HEADER POTASSIUM CHANNEL 23-JUL-98 1BL8 TITLE POTASSIUM CHANNEL (KCSA) FROM STREPTOMYCES LIVIDANS COMPND MOL_ID: 1; COMPND 2 MOLECULE: POTASSIUM CHANNEL PROTEIN; COMPND 3 CHAIN: A, B, C, D; COMPND 4 FRAGMENT: RESIDUES 1 - 125; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: L90C; COMPND 7 BIOLOGICAL_UNIT: HOMOTETRAMER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE; SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PQE60; SOURCE 6 EXPRESSION_SYSTEM_GENE: KCSA KEYWDS POTASSIUM CHANNEL, INTEGRAL MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR D.A.DOYLE,J.M.CABRAL,R.A.PFUETZNER,A.KUO,J.M.GULBIS, AUTHOR 2 S.L.COHEN,B.T.CHAIT,R.MACKINNON REVDAT 1 29-JUL-98 1BL8 0 JRNL AUTH D.A.DOYLE,J.M.CABRAL,R.A.PFUETZNER,A.KUO, JRNL AUTH 2 J.M.GULBIS,S.L.COHEN,B.T.CHAIT,R.MACKINNON JRNL TITL THE STRUCTURE OF THE POTASSIUM CHANNEL: MOLECULAR JRNL TITL 2 BASIS OF K+ CONDUCTION AND SELECTIVITY JRNL REF SCIENCE V. 280 69 1998 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 0038 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.2 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.2 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3 REMARK 3 NUMBER OF REFLECTIONS : 12054 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NONE REMARK 3 FREE R VALUE TEST SET SELECTION : SHELL REMARK 3 R VALUE (WORKING SET) : 0.280 REMARK 3 FREE R VALUE : 0.290 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.4 REMARK 3 FREE R VALUE TEST SET COUNT : 1252 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL 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 : 2824 REMARK 3 NUCLEIC ACID ATOMS : NULL REMARK 3 HETEROGEN ATOMS : 3 REMARK 3 SOLVENT ATOMS : 1 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.1 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.73 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.53 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : GROUP REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : RESTRAINTS 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 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BL8 COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 5 REMARK 5 WARNING REMARK 5 1BL8: THIS IS LAYER 1 RELEASE. REMARK 5 REMARK 5 PLEASE NOTE THAT THIS ENTRY WAS RELEASED AFTER DEPOSITOR REMARK 5 CHECKING AND APPROVAL BUT WITHOUT PDB STAFF INTERVENTION. REMARK 5 AN AUXILIARY FILE, AUX1BL8.RPT, IS AVAILABLE FROM THE REMARK 5 PDB FTP SERVER AND IS ACCESSIBLE THROUGH THE 3DB BROWSER. REMARK 5 THE FILE CONTAINS THE OUTPUT OF THE PROGRAM WHAT_CHECK AND REMARK 5 OTHER DIAGNOSTICS. REMARK 5 REMARK 5 NOMENCLATURE IN THIS ENTRY, INCLUDING HET RESIDUE NAMES REMARK 5 AND HET ATOM NAMES, HAS NOT BEEN STANDARDIZED BY THE PDB REMARK 5 PROCESSING STAFF. A LAYER 2 ENTRY WILL BE RELEASED SHORTLY REMARK 5 AFTER THIS STANDARDIZATION IS COMPLETED AND APPROVED BY THE REMARK 5 DEPOSITOR. THE LAYER 2 ENTRY WILL BE TREATED AS A REMARK 5 CORRECTION TO THIS ONE, WITH THE APPROPRIATE REVDAT RECORD. REMARK 5 REMARK 5 FURTHER INFORMATION INCLUDING VALIDATION CRITERIA USED IN REMARK 5 CHECKING THIS ENTRY AND A LIST OF MANDATORY DATA FIELDS REMARK 5 ARE AVAILABLE FROM THE PDB WEB SITE AT REMARK 5 HTTP://WWW.PDB.BNL.GOV/. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 6 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.908 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12603 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.2 REMARK 200 RESOLUTION RANGE LOW (A) : 30.0 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 200 DATA REDUNDANCY : 6.1 REMARK 200 R MERGE (I) : 0.086 REMARK 200 R SYM (I) : NONE REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.2 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.3 REMARK 200 COMPLETENESS FOR SHELL (%) : 66.