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HEADER IMMUNE SYSTEM 12-MAR-01 1I7Z TITLE ANTIBODY GNC92H2 BOUND TO LIGAND COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA OF IG KAPPA CHAIN: HUMAN CONSTANT REGION COMPND 3 AND MOUSE VARIABLE REGION; COMPND 4 CHAIN: A, C; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: THE CHIMERA CONSISTS OF RESIDUES 1-108 OF COMPND 7 MOUSE PORTION AND 109-214 OF HUMAN PORTION OF IG KAPPA COMPND 8 CHAIN.; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: CHIMERA OF IG GAMMA-1 CHAIN: HUMAN CONSTANT COMPND 11 REGION AND MOUSE VARIABLE REGION; COMPND 12 CHAIN: B, D; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: THE CHIMERA CONSISTS OF RESIDUES 1-113 OF COMPND 15 MOUSE PORTION AND 114-228 OF HUMAN PORTION OF IG GAMMA-1 COMPND 16 CHAIN. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS AND HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: MOUSE AND HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS AND HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: MOUSE AND HUMAN; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET KEYWDS IGG FOLD, ANTIBODY, CHIMERA EXPDTA X-RAY DIFFRACTION AUTHOR N.A.LARSEN,I.A.WILSON REVDAT 1 08-AUG-01 1I7Z 0 JRNL AUTH N.A.LARSEN,B.ZHOU,A.HEINE,P.WIRSCHING,K.D.JANDA, JRNL AUTH 2 I.A.WILSON JRNL TITL CRYSTAL STRUCTURE OF A COCAINE-BINDING ANTIBODY. JRNL REF J.MOL.BIOL. V. 311 9 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 43057 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) : 0.220 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2153 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 : 6690 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 44 REMARK 3 SOLVENT ATOMS : 233 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.00 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) : NULL 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) : 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 : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL 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: NULL REMARK 4 REMARK 4 1I7Z 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 RCSB013018. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAY-2000 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 : 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) : 1.039 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 : 43057 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 113.100 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.08200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.9000 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) : 2.34 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.51200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1NSN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 71.01000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.03500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.01000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.03500 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 OE1 GLU A 79 O HOH 143 2.18 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 B 34 CG MET B 34 SD -0.049 REMARK 500 MET B 48 SD MET B 48 CE 0.044 REMARK 500 PRO B 151 CG PRO B 151 CD 0.038 REMARK 500 PRO D 149 CG PRO D 149 CD 0.040 REMARK 500 PRO D 151 CG PRO D 151 CD 0.045 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 A 99 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 SER A 114 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 ARG B 66 N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 SER B 120 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 LEU B 124 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLU B 150 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 LEU B 187 CA - CB - CG ANGL. DEV. = 9.5 DEGREES REMARK 500 ALA C 51 N - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 SER C 52 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 GLY C 66 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 CYS C 88 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 PRO C 95A C - N - CA ANGL. DEV. = 12.1 DEGREES REMARK 500 PRO C 95A C - N - CD ANGL. DEV. = -9.4 DEGREES REMARK 500 SER C 114 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 LEU C 136 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 TYR D 32 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 ALA D 72 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 500 LEU D 124 N - CA - C ANGL. DEV. =-14.1 DEGREES REMARK 500 ASP D 146 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 THR D 200 N - CA - C ANGL. DEV. = 9.1 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 ALA A 51 -34.62 62.06 REMARK 500 ALA C 51 -34.82 62.47 DBREF 1I7Z A 109 214 UNP P01834 KAC_HUMAN 1 106 DBREF 1I7Z B 114 228 UNP P01857 IGHG1_HUMAN 1 103 DBREF 1I7Z C 109 214 UNP P01834 KAC_HUMAN 1 106 DBREF 1I7Z D 114 228 UNP P01857 IGHG1_HUMAN 1 103 SEQRES 1 A 219 ASP LEU VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 A 219 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 A 219 LYS SER VAL SER THR SER GLY TYR ASN TYR MET HIS TRP SEQRES 4 A 219 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 A 219 TYR LEU ALA SER ASN LEU ALA SER GLY VAL PRO ALA ARG SEQRES 6 A 219 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 A 219 ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR SEQRES 8 A 219 CYS LEU TYR SER ARG GLU PHE PRO PRO TRP THR PHE GLY SEQRES 9 A 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 A 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 A 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 A 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 A 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 A 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 A 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 A 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 A 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 220 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 B 220 PRO GLY GLU THR VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 B 220 TYR SER PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN SEQRES 4 B 220 ALA PRO GLY LYS GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 B 220 THR TYR THR GLY GLU PRO THR TYR ALA ASP ASP PHE ARG SEQRES 6 B 220 GLY ARG PHE ALA PHE SER LEU ALA THR SER ALA SER THR SEQRES 7 B 220 ALA TYR LEU GLN ILE ILE ASN LEU LYS ASN GLU ASP THR SEQRES 8 B 220 ALA THR TYR PHE CYS GLU THR TYR ASP SER PRO LEU GLY SEQRES 9 B 220 ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 10 B 220 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 B 220 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 B 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 B 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 B 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 B 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 B 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 B 220 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 C 219 ASP LEU VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 C 219 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 C 219 LYS SER VAL SER THR SER GLY TYR ASN TYR MET HIS TRP SEQRES 4 C 219 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 C 219 TYR LEU ALA SER ASN LEU ALA SER GLY VAL PRO ALA ARG SEQRES 6 C 219 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 C 219 ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR SEQRES 8 C 219 CYS LEU TYR SER ARG GLU PHE PRO PRO TRP THR PHE GLY SEQRES 9 C 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 C 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 C 