HEADER APOPTOSIS 09-MAR-09 3GJS
TITLE CASPASE-3 BINDS DIVERSE P4 RESIDUES IN PEPTIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3 SUBUNIT P17;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, CPP-32, YAMA
COMPND 5 PROTEIN, SREBP CLEAVAGE ACTIVITY 1, SCA-1, CASPASE-3 SUBUNIT P17,
COMPND 6 CASPASE-3 SUBUNIT P12;
COMPND 7 EC: 3.4.22.56;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CASPASE-3 SUBUNIT P12;
COMPND 11 CHAIN: B, D;
COMPND 12 SYNONYM: CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, CPP-32, YAMA
COMPND 13 PROTEIN, SREBP CLEAVAGE ACTIVITY 1, SCA-1, CASPASE-3 SUBUNIT P17,
COMPND 14 CASPASE-3 SUBUNIT P12;
COMPND 15 EC: 3.4.22.56;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: AC-YVAD-CHO INHIBITOR;
COMPND 19 CHAIN: E, F;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CASP3, CPP32;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CASP3, CPP32;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES
KEYWDS ENZYME CATALYSIS, CYSTEINE PROTEASE, PROTEIN RECOGNITION, APOPTOSIS,
KEYWDS 2 HYDROLASE, PHOSPHOPROTEIN, PROTEASE, S-NITROSYLATION, THIOL
KEYWDS 3 PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.FANG,G.FU,J.AGNISWAMY,R.W.HARRISON,I.T.WEBER
REVDAT 4 17-AUG-11 3GJS 1 SEQRES COMPND LINK SITE
REVDAT 4 2 1 REMARK
REVDAT 3 13-JUL-11 3GJS 1 VERSN
REVDAT 2 26-MAY-09 3GJS 1 JRNL
REVDAT 1 24-MAR-09 3GJS 0
JRNL AUTH B.FANG,G.FU,J.AGNISWAMY,R.W.HARRISON,I.T.WEBER
JRNL TITL CASPASE-3 BINDS DIVERSE P4 RESIDUES IN PEPTIDES AS REVEALED
JRNL TITL 2 BY CRYSTALLOGRAPHY AND STRUCTURAL MODELING.
JRNL REF APOPTOSIS V. 14 741 2009
JRNL REFN ISSN 1360-8185
JRNL PMID 19283487
JRNL DOI 10.1007/S10495-009-0333-Y
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 42106
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) : 0.216
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3862
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 3GJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB051948.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42106
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> 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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, 5% GLYCEROL, 10
REMARK 280 MM DITHIOTHREITOL, 14-18% PEG6000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.15000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
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 SER A 29
REMARK 465 GLY A 30
REMARK 465 ILE A 31
REMARK 465 SER A 32
REMARK 465 LEU A 33
REMARK 465 ASP A 175
REMARK 465 SER B 176
REMARK 465 GLY B 177
REMARK 465 VAL B 178
REMARK 465 ASP B 179
REMARK 465 ASP B 180
REMARK 465 ASP B 181
REMARK 465 MET B 182
REMARK 465 ALA B 183
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 HIS B 282
REMARK 465 HIS B 283
REMARK 465 SER C 29
REMARK 465 GLY C 30
REMARK 465 ILE C 31
REMARK 465 SER C 32
REMARK 465 LEU C 33
REMARK 465 ASP C 34
REMARK 465 ASP C 175
REMARK 465 SER D 176
REMARK 465 GLY D 177
REMARK 465 VAL D 178
REMARK 465 ASP D 179
REMARK 465 ASP D 180
REMARK 465 ASP D 181
REMARK 465 MET D 182
REMARK 465 ALA D 183
REMARK 465 CYS D 184
REMARK 465 HIS D 185
REMARK 465 HIS D 278
REMARK 465 HIS D 279
REMARK 465 HIS D 280
REMARK 465 HIS D 281
REMARK 465 HIS D 282
REMARK 465 HIS D 283
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 A 1261 O HOH B 1141 2646 1.59
REMARK 500 O HOH A 1261 O HOH B 1262 2646 1.95
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 90 77.51 39.94