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.3 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: CCP4 PROGRAM SUITE, SHELX-97 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): N/A REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: REMARK 280 ONE-TO-MIXTURE OF PROTEIN SOLUTION AND RESERVOIR REMARK 280 (200 MM CACL2, 100 MM HEPES PH 7.5, 48% PEG 400). REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.39150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.46612 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.39150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.46612 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 295 REMARK 295 REMARK REMARK 295 TRANSFORMATION RELATES CHAIN B TO CHAIN A REMARK 295 TRANSFORMATION RELATES CHAIN C TO CHAIN A REMARK 295 TRANSFORMATION RELATES CHAIN D TO CHAIN A 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 MET A 1 REMARK 465 PRO A 2 REMARK 465 PRO A 3 REMARK 465 MET A 4 REMARK 465 LEU A 5 REMARK 465 SER A 6 REMARK 465 GLY A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 ALA A 10 REMARK 465 ARG A 11 REMARK 465 LEU A 12 REMARK 465 VAL A 13 REMARK 465 LYS A 14 REMARK 465 LEU A 15 REMARK 465 LEU A 16 REMARK 465 LEU A 17 REMARK 465 GLY A 18 REMARK 465 ARG A 19 REMARK 465 HIS A 20 REMARK 465 GLY A 21 REMARK 465 SER A 22 REMARK 465 GLU A 120 REMARK 465 ARG A 121 REMARK 465 ARG A 122 REMARK 465 GLY A 123 REMARK 465 HIS A 124 REMARK 465 PHE A 125 REMARK 465 MET B 1 REMARK 465 PRO B 2 REMARK 465 PRO B 3 REMARK 465 MET B 4 REMARK 465 LEU B 5 REMARK 465 SER B 6 REMARK 465 GLY B 7 REMARK 465 LEU B 8 REMARK 465 LEU B 9 REMARK 465 ALA B 10 REMARK 465 ARG B 11 REMARK 465 LEU B 12 REMARK 465 VAL B 13 REMARK 465 LYS B 14 REMARK 465 LEU B 15 REMARK 465 LEU B 16 REMARK 465 LEU B 17 REMARK 465 GLY B 18 REMARK 465 ARG B 19 REMARK 465 HIS B 20 REMARK 465 GLY B 21 REMARK 465 SER B 22 REMARK 465 GLU B 120 REMARK 465 ARG B 121 REMARK 465 ARG B 122 REMARK 465 GLY B 123 REMARK 465 HIS B 124 REMARK 465 PHE B 125 REMARK 465 MET C 1 REMARK 465 PRO C 2 REMARK 465 PRO C 3 REMARK 465 MET C 4 REMARK 465 LEU C 5 REMARK 465 SER C 6 REMARK 465 GLY C 7 REMARK 465 LEU C 8 REMARK 465 LEU C 9 REMARK 465 ALA C 10 REMARK 465 ARG C 11 REMARK 465 LEU C 12 REMARK 465 VAL C 13 REMARK 465 LYS C 14 REMARK 465 LEU C 15 REMARK 465 LEU C 16 REMARK 465 LEU C 17 REMARK 465 GLY C 18 REMARK 465 ARG C 19 REMARK 465 HIS C 20 REMARK 465 GLY C 21 REMARK 465 SER C 22 REMARK 465 GLU A 120 REMARK 465 ARG A 121 REMARK 465 ARG A 122 REMARK 465 GLY A 123 REMARK 465 HIS A 124 REMARK 465 PHE A 125 REMARK 465 MET D 1 REMARK 465 PRO D 2 REMARK 465 PRO D 3 REMARK 465 MET D 4 REMARK 465 LEU D 5 REMARK 465 SER D 6 REMARK 465 GLY D 7 REMARK 465 LEU D 8 REMARK 465 LEU D 9 REMARK 465 ALA D 10 REMARK 465 ARG D 11 REMARK 465 LEU D 12 REMARK 465 VAL D 13 REMARK 465 LYS D 14 REMARK 465 LEU D 15 REMARK 465 LEU D 16 REMARK 465 LEU D 17 REMARK 465 GLY D 18 REMARK 465 ARG D 19 REMARK 465 HIS D 20 REMARK 465 GLY D 21 REMARK 465 SER D 22 REMARK 465 GLU D 120 REMARK 465 ARG D 121 REMARK 465 ARG D 122 REMARK 465 GLY D 123 REMARK 465 HIS D 124 REMARK 465 PHE D 125 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 27 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 60 CD1 REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 71 CG CD OE1 OE2 REMARK 470 ARG A 117 CZ NH1 NH2 REMARK 470 ARG B 27 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 60 CD1 REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 71 CG CD OE1 OE2 REMARK 470 ARG B 117 CZ NH1 NH2 REMARK 470 ARG C 27 CG CD NE CZ NH1 NH2 REMARK 470 ILE C 60 CD1 REMARK 470 ARG C 64 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 71 CG CD OE1 OE2 REMARK 470 ARG C 117 CZ NH1 NH2 REMARK 470 ARG D 27 CG CD NE CZ NH1 NH2 REMARK 470 ILE D 60 CD1 REMARK 470 ARG D 64 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 71 CG CD OE1 OE2 REMARK 470 ARG D 117 CZ NH1 NH2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: SEL REMARK 800 SITE_DESCRIPTION: REMARK 800 FILTER TO SELECT FOR POTASSIUM IONS REMARK 800 OVER OTHER MONOVALENT CATIONS. REMARK 800 DBREF 1BL8 A 23 119 PDB 1BL8 1BL8 23 119 DBREF 1BL8 B 23 119 PDB 1BL8 1BL8 23 119 DBREF 1BL8 C 23 119 PDB 1BL8 1BL8 23 119 DBREF 1BL8 D 23 119 PDB 1BL8 1BL8 23 119 SEQADV 1BL8 CYS 90 PIR S60172 LEU 90 ENGINEERED MUTATION SEQADV 1BL8 ARG 27 PIR S60172 ARG 27 DISORDERED SEQADV 1BL8 ILE 60 PIR S60172 ILE 60 DISORDERED SEQADV 1BL8 ARG 64 PIR S60172 ARG 64 DISORDERED SEQADV 1BL8 GLU 71 PIR S60172 GLU 71 DISORDERED SEQADV 1BL8 ARG 117 PIR S60172 ARG 117 DISORDERED SEQRES 1 A 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU SEQRES 2 A 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL SEQRES 3 A 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR SEQRES 4 A 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR SEQRES 5 A 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP SEQRES 6 A 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE SEQRES 7 A 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP SEQRES 8 A 97 PHE VAL GLY ARG GLU GLN SEQRES 1 B 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU SEQRES 2 B 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL SEQRES 3 B 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR SEQRES 4 B 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR SEQRES 5 B 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP SEQRES 6 B 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE SEQRES 7 B 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP SEQRES 8 B 97 PHE VAL GLY ARG GLU GLN SEQRES 1 C 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU SEQRES 2 C 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL SEQRES 3 C 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR SEQRES 4 C 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR SEQRES 5 C 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP SEQRES 6 C 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE SEQRES 7 C 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP SEQRES 8 C 97 PHE VAL GLY ARG GLU GLN SEQRES 1 D 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU SEQRES 2 D 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL SEQRES 3 D 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR SEQRES 4 D 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR SEQRES 5 D 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP SEQRES 6 D 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE SEQRES 7 D 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP SEQRES 8 D 97 PHE VAL GLY ARG GLU GLN HET K E 1 0 HET K E 2 0 HET K E 3 0 HETNAM K K HETSYN K POTASSIUM ION FORMUL 9 K 3(K 1+) FORMUL 6 HOH *1(H2 O1) HELIX 1 1 ARG A 27 GLU A 51 1 25 HELIX 2 2 TYR A 62 THR A 74 1 13 HELIX 3 3 LEU A 86 THR A 112 1 27 HELIX 4 4 ARG B 27 GLU B 51 1 25 HELIX 5 5 TYR B 62 THR B 74 1 13 HELIX 6 6 LEU B 86 THR B 112 1 27 HELIX 7 7 ARG C 27 GLU C 51 1 25 HELIX 8 8 TYR C 62 THR C 74 1 13 HELIX 9 9 LEU C 86 THR C 112 1 27 HELIX 10 10 ARG D 27 GLU D 51 1 25 HELIX 11 11 TYR D 62 THR D 74 1 13 HELIX 12 12 LEU D 86 THR D 112 1 27 SITE 1 SEL 4 VAL 76 GLY 77 TYR 78 GLY 79 CRYST1 128.780 68.930 112.040 90.00 124.63 90.00 C 1 2 1 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 0.007765 0.000000 0.005363 0.00000 SCALE2 0.000000 0.014507 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010847 0.00000 MTRIX1 1 0.126600 0.928780 0.348340 31.41247 1 MTRIX2 1 -0.931190 -0.009730 0.364390 86.76519 1 MTRIX3 1 0.341830 -0.370510 0.863640 -12.10887 1 MTRIX1 2 -0.736910 -0.010340 0.675910 112.17546 1 MTRIX2 2 0.004580 -0.999940 -0.010300 53.01701 1 MTRIX3 2 0.675980 -0.004490 0.736910 -43.35083 1 MTRIX1 3 0.137220 -0.931030 0.338160 80.28391 1 MTRIX2 3 0.929330 0.002860 -0.369240 -33.25713 1 MTRIX3 3 0.342800 0.364930 0.865630 -31.77395 1