HEADER TRANSFERASE 02-MAY-01 1IK7 TITLE CRYSTAL STRUCTURE OF THE UNCOMPLEXED PELLE DEATH DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROBABLE SERINE/THREONINE-PROTEIN KINASE PELLE; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: DEATH DOMAIN; COMPND 5 SYNONYM: PELLE; COMPND 6 EC: 2.7.1.37; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 GENE: PELLE; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS SINGLE HELIX, MPD CRYSTALLIZATION, STRUCTURAL TRANSITION EXPDTA X-RAY DIFFRACTION AUTHOR T.XIAO,K.H.GARDNER,S.R.SPRANG REVDAT 2 25-SEP-02 1IK7 1 JRNL REVDAT 1 31-JUL-02 1IK7 0 JRNL AUTH T.XIAO,K.H.GARDNER,S.R.SPRANG JRNL TITL COSOLVENT-INDUCED TRANSFORMATION OF A DEATH DOMAIN JRNL TITL 2 TERTIARY STRUCTURE JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 11151 2002 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.79 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 361892.850 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 15265 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.239 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1550 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2181 REMARK 3 BIN R VALUE (WORKING SET) : 0.2640 REMARK 3 BIN FREE R VALUE : 0.3080 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 240 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 848 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 32 REMARK 3 SOLVENT ATOMS : 27 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 18.55000 REMARK 3 B22 (A**2) : -9.90000 REMARK 3 B33 (A**2) : -8.66000 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) : 0.29 REMARK 3 ESD FROM SIGMAA (A) : 0.22 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) : 0.33 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 0.80 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 17.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.96 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.440 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.460 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.390 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 54.12 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 : PROTEIN.PARAM REMARK 3 PARAMETER FILE 2 : WATER.PARAM REMARK 3 PARAMETER FILE 3 : MPD.PARAM REMARK 3 PARAMETER FILE 4 : TRS.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : MPD.TOP REMARK 3 TOPOLOGY FILE 4 : TRS.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD REFINEMENT TARGET REMARK 3 USING AMPLITUDES REMARK 4 REMARK 4 1IK7 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 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB013358. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-FEB-2000; 10-FEB-2000; 10- REMARK 200 FEB-2000 REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100 REMARK 200 PH : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y REMARK 200 RADIATION SOURCE : CHESS; CHESS; CHESS REMARK 200 BEAMLINE : F1; F1; F2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9470; 0.9470; 0.9795, REMARK 200 0.9791, 0.9789, 0.9778 REMARK 200 MONOCHROMATOR : YALE MIRRORS; YALE MIRRORS; REMARK 200 CRYSTAL REMARK 200 OPTICS : MIRRORS; MIRRORS; MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM REMARK 200 4; ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15711 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.06300 REMARK 200 R SYM (I) : 0.06300 REMARK 200 FOR THE DATA SET : 19.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 0.25600 REMARK 200 R SYM FOR SHELL (I) : 0.25600 REMARK 200 FOR SHELL : 3.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: MLPHARE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 45% 2-METHYL-2,4-PENTANEDIOL, TRIS, REMARK 280 0.4 M SODIUM CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 1/2+X,1/2+Y,1/2+Z REMARK 290 6555 -X,1/2-Y,Z REMARK 290 7555 1/2-X,Y,-Z REMARK 290 8555 X,-Y,1/2-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 35.05300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.59800 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.77100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.59800 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.05300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.77100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.05300 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.77100 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 51.59800 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.77100 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.05300 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 