REMARK 500 SER A 120 -174.83 -173.29
REMARK 500 HIS B 185 92.72 -63.93
REMARK 500 LYS B 229 -62.29 -139.75
REMARK 500 LYS C 82 32.68 75.85
REMARK 500 ASP C 90 78.01 41.56
REMARK 500 SER C 113 -168.06 -160.23
REMARK 500 SER C 120 -174.30 -172.87
REMARK 500 ASP D 192 31.78 70.63
REMARK 500 LYS D 229 -60.49 -136.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GJQ RELATED DB: PDB
REMARK 900 RELATED ID: 3GJR RELATED DB: PDB
REMARK 900 RELATED ID: 3GJT RELATED DB: PDB
DBREF 3GJS A 29 175 UNP P42574 CASP3_HUMAN 29 175
DBREF 3GJS B 176 277 UNP P42574 CASP3_HUMAN 176 277
DBREF 3GJS C 29 175 UNP P42574 CASP3_HUMAN 29 175
DBREF 3GJS D 176 277 UNP P42574 CASP3_HUMAN 176 277
DBREF 3GJS E 1 5 PDB 3GJS 3GJS 1 5
DBREF 3GJS F 6 10 PDB 3GJS 3GJS 6 10
SEQADV 3GJS HIS B 278 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS B 279 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS B 280 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS B 281 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS B 282 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS B 283 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS D 278 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS D 279 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS D 280 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS D 281 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS D 282 UNP P42574 EXPRESSION TAG
SEQADV 3GJS HIS D 283 UNP P42574 EXPRESSION TAG
SEQRES 1 A 147 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 A 147 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 A 147 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 A 147 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 A 147 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 A 147 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 A 147 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 A 147 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 A 147 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 A 147 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 A 147 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP CYS GLY
SEQRES 12 A 147 ILE GLU THR ASP
SEQRES 1 B 108 SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE PRO
SEQRES 2 B 108 VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA PRO
SEQRES 3 B 108 GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER TRP
SEQRES 4 B 108 PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR ALA
SEQRES 5 B 108 ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL ASN
SEQRES 6 B 108 ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE ASP
SEQRES 7 B 108 ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE VAL
SEQRES 8 B 108 SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS HIS HIS
SEQRES 9 B 108 HIS HIS HIS HIS
SEQRES 1 C 147 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 C 147 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 C 147 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 C 147 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 C 147 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 C 147 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 C 147 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 C 147 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 C 147 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 C 147 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 C 147 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP CYS GLY
