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HEADER APOPTOSIS 28-SEP-99 1D2Z TITLE THREE-DIMENSIONAL STRUCTURE OF A COMPLEX BETWEEN THE DEATH TITLE 2 DOMAINS OF PELLE AND TUBE COMPND MOL_ID: 1; COMPND 2 MOLECULE: DEATH DOMAIN OF PELLE; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DEATH DOMAIN OF TUBE; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PET15(B); SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PET28(A) KEYWDS SIX-HELIX BUNDLE, LINEAR ARRAY OF DEATH DOMAINS, PLASTIC KEYWDS 2 INTERFACES, APOPTOSIS EXPDTA X-RAY DIFFRACTION AUTHOR T.XIAO,P.TOWB,S.A.WASSERMAN,S.R.SPRANG REVDAT 2 28-AUG-02 1D2Z 1 SOURCE REMARK HELIX MASTER REVDAT 1 29-NOV-99 1D2Z 0 JRNL AUTH T.XIAO,P.TOWB,S.A.WASSERMAN,S.R.SPRANG JRNL TITL THREE-DIMENSIONAL STRUCTURE OF A COMPLEX BETWEEN JRNL TITL 2 THE DEATH DOMAINS OF PELLE AND TUBE. JRNL REF CELL V. 99 545 1999 JRNL REFN ASTM CELLB5 US ISSN 0092-8674 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6 REMARK 3 NUMBER OF REFLECTIONS : 39471 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.244 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600 REMARK 3 FREE R VALUE TEST SET COUNT : 3946 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4105 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 15 REMARK 3 SOLVENT ATOMS : 266 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 35.92 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.45 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.61000 REMARK 3 B22 (A**2) : 3.02000 REMARK 3 B33 (A**2) : -10.63000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25 REMARK 3 ESD FROM SIGMAA (A) : 0.26 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.730 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.410 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.740 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.610 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 32.43 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: USED MAXIMUM LIKELIHOOD TARGET REMARK 4 REMARK 4 1D2Z COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-16) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB009749. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9810 REMARK 200 MONOCHROMATOR : MIRROR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40020 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.05500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.40 REMARK 200 R MERGE FOR SHELL (I) : 0.49900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 2000 MONOMETHYL ETHER, REMARK 280 100 MM HEPES PH 7.2-8.4 0-200 MM NACL, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 277.