Header list of 1ysx.pdb file
Complete list - 2 20 Bytes
HEADER APOPTOSIS 09-FEB-05 1YSX TITLE SOLUTION STRUCTURE OF DOMAIN 3 FROM HUMAN SERUM ALBUMIN COMPLEXED TO TITLE 2 AN ANTI-APOPTOTIC LIGAND DIRECTED AGAINST BCL-XL AND BCL-2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SERUM ALBUMIN; COMPND 3 CHAIN: A; COMPND 4 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: ALB; 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: PET15B 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 3 02-MAR-22 1YSX 1 REMARK REVDAT 2 24-FEB-09 1YSX 1 VERSN REVDAT 1 07-JUN-05 1YSX 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 1YSX 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_1000031893. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 200 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM HUMAN SERUM ALBUMIN REMARK 210 DOMAIN 3 U-15N,13C, 50 MM SODIUM REMARK 210 PHOSPHATE, 150 MM SODIUM REMARK 210 CHLORIDE, 0.1 MM EDTA, 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 : 800 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 RES C SSSEQI REMARK 465 LEU A 585 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 LEU A 398 -63.34 -99.92 REMARK 500 GLN A 417 44.45 73.35 REMARK 500 SER A 419 151.55 62.04 REMARK 500 CYS A 438 73.01 -171.42 REMARK 500 LYS A 439 -38.28 177.97 REMARK 500 PRO A 468 71.10 -69.10 REMARK 500 SER A 470 -174.26 69.99 REMARK 500 ASP A 471 -76.08 -137.73 REMARK 500 SER A 480 32.53 -98.72 REMARK 500 LEU A 481 144.14 63.60 REMARK 500 VAL A 482 -3.76 80.37 REMARK 500 ASN A 483 31.52 -141.63 REMARK 500 THR A 496 49.50 -95.83 REMARK 500 THR A 506 -179.21 -65.63 REMARK 500 PHE A 507 118.92 65.66 REMARK 500 HIS A 510 156.64 63.10 REMARK 500 THR A 515 -48.94 -153.00 REMARK 500 SER A 517 104.64 62.78 REMARK 500 GLN A 526 -45.13 -176.90 REMARK 500 LYS A 536 84.24 -165.62 REMARK 500 PRO A 537 173.45 -51.77 REMARK 500 LYS A 538 93.07 70.19 REMARK 500 LYS A 560 33.84 -168.09 REMARK 500 ASP A 563 58.32 -111.50 REMARK 500 ALA A 582 167.99 174.25 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 4EB A 1000 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1YSG RELATED DB: PDB REMARK 900 RELATED ID: 1YSI RELATED DB: PDB REMARK 900 RELATED ID: 1YSN RELATED DB: PDB REMARK 900 RELATED ID: 1YSW RELATED DB: PDB DBREF 1YSX A 385 585 UNP P02768 ALBU_HUMAN 409 609 SEQRES 1 A 201 GLN ASN LEU ILE LYS GLN ASN CYS GLU LEU PHE GLU GLN SEQRES 2 A 201 LEU GLY GLU TYR LYS PHE GLN ASN ALA LEU LEU VAL ARG SEQRES 3 A 201 TYR THR LYS LYS VAL PRO GLN VAL SER THR PRO THR LEU SEQRES 4 A 201 VAL GLU VAL SER ARG ASN LEU GLY LYS VAL GLY SER LYS SEQRES 5 A 201 CYS CYS LYS HIS PRO GLU ALA LYS ARG MET PRO CYS ALA SEQRES 6 A 201 GLU ASP TYR LEU SER VAL VAL LEU ASN GLN LEU CYS VAL SEQRES 7 A 201 LEU HIS GLU LYS THR PRO VAL SER ASP ARG VAL THR LYS SEQRES 8 A 201 CYS CYS THR GLU SER LEU VAL ASN ARG ARG PRO CYS PHE SEQRES 9 A 201 SER ALA LEU GLU VAL ASP GLU THR TYR VAL PRO LYS GLU SEQRES 10 A 201 PHE ASN ALA GLU THR PHE THR PHE HIS ALA ASP ILE CYS SEQRES 11 A 201 THR LEU SER GLU LYS GLU ARG GLN ILE LYS LYS GLN THR SEQRES 12 A 201 ALA LEU VAL GLU LEU VAL LYS HIS LYS PRO LYS ALA THR SEQRES 13 A 201 LYS GLU GLN LEU LYS ALA VAL MET ASP ASP PHE ALA ALA SEQRES 14 A 201 PHE VAL GLU LYS CYS CYS LYS ALA ASP ASP LYS GLU THR SEQRES 15 A 201 CYS PHE ALA GLU GLU GLY LYS LYS LEU VAL ALA ALA SER SEQRES 16 A 201 GLN ALA ALA LEU GLY LEU HET 4EB A1000 66 HETNAM 4EB 4-({2-[(2,4-DIMETHYLPHENYL)SULFANYL]ETHYL}AMINO)-N- HETNAM 2 4EB [(4'-FLUORO-1,1'-BIPHENYL-4-YL)CARBONYL]-3- HETNAM 3 4EB NITROBENZENESULFONAMIDE FORMUL 2 4EB C29 H26 F N3 O5 S2 HELIX 1 1 GLN A 385 GLY A 399 1 15 HELIX 2 2 GLU A 400 VAL A 415 1 16 HELIX 3 3 SER A 419 CYS A 437 1 19 HELIX 4 4 PRO A 441 THR A 467 1 27 HELIX 5 5 ASP A 471 CYS A 476 1 6 HELIX 6 6 ASN A 483 LEU A 491 1 9 HELIX 7 7 ALA A 511 THR A 515 5 5 HELIX 8 8 GLU A 520 LYS A 536 1 17 HELIX 9 9 THR A 540 CYS A 559 1 20 HELIX 10 10 ASP A 563 ALA A 582 1 20 SITE 1 AC1 12 ASN A 391 CYS A 392 LEU A 407 TYR A 411 SITE 2 AC1 12 LYS A 414 VAL A 415 THR A 422 LEU A 423 SITE 3 AC1 12 VAL A 426 TYR A 452 LEU A 460 HIS A 464 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