Header list of 1g3f.pdb file
Complete list - 23 20 Bytes
HEADER APOPTOSIS 24-OCT-00 1G3F TITLE NMR STRUCTURE OF A 9 RESIDUE PEPTIDE FROM SMAC/DIABLO COMPLEXED TO THE TITLE 2 BIR3 DOMAIN OF XIAP COMPND MOL_ID: 1; COMPND 2 MOLECULE: INHIBITOR OF APOPTOSIS PROTEIN 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 241-356; COMPND 5 SYNONYM: X-LINKED INHIBITOR OF APOPTOSIS PROTEIN, XIAP; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: SMAC; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: 9 RESIDUE PEPTIDE; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B; SOURCE 9 MOL_ID: 2; SOURCE 10 SYNTHETIC: YES; SOURCE 11 OTHER_DETAILS: THE 9 RESIDUE PEPTIDE WAS CHEMICALLY SYNTHESIZED. KEYWDS ZINC FINGER, COMPLEX, PEPTIDE-PROTEIN, APOPTOSIS, BIR EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR Z.LIU,C.SUN,E.T.OLEJNICZAK,R.P.MEADOWS,S.F.BETZ,T.OOST,J.HERRMANN, AUTHOR 2 J.C.WU,S.W.FESIK REVDAT 4 23-FEB-22 1G3F 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1G3F 1 VERSN REVDAT 2 30-SEP-03 1G3F 1 DBREF REVDAT 1 10-JAN-01 1G3F 0 JRNL AUTH Z.LIU,C.SUN,E.T.OLEJNICZAK,R.P.MEADOWS,S.F.BETZ,T.OOST, JRNL AUTH 2 J.HERRMANN,J.C.WU,S.W.FESIK JRNL TITL STRUCTURAL BASIS FOR BINDING OF SMAC/DIABLO TO THE XIAP BIR3 JRNL TITL 2 DOMAIN. JRNL REF NATURE V. 408 1004 2000 JRNL REFN ISSN 0028-0836 JRNL PMID 11140637 JRNL DOI 10.1038/35050006 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNX 2000 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1G3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-00. REMARK 100 THE DEPOSITION ID IS D_1000012184. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN/PEPTIDE COMPLEX, REMARK 210 120 MM NACL, 1MM DTT, 10MM REMARK 210 PHOSPHATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 SER A 241 99.10 -69.59 REMARK 500 ASP A 242 -64.87 -108.37 REMARK 500 ALA A 243 176.01 72.46 REMARK 500 SER A 246 57.51 -169.02 REMARK 500 ASP A 247 -74.85 -174.86 REMARK 500 ASN A 249 -161.57 -65.40 REMARK 500 PHE A 250 103.29 -38.60 REMARK 500 PRO A 251 -70.53 -54.73 REMARK 500 ASN A 252 -73.70 -47.94 REMARK 500 SER A 253 -30.29 165.70 REMARK 500 THR A 254 -36.24 -175.53 REMARK 500 ASN A 255 150.20 -39.88 REMARK 500 ARG A 258 -176.98 49.52 REMARK 500 ASN A 259 123.74 170.26 REMARK 500 SER A 261 -35.79 -35.89 REMARK 500 ALA A 263 53.90 -104.68 REMARK 500 ASP A 264 -98.85 -96.47 REMARK 500 TYR A 265 -71.19 -48.35 REMARK 500 ALA A 267 -71.40 -44.77 REMARK 500 TRP A 275 154.51 -41.02 REMARK 500 ILE A 276 127.52 -178.69 REMARK 500 LEU A 292 40.46 -104.67 REMARK 500 ASP A 296 -72.45 86.60 REMARK 500 HIS A 302 -62.31 70.28 REMARK 500 ASP A 309 57.36 70.51 REMARK 500 TRP A 310 -178.20 -52.76 REMARK 500 GLN A 319 -71.68 -67.11 REMARK 500 PRO A 325 64.80 -68.23 REMARK 500 LEU A 344 -40.64 168.46 REMARK 500 LEU A 348 -176.46 61.19 REMARK 500 GLU A 349 99.28 66.06 REMARK 500 GLU A 350 -141.90 -119.55 REMARK 500 CYS A 351 -3.14 84.11 REMARK 500 VAL A 353 -66.73 69.65 REMARK 500 ILE B 904 -80.38 -47.80 REMARK 500 ALA B 905 -82.89 60.08 REMARK 500 GLN B 906 -82.61 62.23 REMARK 500 LYS B 907 -90.66 40.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 999 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 300 SG REMARK 620 2 CYS A 303 SG 107.5 REMARK 620 3 HIS A 320 ND1 107.2 113.1 REMARK 620 4 CYS A 327 SG 108.5 108.6 111.7 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999 DBREF 1G3F A 241 356 UNP P98170 BIRC4_HUMAN 241 356 DBREF 1G3F B 901 909 UNP Q9NR28 DBLOH_HUMAN 56 64 SEQADV 1G3F MET A 240 UNP P98170 CLONING ARTIFACT SEQRES 1 A 117 MET SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SEQRES 2 A 117 SER THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR SEQRES 3 A 117 GLU ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER SEQRES 4 A 117 VAL ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA SEQRES 5 A 117 LEU GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY SEQRES 6 A 117 GLY GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP SEQRES 7 A 117 GLU GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU SEQRES 8 A 117 LEU GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS SEQRES 9 A 117 LEU THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR SEQRES 1 B 9 ALA VAL PRO ILE ALA GLN LYS SER GLU HET ZN A 999 1 HETNAM ZN ZINC ION FORMUL 3 ZN ZN 2+ HELIX 1 1 ALA A 243 ASP A 247 5 5 HELIX 2 2 ASP A 264 GLY A 273 1 10 HELIX 3 3 ASN A 280 GLY A 288 1 9 HELIX 4 4 ASP A 315 TYR A 324 1 10 HELIX 5 5 CYS A 327 GLY A 335 1 9 HELIX 6 6 LYS A 334 HIS A 343 1 10 SHEET 1 A 4 PHE A 289 ALA A 291 0 SHEET 2 A 4 VAL A 298 CYS A 300 -1 O LYS A 299 N TYR A 290 SHEET 3 A 4 GLY A 306 THR A 308 -1 N LEU A 307 O VAL A 298 SHEET 4 A 4 VAL B 902 PRO B 903 -1 N VAL B 902 O THR A 308 LINK SG CYS A 300 ZN ZN A 999 1555 1555 2.10 LINK SG CYS A 303 ZN ZN A 999 1555 1555 2.11 LINK ND1 HIS A 320 ZN ZN A 999 1555 1555 2.22 LINK SG CYS A 327 ZN ZN A 999 1555 1555 2.11 SITE 1 AC1 4 CYS A 300 CYS A 303 HIS A 320 CYS A 327 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 - 23 20 Bytes