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HEADER IMMUNE SYSTEM 23-SEP-03 1UM5 TITLE CATALYTIC ANTIBODY 21H3 WITH ALCOHOL SUBSTRATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY 21H3 L CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY 21H3 H CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: MOUSE; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS CATALYTIC ANTIBODY LIGAND TRANSESTERIFICATION EXPDTA X-RAY DIFFRACTION AUTHOR A.E.BEUSCHER IV,J.REUTER,A.J.OLSON,F.E.ROMESBERG, AUTHOR 2 P.G.SCHULTZ,P.WIRSCHING,K.D.JANDA,R.A.LERNER,R.C.STEVENS REVDAT 1 05-OCT-04 1UM5 0 JRNL AUTH A.E.BEUSCHER IV,J.REUTER,A.J.OLSON,F.E.ROMESBERG, JRNL AUTH 2 P.G.SCHULTZ,P.WIRSCHING,K.D.JANDA,R.A.LERNER, JRNL AUTH 3 R.C.STEVENS JRNL TITL STRUCTURAL STUDIES OF AN EFFICIENT CATALYTIC JRNL TITL 2 ANTIBODY OPERATING BY PING-PONG AND INDUCED FIT JRNL TITL 3 MECHANISMS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 55779 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) : 0.205 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.400 REMARK 3 FREE R VALUE TEST SET COUNT : 1919 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6434 REMARK 3 BIN R VALUE (WORKING SET) : 0.2190 REMARK 3 BIN FREE R VALUE : 0.2710 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 216 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3275 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 9 REMARK 3 SOLVENT ATOMS : 398 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 15.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.75 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.39000 REMARK 3 B22 (A**2) : 2.71000 REMARK 3 B33 (A**2) : -3.10000 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) : 0.17 REMARK 3 ESD FROM SIGMAA (A) : 0.04 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) : 0.21 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.07 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.023 REMARK 3 BOND ANGLES (DEGREES) : 2.20 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) : 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED REMARK 3 KSOL : 0.34 REMARK 3 BSOL : 38.49 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_REP.PARAM REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : SSU.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : SSU.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UM5 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 PDBJ. REMARK 100 THE RCSB ID CODE IS RCSB005979. 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 : 4.25 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55779 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 47.280 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: EPMR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.48 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, LITHIUM SULFATE, PH 4.25, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K 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 23.56400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.25500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.35300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.25500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.56400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.35300 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: L, H 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 ALA L 218 REMARK 465 GLY L 219 REMARK 465 ALA L 220 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 LEU L 2 CG CD1 CD2 REMARK 470 CYS L 216 CB SG REMARK 470 VAL H 3 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 303 O HOH 304 4466 2.11 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 ILE L 108 CG1 ILE L 108 CD1 -0.137 REMARK 500 ILE H 52 CG1 ILE H 52 CD1 -0.219 REMARK 500 LEU H 114 CG LEU H 114 CD2 -0.162 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 L 35 CA - CB - CG ANGL. DEV. =-16.2 DEGREES REMARK 500 GLY L 217 N - CA - C ANGL. DEV. =-14.2 DEGREES REMARK 500 LYS H 68 CD - CE - NZ ANGL. DEV. = 13.7 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 CYS L 216 -128.48 90.28 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1UM4 RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH SH4 REMARK 900 RELATED ID: 1UM6 RELATED DB: PDB REMARK 900 THE SAME PROTEIN SEQRES 1 L 219 LEU ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 219 ALA SER LEU GLY GLU ARG VAL SER LEU THR CYS ARG ALA SEQRES 3 L 219 SER GLN GLU ILE SER GLY TYR LEU TYR TRP LEU GLN GLN SEQRES 4 L 219 LYS PRO ASP GLY THR ILE LYS ARG LEU ILE TYR ALA GLY SEQRES 5 L 219 SER THR LEU ASP SER GLY VAL PRO LYS ARG PHE SER GLY SEQRES 6 L 219 SER ARG SER GLY SER ASP TYR SER LEU THR ILE SER SER SEQRES 7 L 219 LEU GLU SER GLU ASP PHE ALA ASP TYR TYR CYS LEU GLN SEQRES 8 L 219 TYR ALA SER TYR PRO ARG THR PHE GLY GLY GLY THR LYS SEQRES 9 L 219 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 219 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 