHEET 1 A 7 VAL A 6 VAL A 12 0 SHEET 2 A 7 LYS A 108 HIS A 115 -1 O THR A 109 N VAL A 12 SHEET 3 A 7 PHE A 97 ASP A 104 -1 N THR A 100 O ASP A 112 SHEET 4 A 7 THR A 76 GLY A 80 -1 N LEU A 77 O VAL A 99 SHEET 5 A 7 GLY A 66 ASP A 72 -1 N ARG A 69 O VAL A 78 SHEET 6 A 7 ARG A 52 TYR A 54 -1 N TRP A 53 O GLY A 66 SHEET 7 A 7 GLY A 45 ASP A 47 -1 N ASP A 47 O ARG A 52 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - r 2 2 Bytes