SEQRES 12 C 147 ILE GLU THR ASP
SEQRES 1 D 108 SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE PRO
SEQRES 2 D 108 VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA PRO
SEQRES 3 D 108 GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER TRP
SEQRES 4 D 108 PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR ALA
SEQRES 5 D 108 ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL ASN
SEQRES 6 D 108 ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE ASP
SEQRES 7 D 108 ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE VAL
SEQRES 8 D 108 SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS HIS HIS
SEQRES 9 D 108 HIS HIS HIS HIS
SEQRES 1 E 5 ACE TYR VAL ALA ASJ
SEQRES 1 F 5 ACE TYR VAL ALA ASJ
HET ACE E 1 3
HET ASJ E 5 8
HET ACE F 6 3
HET ASJ F 10 8
HETNAM ACE ACETYL GROUP
HETNAM ASJ (3S)-3-AMINO-4-HYDROXYBUTANOIC ACID
FORMUL 5 ACE 2(C2 H4 O)
FORMUL 5 ASJ 2(C4 H9 N O3)
FORMUL 7 HOH *270(H2 O)
HELIX 1 1 HIS A 56 GLY A 60 5 5
HELIX 2 2 GLY A 66 LEU A 81 1 16
HELIX 3 3 THR A 92 LYS A 105 1 14
HELIX 4 4 LEU A 136 ASN A 141 1 6
HELIX 5 5 PHE A 142 ARG A 144 5 3
HELIX 6 6 CYS A 148 THR A 152 5 5
HELIX 7 7 TRP B 214 ALA B 227 1 14
HELIX 8 8 GLU B 231 PHE B 247 1 17
HELIX 9 9 ASP B 253 HIS B 257 5 5
HELIX 10 10 GLY C 66 LEU C 81 1 16
HELIX 11 11 THR C 92 LYS C 105 1 14
HELIX 12 12 LEU C 136 ASN C 141 1 6
HELIX 13 13 PHE C 142 ARG C 144 5 3
HELIX 14 14 CYS C 148 THR C 152 5 5
HELIX 15 15 TRP D 214 ALA D 227 1 14
HELIX 16 16 GLU D 231 PHE D 247 1 17
HELIX 17 17 ASP D 253 HIS D 257 5 5
SHEET 1 A12 GLU A 84 ASN A 89 0
SHEET 2 A12 GLU A 43 ASN A 51 1 N ASN A 51 O LYS A 88
SHEET 3 A12 ARG A 111 LEU A 119 1 O VAL A 117 N ILE A 48
SHEET 4 A12 LYS A 156 GLN A 161 1 O LEU A 157 N PHE A 114
SHEET 5 A12 PHE B 193 TYR B 197 1 O LEU B 194 N PHE A 158
SHEET 6 A12 CYS B 264 SER B 267 -1 O VAL B 266 N TYR B 195
SHEET 7 A12 CYS D 264 SER D 267 -1 O SER D 267 N ILE B 265
SHEET 8 A12 PHE D 193 TYR D 197 -1 N TYR D 195 O VAL D 266
SHEET 9 A12 LYS C 156 GLN C 161 1 N PHE C 158 O LEU D 194
SHEET 10 A12 ARG C 111 LEU C 119 1 N PHE C 114 O LEU C 157
SHEET 11 A12 GLU C 43 ASN C 51 1 N ILE C 48 O VAL C 117
SHEET 12 A12 GLU C 84 ASN C 89 1 O LYS C 88 N ASN C 51
SHEET 1 B 3 GLY A 122 GLU A 123 0
SHEET 2 B 3 ILE A 126 GLY A 129 -1 O ILE A 126 N GLU A 123
SHEET 3 B 3 GLY A 132 ASP A 135 -1 O GLY A 132 N GLY A 129
SHEET 1 C 2 LYS B 186 ILE B 187 0
SHEET 2 C 2 ILE C 172 GLU C 173 -1 O ILE C 172 N ILE B 187
SHEET 1 D 3 GLY B 212 SER B 213 0
SHEET 2 D 3 TRP B 206 ASN B 208 -1 N ASN B 208 O GLY B 212
SHEET 3 D 3 VAL E 3 ALA E 4 -1 O VAL E 3 N ARG B 207
SHEET 1 E 3 GLY C 122 GLU C 123 0
SHEET 2 E 3 ILE C 126 GLY C 129 -1 O ILE C 126 N GLU C 123
SHEET 3 E 3 GLY C 132 ASP C 135 -1 O GLY C 132 N GLY C 129
SHEET 1 F 3 GLY D 212 SER D 213 0
SHEET 2 F 3 TRP D 206 ASN D 208 -1 N ASN D 208 O GLY D 212
SHEET 3 F 3 VAL F 8 ALA F 9 -1 O VAL F 8 N ARG D 207
LINK C ACE E 1 N TYR E 2 1555 1555 1.33
LINK C ALA E 4 N ASJ E 5 1555 1555 1.33
LINK C ACE F 6 N TYR F 7 1555 1555 1.33
LINK C ALA F 9 N ASJ F 10 1555 1555 1.33
LINK SG CYS A 163 C ASJ E 5 1555 1555 1.78
LINK SG CYS C 163 C ASJ F 10 1555 1555 1.77
CRYST1 50.400 70.300 93.400 90.00 102.40 90.00 P 1 21 1 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 0.019841 0.000000 0.004362 0.00000
SCALE2 0.000000 0.014225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010962 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