219 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 219 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 219 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 219 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 219 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 219 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 219 SER PHE ASN ARG GLY GLU CYS GLY ALA GLY ALA SEQRES 1 H 217 VAL GLN LEU GLN GLN SER GLY PRO VAL LEU VAL LYS PRO SEQRES 2 H 217 GLY GLY SER VAL LYS MET SER CYS LYS ALA SER GLU TYR SEQRES 3 H 217 THR LEU THR SER TYR LEU PHE GLN TRP VAL LYS GLN LYS SEQRES 4 H 217 SER GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE TYR PRO SEQRES 5 H 217 TYR ASN GLY GLY THR ARG TYR ASN GLU LYS PHE ARG GLY SEQRES 6 H 217 LYS ALA THR LEU THR SER ASP LYS SER SER ASN THR ALA SEQRES 7 H 217 TYR LEU GLU LEU SER SER LEU THR SER GLU ASP SER ALA SEQRES 8 H 217 VAL TYR TYR CYS ALA ARG SER SER MET SER ASP PRO GLY SEQRES 9 H 217 ALA ASN TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 10 H 217 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 H 217 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 H 217 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 H 217 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 H 217 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 H 217 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 H 217 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 H 217 THR LYS VAL ASP LYS LYS VAL GLU PRO HET SS1 1001 9 HETNAM SS1 1-PHENYLETHANOL HETSYN SS1 (1S)-1-PHENYL-ETHANOL FORMUL 3 SS1 C8 H10 O FORMUL 4 HOH *398(H2 O) HELIX 1 1 GLU L 81 PHE L 85 5 5 HELIX 2 2 SER L 123 LYS L 128 1 6 HELIX 3 3 LYS L 185 HIS L 191 1 7 HELIX 4 4 GLY L 214 CYS L 216 5 3 HELIX 5 5 GLU H 63 ARG H 66 5 4 HELIX 6 6 THR H 88 SER H 92 5 5 HELIX 7 7 SER H 133 THR H 137 5 5 HELIX 8 8 SER H 162 ALA H 164 5 3 HELIX 9 9 SER H 193 LEU H 195 5 3 HELIX 10 10 LYS H 207 ASN H 210 5 4 SHEET 1 A 4 MET L 6 SER L 9 0 SHEET 2 A 4 VAL L 21 ALA L 27 -1 O THR L 24 N SER L 9 SHEET 3 A 4 ASP L 72 ILE L 77 -1 O LEU L 75 N LEU L 23 SHEET 4 A 4 PHE L 64 SER L 69 -1 N SER L 69 O ASP L 72 SHEET 1 B 6 SER L 12 SER L 16 0 SHEET 2 B 6 THR L 104 LYS L 109 1 O GLU L 107 N LEU L 13 SHEET 3 B 6 ALA L 86 GLN L 92 -1 N ALA L 86 O VAL L 106 SHEET 4 B 6 LEU L 35 GLN L 40 -1 N GLN L 40 O ASP L 87 SHEET 5 B 6 ILE L 46 TYR L 51 -1 O LEU L 49 N TRP L 37 SHEET 6 B 6 THR L 55 LEU L 56 -1 O THR L 55 N TYR L 51 SHEET 1 C 4 SER L 12 SER L 16 0 SHEET 2 C 4 THR L 104 LYS L 109 1 O GLU L 107 N LEU L 13 SHEET 3 C 4 ALA L 86 GLN L 92 -1 N ALA L 86 O VAL L 106 SHEET 4 C 4 THR L 99 PHE L 100 -1 O THR L 99 N GLN L 92 SHEET 1 D 4 SER L 116 PHE L 120 0 SHEET 2 D 4 THR L 131 PHE L 141 -1 O ASN L 139 N SER L 116 SHEET 3 D 4 TYR L 175 SER L 184 -1 O LEU L 177 N LEU L 138 SHEET 4 D 4 SER L 161 VAL L 165 -1 N GLN L 162 O THR L 180 SHEET 1 E 4 ALA L 155 LEU L 156 0 SHEET 2 E 4 LYS L 147 VAL L 152 -1 N VAL L 152 O ALA L 155 SHEET 3 E 4 VAL L 193 THR L 199 -1 O GLU L 197 N GLN L 149 SHEET 4 E 4 VAL L 207 ASN L 212 -1 O VAL L 207 N VAL L 198 SHEET 1 F 4 LEU H 5 GLN H 7 0 SHEET 2 F 4 VAL H 19 ALA H 25 -1 O LYS H 24 N GLN H 6 SHEET 3 F 4 THR H 79 LEU H 84 -1 O ALA H 80 N CYS H 23 SHEET 4 F 4 ALA H 69 ASP H 74 -1 N THR H 70 O GLU H 83 SHEET 1 G 6 VAL H 11 VAL H 13 0 SHEET 2 G 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 11 SHEET 3 G 6 ALA H 93 SER H 101 -1 N ALA H 93 O VAL H 115 SHEET 4 G 6 LEU H 34 GLN H 40 -1 N VAL H 38 O TYR H 96 SHEET 5 G 6 LEU H 46 ILE H 52 -1 O ILE H 49 N TRP H 37 SHEET 6 G 6 THR H 59 TYR H 61 -1 O ARG H 60 N TYR H 51 SHEET 1 H 4 VAL H 11 VAL H 13 0 SHEET 2 H 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 11 SHEET 3 H 4 ALA H 93 SER H 101 -1 N ALA H 93 O VAL H 115 SHEET 4 H 4 ASP H 104 TRP H 109 -1 O ASP H 104 N SER H 101 SHEET 1 I 4 SER H 126 LEU H 130 0 SHEET 2 I 4 THR H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 I 4 TYR H 182 PRO H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 I 4 VAL H 169 THR H 171 -1 N HIS H 170 O VAL H 187 SHEET 1 J 4 SER H 126 LEU H 130 0 SHEET 2 J 4 THR H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 J 4 TYR H 182 PRO H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 J 4 VAL H 175 LEU H 176 -1 N VAL H 175 O SER H 183 SHEET 1 K 3 THR H 157 TRP H 160 0 SHEET 2 K 3 ILE H 201 HIS H 206 -1 O ASN H 203 N SER H 159 SHEET 3 K 3 THR H 211 LYS H 216 -1 O VAL H 213 N VAL H 204 SSBOND 1 CYS L 25 CYS L 90 SSBOND 2 CYS L 136 CYS L 196 SSBOND 3 CYS H 23 CYS H 97 SSBOND 4 CYS H 146 CYS H 202 CISPEP 1 SER L 9 PRO L 10 0 -0.40 CISPEP 2 TYR L 96 PRO L 97 0 1.25 CISPEP 3 TYR L 142 PRO L 143 0 -1.53 CISPEP 4 PHE H 152 PRO H 153 0 -2.16 CISPEP 5 GLU H 154 PRO H 155 0 0.35 CRYST1 47.128 64.706 138.510 90.00 90.00 90.00 P 21 21 21 4 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 0.021219 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015455 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007220 0.00000