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 C 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 C 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 C 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 C 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 C 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 C 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 220 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 D 220 PRO GLY GLU THR VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 220 TYR SER PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN SEQRES 4 D 220 ALA PRO GLY LYS GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 D 220 THR TYR THR GLY GLU PRO THR TYR ALA ASP ASP PHE ARG SEQRES 6 D 220 GLY ARG PHE ALA PHE SER LEU ALA THR SER ALA SER THR SEQRES 7 D 220 ALA TYR LEU GLN ILE ILE ASN LEU LYS ASN GLU ASP THR SEQRES 8 D 220 ALA THR TYR PHE CYS GLU THR TYR ASP SER PRO LEU GLY SEQRES 9 D 220 ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 10 D 220 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 D 220 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 D 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 D 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 D 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 D 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 D 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 D 220 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS HET COC 301 22 HET COC 302 22 HETNAM COC COCAINE FORMUL 5 COC 2(C17 H21 N O4) FORMUL 7 HOH *233(H2 O) HELIX 1 1 GLU A 79 ALA A 83 5 5 HELIX 2 2 SER A 121 LYS A 126 1 6 HELIX 3 3 LYS A 183 HIS A 189 1 7 HELIX 4 4 ASP B 61 ARG B 64 5 4 HELIX 5 5 THR B 73 ALA B 75 5 3 HELIX 6 6 LYS B 83 THR B 87 5 5 HELIX 7 7 SER B 127 LYS B 129 5 3 HELIX 8 8 SER B 163 ALA B 165 5 3 HELIX 9 9 LYS B 213 ASN B 216 5 4 HELIX 10 10 GLU C 79 ALA C 83 5 5 HELIX 11 11 SER C 121 LYS C 126 1 6 HELIX 12 12 LYS C 183 LYS C 188 1 6 HELIX 13 13 ASP D 61 ARG D 64 5 4 HELIX 14 14 LYS D 83 THR D 87 5 5 HELIX 15 15 SER D 163 ALA D 165 5 3 HELIX 16 16 SER D 196 LEU D 198 5 3 HELIX 17 17 LYS D 213 ASN D 216 5 4 SHEET 1 A1 4 LEU A 4 SER A 7 0 SHEET 2 A1 4 ALA A 19 ALA A 25 -1 N SER A 22 O SER A 7 SHEET 3 A1 4 ASP A 70 ILE A 75 -1 N PHE A 71 O CYS A 23 SHEET 4 A1 4 PHE A 62 SER A 67 -1 O SER A 63 N ASN A 74 SHEET 1 A2 4 SER A 114 PHE A 118 0 SHEET 2 A2 4 THR A 129 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 A2 4 TYR A 173 SER A 182 -1 O TYR A 173 N PHE A 139 SHEET 4 A2 4 SER A 159 VAL A 163 -1 O GLN A 160 N THR A 178 SHEET 1 A3 8 ASN A 53 LEU A 54 0 SHEET 2 A3 8 LYS A 45 TYR A 49 -1 N TYR A 49 O ASN A 53 SHEET 3 A3 8 MET A 33 GLN A 38 -1 O TRP A 35 N LEU A 47 SHEET 4 A3 8 ALA A 84 TYR A 90 -1 N THR A 85 O GLN A 38 SHEET 5 A3 8 THR A 97 PHE A 98 -1 O THR A 97 N TYR A 90 SHEET 6 A3 8 ALA A 84 TYR A 90 -1 N TYR A 90 O THR A 97 SHEET 7 A3 8 THR A 102 LYS A 107 -1 O THR A 102 N TYR A 86 SHEET 8 A3 8 SER A 10 SER A 14 1 O LEU A 11 N GLU A 105 SHEET 1 A4 4 ALA A 153 LEU A 154 0 SHEET 2 A4 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 A4 4 VAL A 191 THR A 197 -1 O ALA A 193 N LYS A 149 SHEET 4 A4 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 A5 4 GLN B 5 GLN B 6 0 SHEET 2 A5 4 VAL B 18 LYS B 23 -1 N LYS B 23 O GLN B 5 SHEET 3 A5 4 THR B 77 ILE B 82 -1 N ALA B 78 O CYS B 22 SHEET 4 A5 4 PHE B 67 ALA B 72 -1 N ALA B 68 O GLN B 81 SHEET 1 A6 8 GLU B 10 LYS B 12 0 SHEET 2 A6 8 THR B 107 VAL B 111 1 O THR B 108 N GLU B 10 SHEET 3 A6 8 ALA B 88 SER B 97 -1 O ALA B 88 N VAL B 109 SHEET 4 A6 8 GLY B 100 TRP B 103 -1 O GLY B 100 N ASP B 96 SHEET 5 A6 8 ALA B 88 SER B 97 -1 O THR B 94 N TYR B 102 SHEET 6 A6 8 MET B 34 GLN B 39 -1 N ASN B 35 O GLU B 93 SHEET 7 A6 8 LYS B 46 ILE B 51 -1 O LYS B 46 N LYS B 38 SHEET 8 A6 8 PRO B 57 TYR B 59 -1 N THR B 58 O TRP B 50 SHEET 1 A7 8 SER B 120 LEU B 124 