Header list of 1tfq.pdb file
Complete list - 2 20 Bytes
HEADER APOPTOSIS 27-MAY-04 1TFQ
TITLE NMR STRUCTURE OF AN ANTAGONISTS OF THE XIAP-CASPASE-9 INTERACTION
TITLE 2 COMPLEXED TO THE BIR3 DOMAIN OF XIAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BIR3 OF XIAP: RESIDUES 241-356;
COMPND 5 SYNONYM: INHIBITOR OF APOPTOSIS PROTEIN 3, X-LINKED INHIBITOR OF
COMPND 6 APOPTOSIS PROTEIN, XIAP, X-LINKED IAP, IAP-LIKE PROTEIN, HILP;
COMPND 7 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: BIRC4, API3, IAP3, XIAP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS COMPLEX, LIGAND-PROTEIN, APOPTOSIS, BIR, XIAP
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR T.K.OOST,C.SUN,R.C.ARMSTRONG,A.S.AL-ASSAAD,S.F.BETZ,T.L.DECKWERTH,
AUTHOR 2 S.W.ELMORE,R.P.MEADOWS,E.T.OLEJNICZAK,A.OLEKSIJEW,T.OLTERSDORF,
AUTHOR 3 S.H.ROSENBERG,A.R.SHOEMAKER,H.ZOU,S.W.FESIK
REVDAT 3 02-MAR-22 1TFQ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1TFQ 1 VERSN
REVDAT 1 07-SEP-04 1TFQ 0
JRNL AUTH T.K.OOST,C.SUN,R.C.ARMSTRONG,A.S.AL-ASSAAD,S.F.BETZ,
JRNL AUTH 2 T.L.DECKWERTH,H.DING,S.W.ELMORE,R.P.MEADOWS,E.T.OLEJNICZAK,
JRNL AUTH 3 A.OLEKSIJEW,T.OLTERSDORF,S.H.ROSENBERG,A.R.SHOEMAKER,
JRNL AUTH 4 K.J.TOMASELLI,H.ZOU,S.W.FESIK
JRNL TITL DISCOVERY OF POTENT ANTAGONISTS OF THE ANTIAPOPTOTIC PROTEIN
JRNL TITL 2 XIAP FOR THE TREATMENT OF CANCER.
JRNL REF J.MED.CHEM. V. 47 4417 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 15317454
JRNL DOI 10.1021/JM040037K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 2000
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TFQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022609.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 20MM TRIS
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N, 0.8MM BIR3,20MM TRIS,
REMARK 210 2MMDTT, 20MM PHOSPHATE BUFFER,
REMARK 210 120MM NACL, 90%H2O, 10%D20; U-
REMARK 210 15N,13C 0.8MM BIR3, 20MM TRIS,
REMARK 210 2MMDTT, 20MM PHOSPHATE BUFFER,
REMARK 210 120MM NACL, 100%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D_13C,15N
REMARK 210 FILTERED NOESY; 2D_13C,15N
REMARK 210 FILTERED TOCSY; 3D_13C,15N
REMARK 210 FILTERED ,13C SEPARATED 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 : 1
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 ALA A 243 -176.77 63.16
REMARK 500 VAL A 244 80.29 -150.92
REMARK 500 SER A 245 -66.69 -159.55
REMARK 500 ASP A 247 -61.36 -147.84
REMARK 500 PHE A 250 72.42 59.36
REMARK 500 ASN A 252 -60.91 -151.81
REMARK 500 SER A 253 -54.37 -178.15
REMARK 500 ASN A 255 100.62 -58.70
REMARK 500 ARG A 258 -63.56 -170.11
REMARK 500 ASN A 259 74.31 57.49
REMARK 500 MET A 262 -50.38 -169.05
REMARK 500 ASP A 264 -59.76 -137.56
REMARK 500 TYR A 277 -52.06 -146.58
REMARK 500 SER A 278 -73.21 -129.35
REMARK 500 ASP A 296 -56.62 72.51
REMARK 500 LYS A 297 100.67 -53.59
REMARK 500 HIS A 302 -66.69 71.10
REMARK 500 ASP A 309 65.49 60.35
REMARK 500 SER A 313 89.11 62.36
REMARK 500 TYR A 324 87.64 -161.02
REMARK 500 LEU A 344 -49.56 -176.09
REMARK 500 LEU A 348 176.69 59.63
REMARK 500 VAL A 353 -67.46 71.76
REMARK 500 ARG A 354 51.36 -166.85
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 108.6
REMARK 620 3 HIS A 320 ND1 110.0 110.0
REMARK 620 4 CYS A 327 SG 109.2 110.1 109.0
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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 998 A 998
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TFT RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF AN ANTAGONISTS OF THE XIAP-CASPASE-9 INTERACTION
REMARK 900 COMPLEXED TO THE BIR3 DOMAIN OF XIAP
DBREF 1TFQ A 241 356 UNP P98170 BIRC4_HUMAN 241 356
SEQADV 1TFQ MET A 240 UNP P98170 INITIATING METHIONINE
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
HET ZN A 999 1
HET 998 A 998 70
HETNAM ZN ZINC ION
HETNAM 998 N-METHYLALANYL-3-METHYLVALYL-N-(1,2,3,4-
HETNAM 2 998 TETRAHYDRONAPHTHALEN-1-YL)PROLINAMIDE
HETSYN 998 1-[3,3-DIMETHYL-2-(2-METHYLAMINO-PROPIONYLAMINO)-
HETSYN 2 998 BUTYRYL]-PYRROLIDINE-2-CARBOXYLIC ACID(1,2,3,4-
HETSYN 3 998 TETRAHYDRO-NAPHTHALEN-1-YL)-AMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 998 C25 H38 N4 O3
HELIX 1 1 ASP A 264 GLY A 273 1 10
HELIX 2 2 ASN A 280 GLY A 288 1 9
HELIX 3 3 ASP A 315 TYR A 324 1 10
HELIX 4 4 CYS A 327 HIS A 343 1 17
SHEET 1 A 3 PHE A 289 ALA A 291 0
SHEET 2 A 3 VAL A 298 CYS A 300 -1 O LYS A 299 N TYR A 290
SHEET 3 A 3 GLY A 306 LEU A 307 -1 O LEU A 307 N VAL A 298
LINK SG CYS A 300 ZN ZN A 999 1555 1555 2.10
LINK SG CYS A 303 ZN ZN A 999 1555 1555 2.10
LINK ND1 HIS A 320 ZN ZN A 999 1555 1555 2.21
LINK SG CYS A 327 ZN ZN A 999 1555 1555 2.10
SITE 1 AC1 4 CYS A 300 CYS A 303 HIS A 320 CYS A 327
SITE 1 AC2 8 LYS A 297 LYS A 299 GLY A 306 LEU A 307
SITE 2 AC2 8 THR A 308 ASP A 309 GLN A 319 TRP A 323
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