Header list of 1ddb.pdb file
Complete list - b 16 2 Bytes
HEADER APOPTOSIS 19-FEB-99 1DDB TITLE STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (BID); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: BID; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) KEYWDS APOPTOSIS, PROGRAMMED CELL DEATH, BCL-2 FAMILY, BH3 DOMAIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.M.MCDONNELL,D.FUSHMAN,C.MILLIMAN,S.J.KORSMEYER,D.COWBURN REVDAT 3 16-FEB-22 1DDB 1 REMARK REVDAT 2 24-FEB-09 1DDB 1 VERSN REVDAT 1 30-AUG-99 1DDB 0 JRNL AUTH J.M.MCDONNELL,D.FUSHMAN,C.L.MILLIMAN,S.J.KORSMEYER,D.COWBURN JRNL TITL SOLUTION STRUCTURE OF THE PROAPOPTOTIC MOLECULE BID: A JRNL TITL 2 STRUCTURAL BASIS FOR APOPTOTIC AGONISTS AND ANTAGONISTS. JRNL REF CELL(CAMBRIDGE,MASS.) V. 96 625 1999 JRNL REFN ISSN 0092-8674 JRNL PMID 10089878 JRNL DOI 10.1016/S0092-8674(00)80573-5 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DDB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-99. REMARK 100 THE DEPOSITION ID IS D_1000000507. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 150MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N)HSQC; (1H-13C)HSQC; HSQC REMARK 210 -J; 2D AND 3D 15N-NOESY-HMQC AND REMARK 210 TOCSY-HMQC; 13C-NOESY-HMQC; HCCH- REMARK 210 TOCSY; HNCA; HN(CO)CA; CBCANH; REMARK 210 CBCA(CO)NH; HNCO; HN(CA)CO; (1H) REMARK 210 15N-NOE; H2O-SELECTIVE 15N- REMARK 210 EDITED NOESY AND ROESY; HYDROGEN- REMARK 210 DEUTERIUM EXCHANGE REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX600; DMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR, XEASY, DIANA, DYANA, REMARK 210 THE ECEPP LIBRARY WAS USED REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: COORDINATES WERE CALCULATED FROM SOLUTION NMR DATA USING REMARK 210 THE PROGRAM DYANA. 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 O THR A 173 HD21 ASN A 176 1.28 REMARK 500 O LEU A 155 H VAL A 159 1.29 REMARK 500 O LYS A 158 H HIS A 162 1.33 REMARK 500 O LEU A 127 H ALA A 130 1.35 REMARK 500 O ALA A 156 H ALA A 160 1.43 REMARK 500 O PHE A 113 H ASN A 115 1.47 REMARK 500 O MET A 151 HD23 LEU A 155 1.48 REMARK 500 O LEU A 166 H VAL A 170 1.49 REMARK 500 O ALA A 130 H VAL A 134 1.53 REMARK 500 O MET A 153 H LYS A 157 1.58 REMARK 500 HG1 THR A 152 O THR A 174 1.59 REMARK 500 O LEU A 109 H GLN A 112 1.59 REMARK 500 O PHE A 177 H ASN A 181 1.60 REMARK 500 OG1 THR A 152 O THR A 173 1.90 REMARK 500 O MET A 151 CD2 LEU A 155 1.98 REMARK 500 O LYS A 158 N HIS A 162 2.00 REMARK 500 O LEU A 155 N VAL A 159 2.18 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 ASP A 2 127.36 168.62 REMARK 500 1 SER A 3 128.60 175.94 REMARK 500 1 GLU A 4 120.73 175.95 REMARK 500 1 SER A 6 129.04 166.69 REMARK 500 1 ASN A 7 160.70 176.48 REMARK 500 1 LEU A 11 135.84 66.26 REMARK 500 1 ALA A 13 129.00 74.03 REMARK 500 1 SER A 28 -141.87 -145.29 REMARK 500 1 CYS A 30 -110.03 -56.06 REMARK 500 1 ARG A 40 97.38 -50.65 REMARK 500 1 