0 SHEET 2 A7 8 THR B 137 TYR B 147 -1 O GLY B 141 N LEU B 124 SHEET 3 A7 8 THR B 133 SER B 134 -1 N SER B 134 O THR B 137 SHEET 4 A7 8 THR B 137 TYR B 147 -1 O THR B 137 N SER B 134 SHEET 5 A7 8 TYR B 185 PRO B 194 -1 N TYR B 185 O TYR B 147 SHEET 6 A7 8 VAL B 171 THR B 173 -1 N HIS B 172 O VAL B 190 SHEET 7 A7 8 TYR B 185 PRO B 194 -1 O VAL B 190 N HIS B 172 SHEET 8 A7 8 VAL B 177 LEU B 178 -1 N VAL B 177 O SER B 186 SHEET 1 A8 3 THR B 153 TRP B 157 0 SHEET 2 A8 3 ILE B 207 HIS B 212 -1 N ASN B 209 O SER B 156 SHEET 3 A8 3 THR B 217 LYS B 222 -1 O THR B 217 N HIS B 212 SHEET 1 A9 4 LEU C 4 SER C 7 0 SHEET 2 A9 4 ALA C 19 ALA C 25 -1 N SER C 22 O SER C 7 SHEET 3 A9 4 ASP C 70 ILE C 75 -1 N PHE C 71 O CYS C 23 SHEET 4 A9 4 PHE C 62 SER C 67 -1 O SER C 63 N ASN C 74 SHEET 1 A10 8 ASN C 53 LEU C 54 0 SHEET 2 A10 8 LYS C 45 TYR C 49 -1 N TYR C 49 O ASN C 53 SHEET 3 A10 8 MET C 33 GLN C 38 -1 O TRP C 35 N LEU C 47 SHEET 4 A10 8 ALA C 84 TYR C 90 -1 O THR C 85 N GLN C 38 SHEET 5 A10 8 THR C 97 PHE C 98 -1 O THR C 97 N TYR C 90 SHEET 6 A10 8 ALA C 84 TYR C 90 -1 N TYR C 90 O THR C 97 SHEET 7 A10 8 THR C 102 LYS C 107 -1 O THR C 102 N TYR C 86 SHEET 8 A10 8 SER C 10 SER C 14 1 N LEU C 11 O LYS C 103 SHEET 1 A11 4 SER C 114 PHE C 118 0 SHEET 2 A11 4 THR C 129 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 A11 4 TYR C 173 SER C 182 -1 O TYR C 173 N PHE C 139 SHEET 4 A11 4 SER C 159 VAL C 163 -1 O GLN C 160 N THR C 178 SHEET 1 A12 4 ALA C 153 GLN C 155 0 SHEET 2 A12 4 LYS C 145 VAL C 150 -1 O TRP C 148 N GLN C 155 SHEET 3 A12 4 VAL C 191 THR C 197 -1 N ALA C 193 O LYS C 149 SHEET 4 A12 4 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196 SHEET 1 A13 4 GLN D 5 GLN D 6 0 SHEET 2 A13 4 VAL D 18 LYS D 23 -1 N LYS D 23 O GLN D 5 SHEET 3 A13 4 THR D 77 ILE D 82 -1 N ALA D 78 O CYS D 22 SHEET 4 A13 4 PHE D 67 ALA D 72 -1 O ALA D 68 N GLN D 81 SHEET 1 A14 8 GLU D 10 LYS D 12 0 SHEET 2 A14 8 THR D 107 VAL D 111 1 O THR D 108 N GLU D 10 SHEET 3 A14 8 ALA D 88 SER D 97 -1 O ALA D 88 N VAL D 109 SHEET 4 A14 8 GLY D 100 TRP D 103 -1 O GLY D 100 N ASP D 96 SHEET 5 A14 8 ALA D 88 SER D 97 -1 O THR D 94 N TYR D 102 SHEET 6 A14 8 MET D 34 GLN D 39 -1 N ASN D 35 O GLU D 93 SHEET 7 A14 8 LYS D 46 ILE D 51 -1 O LYS D 46 N LYS D 38 SHEET 8 A14 8 PRO D 57 TYR D 59 -1 N THR D 58 O TRP D 50 SHEET 1 A15 8 SER D 120 LEU D 124 0 SHEET 2 A15 8 THR D 137 TYR D 147 -1 O GLY D 141 N LEU D 124 SHEET 3 A15 8 THR D 133 SER D 134 -1 N SER D 134 O THR D 137 SHEET 4 A15 8 THR D 137 TYR D 147 -1 O THR D 137 N SER D 134 SHEET 5 A15 8 TYR D 185 PRO D 194 -1 N TYR D 185 O TYR D 147 SHEET 6 A15 8 VAL D 171 THR D 173 -1 N HIS D 172 O VAL D 190 SHEET 7 A15 8 TYR D 185 PRO D 194 -1 O VAL D 190 N HIS D 172 SHEET 8 A15 8 VAL D 177 LEU D 178 -1 N VAL D 177 O SER D 186 SHEET 1 A16 3 THR D 153 TRP D 157 0 SHEET 2 A16 3 ILE D 207 HIS D 212 -1 N ASN D 209 O SER D 156 SHEET 3 A16 3 THR D 217 LYS D 222 -1 O THR D 217 N HIS D 212 SSBOND 1 CYS A 23 CYS A 88 SSBOND 2 CYS A 134 CYS A 194 SSBOND 3 CYS A 214 CYS B 228 SSBOND 4 CYS B 22 CYS B 92 SSBOND 5 CYS B 142 CYS B 208 SSBOND 6 CYS C 23 CYS C 88 SSBOND 7 CYS C 134 CYS C 194 SSBOND 8 CYS D 22 CYS D 92 SSBOND 9 CYS D 142 CYS D 208 CISPEP 1 SER A 7 PRO A 8 0 -0.28 CISPEP 2 HIS A 76 PRO A 77 0 0.15 CISPEP 3 PRO A 95 PRO A 95A 0 0.18 CISPEP 4 TYR A 140 PRO A 141 0 -0.23 CISPEP 5 PHE B 148 PRO B 149 0 -0.55 CISPEP 6 GLU B 150 PRO B 151 0 0.30 CISPEP 7 SER C 7 PRO C 8 0 -0.61 CISPEP 8 HIS C 76 PRO C 77 0 -0.27 CISPEP 9 PRO C 95 PRO C 95A 0 0.36 CISPEP 10 TYR C 140 PRO C 141 0 0.07 CISPEP 11 PHE D 148 PRO D 149 0 -0.13 CISPEP 12 GLU D 150 PRO D 151 0 -0.06 CRYST1 142.020 64.070 129.370 90.00 123.06 90.00 C 1 2 1 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 0.007041 0.000000 0.004583 0.00000 SCALE2 0.000000 0.015608 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009223 0.00000