Header list of 1ysi.pdb file
Complete list - 2 20 Bytes
HEADER APOPTOSIS 08-FEB-05 1YSI TITLE SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-XL IN COMPLEX TITLE 2 WITH AN ACYL-SULFONAMIDE-BASED LIGAND COMPND MOL_ID: 1; COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-X; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: BCL-2-LIKE 1 PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: BCL2L1, BCL2L, BCLX; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30B KEYWDS COMPLEX, APOPTOSIS EXPDTA SOLUTION NMR AUTHOR T.OLTERSDORF,S.W.ELMORE,A.R.SHOEMAKER,R.C.ARMSTRONG,D.J.AUGERI, AUTHOR 2 B.A.BELLI,M.BRUNCKO,T.L.DECKWERTH,J.DINGES,P.J.HAJDUK,M.K.JOSEPH, AUTHOR 3 S.KITADA,S.J.KORSMEYER,A.R.KUNZER,A.LETAI,C.LI,M.J.MITTEN, AUTHOR 4 D.G.NETTESHEIM,S.NG,P.M.NIMMER,J.M.O'CONNOR,A.OLEKSIJEW,A.M.PETROS, AUTHOR 5 J.C.REED,W.SHEN,S.K.TAHIR,C.B.THOMPSON,K.J.TOMASELLI,B.WANG, AUTHOR 6 M.D.WENDT,H.ZHANG,S.W.FESIK,S.H.ROSENBERG REVDAT 4 02-MAR-22 1YSI 1 REMARK SEQADV ATOM REVDAT 3 24-FEB-09 1YSI 1 VERSN REVDAT 2 23-OCT-07 1YSI 1 REMARK REVDAT 1 07-JUN-05 1YSI 0 JRNL AUTH T.OLTERSDORF,S.W.ELMORE,A.R.SHOEMAKER,R.C.ARMSTRONG, JRNL AUTH 2 D.J.AUGERI,B.A.BELLI,M.BRUNCKO,T.L.DECKWERTH,J.DINGES, JRNL AUTH 3 P.J.HAJDUK,M.K.JOSEPH,S.KITADA,S.J.KORSMEYER,A.R.KUNZER, JRNL AUTH 4 A.LETAI,C.LI,M.J.MITTEN,D.G.NETTESHEIM,S.NG,P.M.NIMMER, JRNL AUTH 5 J.M.O'CONNOR,A.OLEKSIJEW,A.M.PETROS,J.C.REED,W.SHEN, JRNL AUTH 6 S.K.TAHIR,C.B.THOMPSON,K.J.TOMASELLI,B.WANG,M.D.WENDT, JRNL AUTH 7 H.ZHANG,S.W.FESIK,S.H.ROSENBERG JRNL TITL AN INHIBITOR OF BCL-2 FAMILY PROTEINS INDUCES REGRESSION OF JRNL TITL 2 SOLID TUMOURS JRNL REF NATURE V. 435 677 2005 JRNL REFN ISSN 0028-0836 JRNL PMID 15902208 JRNL DOI 10.1038/NATURE03579 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1YSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000031880. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 50 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM BCL-XL U-15N,13C 50MM SODIUM REMARK 210 PHOSPHATE, 5 MM DEUTERATED REMARK 210 DITHIOTHREITOL, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_13C REMARK 210 -EDITED_12C-FILTERED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL 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: 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 MET A 3 55.83 34.65 REMARK 500 GLN A 7 33.99 -164.78 REMARK 500 ASN A 9 -52.94 -122.23 REMARK 500 SER A 27 -158.15 66.24 REMARK 500 TRP A 28 -45.25 -150.55 REMARK 500 PHE A 31 -72.29 -55.81 REMARK 500 ASP A 33 -124.27 62.74 REMARK 500 VAL A 34 140.82 79.54 REMARK 500 ASN A 37 -79.24 -54.36 REMARK 500 ARG A 38 -71.15 174.13 REMARK 500 THR A 39 61.85 65.16 REMARK 500 GLU A 43 -84.79 61.03 REMARK 500 THR A 45 -43.06 -165.08 REMARK 500 GLU A 46 39.75 32.78 REMARK 500 GLU A 102 48.61 -92.42 REMARK 500 LEU A 103 -57.66 -150.85 REMARK 500 TYR A 105 76.55 -102.40 REMARK 500 ALA A 108 -70.82 -105.86 REMARK 500 ALA A 123 -77.79 179.52 REMARK 500 LYS A 161 -76.41 -78.20 REMARK 500 GLU A 162 37.76 -178.06 REMARK 500 ASP A 180 13.46 -141.44 REMARK 500 LEU A 182 -36.74 -177.62 REMARK 500 ASN A 202 54.86 -142.22 REMARK 500 ARG A 208 -81.35 64.29 REMARK 500 LYS A 209 -97.96 -58.83 REMARK 500 GLN A 211 -89.88 -52.58 REMARK 500 GLU A 212 75.69 52.84 REMARK 500 ARG A 213 -69.03 69.52 REMARK 500 LEU A 214 32.81 -165.