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.06150 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.83100 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.74750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.83100 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.06150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.74750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 22 REMARK 465 SER A 23 REMARK 465 HIS A 24 REMARK 465 MET A 25 REMARK 465 SER A 26 REMARK 465 HIS A 27 REMARK 465 LEU B 173 REMARK 465 LEU B 174 REMARK 465 GLU B 175 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 114 SD MET A 114 CE -0.040 REMARK 500 MET B 112 SD MET B 112 CE -0.035 REMARK 500 GLY C 22 N GLY C 22 CA 0.040 REMARK 500 MET D 58 SD MET D 58 CE -0.035 REMARK 500 MET D 112 SD MET D 112 CE 0.040 REMARK 500 MET D 113 SD MET D 113 CE -0.036 REMARK 500 ILE D 169 CG1 ILE D 169 CD1 -0.043 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLY B 64 N - CA - C ANGL. DEV. = 6.4 DEGREES REMARK 500 ASP B 66 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 ASN B 77 N - CA - C ANGL. DEV. = -6.5 DEGREES REMARK 500 LEU B 141 N - CA - C ANGL. DEV. = -6.4 DEGREES REMARK 500 PHE B 142 N - CA - C ANGL. DEV. = 7.0 DEGREES REMARK 500 TYR C 94 N - CA - C ANGL. DEV. = 6.4 DEGREES REMARK 500 GLY D 64 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 ASP D 66 N - CA - C ANGL. DEV. =-13.8 DEGREES REMARK 500 SER D 71 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 500 ASN D 77 N - CA - C ANGL. DEV. = -6.8 DEGREES REMARK 500 LYS D 118 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 LEU D 141 N - CA - C ANGL. DEV. = -6.9 DEGREES REMARK 500 PHE D 142 N - CA - C ANGL. DEV. = 7.3 DEGREES DBREF 1D2Z A 22 129 UNP Q05652 KPEL_DROME 26 129 DBREF 1D2Z B 23 175 UNP P22812 TUBE_DROME 23 175 DBREF 1D2Z C 22 129 UNP Q05652 KPEL_DROME 26 129 DBREF 1D2Z D 23 175 UNP P22812 TUBE_DROME 23 175 SEQADV 1D2Z GLY A 22 UNP Q05652 THR 22 CLONING ARTIFACT SEQADV 1D2Z SER A 23 UNP Q05652 ARG 23 CLONING ARTIFACT SEQADV 1D2Z HIS A 24 UNP Q05652 SER 24 CLONING ARTIFACT SEQADV 1D2Z MET A 25 UNP Q05652 ARG 25 CLONING ARTIFACT SEQADV 1D2Z GLY C 22 UNP Q05652 THR 22 CLONING ARTIFACT SEQADV 1D2Z SER C 23 UNP Q05652 ARG 23 CLONING ARTIFACT SEQADV 1D2Z HIS C 24 UNP Q05652 SER 24 CLONING ARTIFACT SEQADV 1D2Z MET C 25 UNP Q05652 ARG 25 CLONING ARTIFACT SEQRES 1 A 108 GLY SER HIS MET SER HIS LEU ASP ASN THR MET ALA ILE SEQRES 2 A 108 ARG LEU LEU PRO LEU PRO VAL ARG ALA GLN LEU CYS ALA SEQRES 3 A 108 HIS LEU ASP ALA LEU ASP VAL TRP GLN GLN LEU ALA THR SEQRES 4 A 108 ALA VAL LYS LEU TYR PRO ASP GLN VAL GLU GLN ILE SER SEQRES 5 A 108 SER GLN LYS GLN ARG GLY ARG SER ALA SER ASN GLU PHE SEQRES 6 A 108 LEU ASN ILE TRP GLY GLY GLN TYR ASN HIS THR VAL GLN SEQRES 7 A 108 THR LEU PHE ALA LEU PHE LYS LYS LEU LYS LEU HIS ASN SEQRES 8 A 108 ALA MET ARG LEU ILE LYS ASP TYR VAL SER GLU ASP LEU SEQRES 9 A 108 HIS LYS TYR ILE SEQRES 1 B 153 LEU SER SER LYS TYR SER ARG ASN THR GLU LEU ARG ARG SEQRES 2 B 153 VAL GLU ASP ASN ASP ILE TYR ARG LEU ALA LYS ILE LEU SEQRES 3 B 153 ASP GLU ASN SER CYS TRP ARG LYS LEU MET SER ILE ILE SEQRES 4 B 153 PRO LYS GLY MET ASP VAL GLN ALA CYS SER GLY ALA GLY SEQRES 5 B 153 CYS LEU ASN PHE PRO ALA GLU ILE LYS LYS GLY PHE LYS SEQRES 6 B 153 TYR THR ALA GLN ASP VAL PHE GLN ILE ASP GLU ALA ALA SEQRES 7 B 153 ASN ARG LEU PRO PRO ASP GLN SER LYS SER GLN MET MET SEQRES 8 B 153 ILE ASP GLU TRP