51.59800 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 2 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 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: 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 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 A 28 REMARK 465 ASP A 29 REMARK 465 ASN A 30 REMARK 465 THR A 31 REMARK 465 MET A 32 REMARK 465 ALA A 33 REMARK 465 ILE A 34 REMARK 465 ARG A 35 REMARK 465 LEU A 36 REMARK 465 LEU A 37 REMARK 465 PRO A 38 REMARK 465 LEU A 39 REMARK 465 PRO A 40 REMARK 465 VAL A 41 REMARK 465 ARG A 42 REMARK 465 ALA A 43 REMARK 465 GLN A 44 REMARK 465 LEU A 45 REMARK 465 CYS A 46 REMARK 465 ALA A 47 REMARK 465 HIS A 48 REMARK 465 LEU A 49 REMARK 465 ASP A 50 REMARK 465 ALA A 51 REMARK 465 LEU A 52 REMARK 465 ASP A 53 REMARK 465 VAL A 54 REMARK 465 TRP A 55 REMARK 465 GLN A 56 REMARK 465 GLN A 57 REMARK 465 LEU A 58 REMARK 465 ALA A 59 REMARK 465 THR A 60 REMARK 465 ALA A 61 REMARK 465 VAL A 62 REMARK 465 LYS A 63 REMARK 465 LEU A 64 REMARK 465 TYR A 65 REMARK 465 PRO A 66 REMARK 465 ASP A 67 REMARK 465 GLN A 68 REMARK 465 VAL A 69 REMARK 465 GLU A 70 REMARK 465 GLN A 71 REMARK 465 ILE A 72 REMARK 465 SER A 73 REMARK 465 SER A 74 REMARK 465 GLN A 75 REMARK 465 LYS A 76 REMARK 465 GLN A 77 REMARK 465 GLY B 22 REMARK 465 SER B 23 REMARK 465 HIS B 24 REMARK 465 MET B 25 REMARK 465 SER B 26 REMARK 465 HIS B 27 REMARK 465 LEU B 28 REMARK 465 ASP B 29 REMARK 465 ASN B 30 REMARK 465 THR B 31 REMARK 465 MET B 32 REMARK 465 ALA B 33 REMARK 465 ILE B 34 REMARK 465 ARG B 35 REMARK 465 LEU B 36 REMARK 465 LEU B 37 REMARK 465 PRO B 38 REMARK 465 LEU B 39 REMARK 465 PRO B 40 REMARK 465 VAL B 41 REMARK 465 ARG B 42 REMARK 465 ALA B 43 REMARK 465 GLN B 44 REMARK 465 LEU B 45 REMARK 465 CYS B 46 REMARK 465 ALA B 47 REMARK 465 HIS B 48 REMARK 465 LEU B 49 REMARK 465 ASP B 50 REMARK 465 ALA B 51 REMARK 465 LEU B 52 REMARK 465 ASP B 53 REMARK 465 VAL B 54 REMARK 465 TRP B 55 REMARK 465 GLN B 56 REMARK 465 GLN B 57 REMARK 465 LEU B 58 REMARK 465 ALA B 59 REMARK 465 THR B 60 REMARK 465 ALA B 61 REMARK 465 VAL B 62 REMARK 465 LYS B 63 REMARK 465 LEU B 64 REMARK 465 TYR B 65 REMARK 465 PRO B 66 REMARK 465 ASP B 67 REMARK 465 GLN B 68 REMARK 465 VAL B 69 REMARK 465 GLU B 70 REMARK 465 GLN B 71 REMARK 465 ILE B 72 REMARK 465 SER B 73 REMARK 465 SER B 74 REMARK 465 GLN B 75 REMARK 465 LYS B 76 REMARK 465 GLN B 77 REMARK 465 ARG B 78 REMARK 465 GLY B 79 REMARK 465 ARG B 80 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 LEU A 116 CA - CB - CG ANGL. DEV. = 7.3 DEGREES REMARK 500 LEU B 116 CA - CB - CG ANGL. DEV. = 7.1 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1D2Z RELATED DB: PDB REMARK 900 1D2Z IS THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE REMARK 900 DEATH DOMAINS OF PELLE AND TUBE DBREF 1IK7 A 26 129 UNP Q05652 KPEL_DROME 26 129 DBREF 1IK7 B 26 129 UNP Q05652 KPEL_DROME 26 129 SEQADV 1IK7 GLY A 22 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 SER A 23 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 HIS A 24 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 MET A 25 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 GLY B 22 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 SER B 23 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 HIS B 24 UNP Q05652 CLONING ARTIFACT SEQADV 1IK7 MET B 25 UNP Q05652 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 108 GLY SER HIS MET SER HIS LEU ASP ASN THR MET ALA ILE SEQRES 2 B 108 ARG LEU LEU PRO LEU PRO VAL ARG ALA GLN LEU CYS ALA SEQRES 3 B 108 HIS LEU ASP ALA LEU ASP VAL TRP GLN GLN LEU ALA THR SEQRES 4 B 108 ALA VAL LYS LEU TYR PRO ASP GLN VAL GLU GLN ILE SER SEQRES 5 B 108 SER GLN LYS GLN ARG GLY ARG SER ALA SER ASN GLU PHE SEQRES 6 B 108 LEU ASN ILE TRP GLY GLY GLN TYR ASN HIS THR VAL GLN SEQRES 7 B 108 THR LEU PHE ALA LEU PHE LYS LYS LEU LYS LEU HIS ASN SEQRES 8 B 108 ALA MET ARG LEU ILE LYS ASP TYR VAL SER GLU ASP LEU SEQRES 9 B 108 HIS LYS TYR ILE HET TRS 201 8 HET TRS 202 8 HET TRS 203 8 HET TRS 204 8 HET MPD 101 8 HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL HETSYN TRS TRIS BUFFER FORMUL 3 TRS 4(C4 H12 N O3 1+) FORMUL 7 MPD C6 H14 O2 FORMUL 8 HOH *19(H2 O) HELIX 1 1 GLY A 79 HIS A 126 1 48 HELIX 2 2 LYS A 127 ILE A 129 5 3 HELIX 3 3 SER B 81 HIS B 126 1 46 HELIX 4 4 LYS B 127 ILE B 129 5 3 CRYST1 70.106 95.542 103.196 90.00 90.00 90.00 I 21 21 21 16 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 0.014264 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010467 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009690 0.00000