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 10 0.29 SIDE CHAIN REMARK 500 ARG A 38 0.32 SIDE CHAIN REMARK 500 ARG A 95 0.27 SIDE CHAIN REMARK 500 ARG A 104 0.30 SIDE CHAIN REMARK 500 ARG A 106 0.27 SIDE CHAIN REMARK 500 ARG A 107 0.28 SIDE CHAIN REMARK 500 ARG A 136 0.28 SIDE CHAIN REMARK 500 ARG A 143 0.20 SIDE CHAIN REMARK 500 ARG A 169 0.31 SIDE CHAIN REMARK 500 ARG A 208 0.31 SIDE CHAIN REMARK 500 ARG A 213 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N3B A 1000 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LXL RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF SAME PROTEIN, UNCOMPLEXED REMARK 900 RELATED ID: 1MAZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF SAME PROTEIN, UNCOMPLEXED REMARK 900 RELATED ID: 1BXL RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF SAME PROTEIN COMPLEXED WITH BAK PEPTIDE REMARK 900 RELATED ID: 1G5J RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF SAME PROTEIN COMPLEXED WITH BAD PEPTIDE REMARK 900 RELATED ID: 1YSG RELATED DB: PDB REMARK 900 RELATED ID: 1YSX RELATED DB: PDB REMARK 900 RELATED ID: 1YSN RELATED DB: PDB REMARK 900 RELATED ID: 1YSW RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES 49-88 (SEQUENCE DATABASE RESIDUES 45-84) REMARK 999 ARE NOT PRESENT DUE TO A LOOP DELETION. DBREF 1YSI A 5 48 UNP Q07817 BCLX_HUMAN 1 44 DBREF 1YSI A 89 213 UNP Q07817 BCLX_HUMAN 85 209 SEQADV 1YSI MET A 1 UNP Q07817 EXPRESSION TAG SEQADV 1YSI SER A 2 UNP Q07817 EXPRESSION TAG SEQADV 1YSI MET A 3 UNP Q07817 EXPRESSION TAG SEQADV 1YSI ALA A 4 UNP Q07817 EXPRESSION TAG SEQADV 1YSI LEU A 214 UNP Q07817 EXPRESSION TAG SEQADV 1YSI GLU A 215 UNP Q07817 EXPRESSION TAG SEQADV 1YSI HIS A 216 UNP Q07817 EXPRESSION TAG SEQADV 1YSI HIS A 217 UNP Q07817 EXPRESSION TAG SEQADV 1YSI HIS A 218 UNP Q07817 EXPRESSION TAG SEQADV 1YSI HIS A 219 UNP Q07817 EXPRESSION TAG SEQADV 1YSI HIS A 220 UNP Q07817 EXPRESSION TAG SEQADV 1YSI HIS A 181 UNP Q07817 EXPRESSION TAG SEQRES 1 A 181 MET SER MET ALA MET SER GLN SER ASN ARG GLU LEU VAL SEQRES 2 A 181 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR SEQRES 3 A 181 SER TRP SER GLN PHE SER ASP VAL GLU GLU ASN ARG THR SEQRES 4 A 181 GLU ALA PRO GLU GLY THR GLU SER GLU ALA VAL LYS GLN SEQRES 5 A 181 ALA LEU ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR SEQRES 6 A 181 ARG ARG ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE SEQRES 7 A 181 THR PRO GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL SEQRES 8 A 181 ASN GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE SEQRES 9 A 181 VAL ALA PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SEQRES 10 A 181 SER VAL ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE SEQRES 11 A 181 ALA ALA TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU SEQRES 12 A 181 PRO TRP ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL SEQRES 13 A 181 GLU LEU TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS SEQRES 14 A 181 GLY GLN GLU ARG LEU GLU HIS HIS HIS HIS HIS HIS HET N3B A1000 60 HETNAM N3B N-[(4'-FLUORO-1,1'-BIPHENYL-4-YL)CARBONYL]-3-NITRO-4- HETNAM 2 N3B {[2-(PHENYLSULFANYL)ETHYL]AMINO}BENZENESULFONAMIDE FORMUL 2 N3B C27 H22 F N3 O5 S2 HELIX 1 1 ASN A 9 GLY A 25 1 17 HELIX 2 2 ALA A 89 TYR A 105 1 17 HELIX 3 3 PHE A 109 GLN A 115 1 7 HELIX 4 4 ALA A 123 PHE A 135 1 13 HELIX 5 5 ASN A 140 GLU A 162 1 23 HELIX 6 6 LEU A 166 ASP A 180 1 15 HELIX 7 7 LEU A 182 GLY A 190 1 9 HELIX 8 8 GLY A 191 LEU A 198 1 8 SITE 1 AC1 10 PHE A 101 TYR A 105 ALA A 108 PHE A 109 SITE 2 AC1 10 LEU A 134 ASN A 140 GLY A 142 ARG A 143 SITE 3 AC1 10 VAL A 145 TYR A 199 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
Complete list - 2 20 Bytes