LYS THR SER GLY LYS LEU ASN GLU ARG SEQRES 9 B 153 PRO THR VAL GLY VAL LEU LEU GLN LEU LEU VAL GLN ALA SEQRES 10 B 153 GLU LEU PHE SER ALA ALA ASP PHE VAL ALA LEU ASP PHE SEQRES 11 B 153 LEU ASN GLU SER THR PRO ALA ARG PRO VAL ASP GLY PRO SEQRES 12 B 153 GLY ALA LEU ILE SER LEU GLU LEU LEU GLU SEQRES 1 C 108 GLY SER HIS MET SER HIS LEU ASP ASN THR MET ALA ILE SEQRES 2 C 108 ARG LEU LEU PRO LEU PRO VAL ARG ALA GLN LEU CYS ALA SEQRES 3 C 108 HIS LEU ASP ALA LEU ASP VAL TRP GLN GLN LEU ALA THR SEQRES 4 C 108 ALA VAL LYS LEU TYR PRO ASP GLN VAL GLU GLN ILE SER SEQRES 5 C 108 SER GLN LYS GLN ARG GLY ARG SER ALA SER ASN GLU PHE SEQRES 6 C 108 LEU ASN ILE TRP GLY GLY GLN TYR ASN HIS THR VAL GLN SEQRES 7 C 108 THR LEU PHE ALA LEU PHE LYS LYS LEU LYS LEU HIS ASN SEQRES 8 C 108 ALA MET ARG LEU ILE LYS ASP TYR VAL SER GLU ASP LEU SEQRES 9 C 108 HIS LYS TYR ILE SEQRES 1 D 153 LEU SER SER LYS TYR SER ARG ASN THR GLU LEU ARG ARG SEQRES 2 D 153 VAL GLU ASP ASN ASP ILE TYR ARG LEU ALA LYS ILE LEU SEQRES 3 D 153 ASP GLU ASN SER CYS TRP ARG LYS LEU MET SER ILE ILE SEQRES 4 D 153 PRO LYS GLY MET ASP VAL GLN ALA CYS SER GLY ALA GLY SEQRES 5 D 153 CYS LEU ASN PHE PRO ALA GLU ILE LYS LYS GLY PHE LYS SEQRES 6 D 153 TYR THR ALA GLN ASP VAL PHE GLN ILE ASP GLU ALA ALA SEQRES 7 D 153 ASN ARG LEU PRO PRO ASP GLN SER LYS SER GLN MET MET SEQRES 8 D 153 ILE ASP GLU TRP LYS THR SER GLY LYS LEU ASN GLU ARG SEQRES 9 D 153 PRO THR VAL GLY VAL LEU LEU GLN LEU LEU VAL GLN ALA SEQRES 10 D 153 GLU LEU PHE SER ALA ALA ASP PHE VAL ALA LEU ASP PHE SEQRES 11 D 153 LEU ASN GLU SER THR PRO ALA ARG PRO VAL ASP GLY PRO SEQRES 12 D 153 GLY ALA LEU ILE SER LEU GLU LEU LEU GLU HET EPE 300 15 HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETSYN EPE HEPES FORMUL 5 EPE C8 H18 N2 O4 S FORMUL 6 HOH *266(H2 O) HELIX 1 H1 LEU A 39 LEU A 52 1 14 HELIX 2 H2 TRP A 55 ALA A 61 1 7 HELIX 3 H3 PRO A 66 ARG A 78 1 13 HELIX 4 H4 ALA A 82 TYR A 94 1 13 HELIX 5 H5 VAL A 98 LEU A 108 1 11 HELIX 6 H6 HIS A 111 ILE A 117 1 7 HELIX 7 H7 ASP B 38 ASP B 49 1 12 HELIX 8 H8 TRP B 54 ILE B 60 1 7 HELIX 9 H9 VAL B 67 SER B 71 1 5 HELIX 10 H10 PHE B 78 LYS B 84 1 7 HELIX 11 H11 GLN B 91 ARG B 102 1 12 HELIX 12 H12 LYS B 109 THR B 119 1 11 HELIX 13 H13 VAL B 129 ALA B 139 1 11 HELIX 14 H14 PHE B 142 ASP B 151 1 10 HELIX 15 H15 LEU C 39 LEU C 52 1 14 HELIX 16 H16 TRP C 55 ALA C 61 1 7 HELIX 17 H17 PRO C 66 ARG C 78 1 13 HELIX 18 H18 ALA C 82 TYR C 94 1 13 HELIX 19 H19 VAL C 98 LEU C 108 1 11 HELIX 20 H20 HIS C 111 ILE C 117 1 7 HELIX 21 H21 ASP D 38 ASP D 49 1 12 HELIX 22 H22 TRP D 54 ILE D 60 1 7 HELIX 23 H23 VAL D 67 SER D 71 1 5 HELIX 24 H24 PHE D 78 LYS D 84 1 7 HELIX 25 H25 GLN D 91 ARG D 102 1 12 HELIX 26 H26 LYS D 109 THR D 119 1 11 HELIX 27 H27 VAL D 129 ALA D 139 1 11 HELIX 28 H28 PHE D 142 ASP D 151 1 10 CRYST1 58.123 87.495 117.662 90.00 90.00 90.00 P 21 21 21 8 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 0.017205 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011429 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008499 0.00000