PRO A 43 -163.72 -75.04 REMARK 500 1 GLN A 45 -92.09 159.73 REMARK 500 1 ALA A 46 63.07 174.21 REMARK 500 1 TYR A 47 164.19 -41.19 REMARK 500 1 TRP A 48 136.99 161.10 REMARK 500 1 GLU A 49 -150.64 -146.10 REMARK 500 1 ALA A 50 163.67 162.63 REMARK 500 1 ASP A 51 108.09 -172.24 REMARK 500 1 LEU A 52 150.44 -35.22 REMARK 500 1 SER A 61 153.34 79.05 REMARK 500 1 GLN A 62 -66.88 -134.91 REMARK 500 1 SER A 66 105.66 -35.92 REMARK 500 1 PHE A 67 93.88 -177.88 REMARK 500 1 ASN A 68 156.73 176.22 REMARK 500 1 GLN A 69 73.85 -175.17 REMARK 500 1 ARG A 71 45.12 -149.38 REMARK 500 1 SER A 78 102.85 -162.56 REMARK 500 1 GLU A 81 115.87 66.74 REMARK 500 1 ASP A 98 -29.36 -39.06 REMARK 500 1 ILE A 101 72.69 -118.73 REMARK 500 1 GLN A 102 55.85 157.95 REMARK 500 1 THR A 104 7.59 177.58 REMARK 500 1 LEU A 105 32.19 105.47 REMARK 500 1 VAL A 106 -82.45 -63.17 REMARK 500 1 MET A 114 65.39 -55.04 REMARK 500 1 LEU A 118 90.01 -178.39 REMARK 500 1 ASP A 122 106.40 154.48 REMARK 500 1 ARG A 124 -29.98 166.72 REMARK 500 1 LEU A 127 -70.63 -51.32 REMARK 500 1 PHE A 138 62.53 -117.78 REMARK 500 1 ARG A 140 -169.50 155.01 REMARK 500 1 ASP A 141 -103.64 -89.44 REMARK 500 1 ASN A 181 -154.35 -101.31 REMARK 500 1 PHE A 183 -86.62 22.17 REMARK 500 1 MET A 194 138.47 70.51 REMARK 500 2 GLU A 4 71.29 -101.47 REMARK 500 2 SER A 6 143.42 63.97 REMARK 500 2 LYS A 14 -38.68 -179.90 REMARK 500 2 ILE A 16 -8.92 -55.21 REMARK 500 2 ARG A 40 131.99 175.39 REMARK 500 REMARK 500 THIS ENTRY HAS 1007 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1DDB A 1 195 UNP P70444 BID_MOUSE 1 195 SEQRES 1 A 195 MET ASP SER GLU VAL SER ASN GLY SER GLY LEU GLY ALA SEQRES 2 A 195 LYS HIS ILE THR ASP LEU LEU VAL PHE GLY PHE LEU GLN SEQRES 3 A 195 SER SER GLY CYS THR ARG GLN GLU LEU GLU VAL LEU GLY SEQRES 4 A 195 ARG GLU LEU PRO VAL GLN ALA TYR TRP GLU ALA ASP LEU SEQRES 5 A 195 GLU ASP GLU LEU GLN THR ASP GLY SER GLN ALA SER ARG SEQRES 6 A 195 SER PHE ASN GLN GLY ARG ILE GLU PRO ASP SER GLU SER SEQRES 7 A 195 GLN GLU GLU ILE ILE HIS ASN ILE ALA ARG HIS LEU ALA SEQRES 8 A 195 GLN ILE GLY ASP GLU MET ASP HIS ASN ILE GLN PRO THR SEQRES 9 A 195 LEU VAL ARG GLN LEU ALA ALA GLN PHE MET ASN GLY SER SEQRES 10 A 195 LEU SER GLU GLU ASP LYS ARG ASN CYS LEU ALA LYS ALA SEQRES 11 A 195 LEU ASP GLU VAL LYS THR ALA PHE PRO ARG ASP MET GLU SEQRES 12 A 195 ASN ASP LYS ALA MET LEU ILE MET THR MET LEU LEU ALA SEQRES 13 A 195 LYS LYS VAL ALA SER HIS ALA PRO SER LEU LEU ARG ASP SEQRES 14 A 195 VAL PHE HIS THR THR VAL ASN PHE ILE ASN GLN ASN LEU SEQRES 15 A 195 PHE SER TYR VAL ARG ASN LEU VAL ARG ASN GLU MET ASP HELIX 1 1 HIS A 15 SER A 27 1 13 HELIX 2 2 ARG A 32 GLY A 39 1 8 HELIX 3 3 ILE A 83 ASN A 100 1 18 HELIX 4 4 VAL A 106 PHE A 113 1 8 HELIX 5 5 ASN A 125 PHE A 138 1 14 HELIX 6 6 MET A 142 HIS A 162 1 21 HELIX 7 7 LEU A 167 GLN A 180 1 14 HELIX 8 8 TYR A 185 ASN A 192 1 8 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 - b 16 2 Bytes