HEADER HYDROLASE/HYDROLASE INHIBITOR 26-MAY-06 2H5I
TITLE CRYSTAL STRUCTURE OF CASPASE-3 WITH INHIBITOR AC-DEVD-CHO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3, P17 SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 29-174;
COMPND 5 SYNONYM: CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, YAMA PROTEIN, CPP-
COMPND 6 32, SREBP CLEAVAGE ACTIVITY 1, SCA-1;
COMPND 7 EC: 3.4.22.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CASPASE-3, P12 SUBUNIT;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RESIDUES 184-277;
COMPND 13 EC: 3.4.22.-;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: AC-DEV(ASJ);
COMPND 17 CHAIN: C;
COMPND 18 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 BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CASP3, CPP32;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET23B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES
KEYWDS ENZYME CATALYSIS, CYSTEINE PROTEASE, APOPTOSIS, INDUCED FIT,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.FANG,P.I.BOROSS,J.TOZSER,I.T.WEBER
REVDAT 5 15-NOV-23 2H5I 1 REMARK
REVDAT 4 30-AUG-23 2H5I 1 SEQADV LINK
REVDAT 3 13-JUL-11 2H5I 1 VERSN
REVDAT 2 24-FEB-09 2H5I 1 VERSN
REVDAT 1 19-SEP-06 2H5I 0
JRNL AUTH B.FANG,P.I.BOROSS,J.TOZSER,I.T.WEBER
JRNL TITL STRUCTURAL AND KINETIC ANALYSIS OF CASPASE-3 REVEALS ROLE
JRNL TITL 2 FOR S5 BINDING SITE IN SUBSTRATE RECOGNITION
JRNL REF J.MOL.BIOL. V. 360 654 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16781734
JRNL DOI 10.1016/J.JMB.2006.05.041
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.187
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.184
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1651
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 32669
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.179
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.176
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1515
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 30041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1974
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2197.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 6
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 8881
REMARK 3 NUMBER OF RESTRAINTS : 8132
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.026
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.038
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.051
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.014
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.047
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000037954.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : SI 220
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, MADCCD
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32669
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.35700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
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: 1NME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, 5% GLYCEROL, 10
REMARK 280 MM DITHIOTHREITOL AND 14-18% PEG 6000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.02500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.99500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.02500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.99500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.02500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.99500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.02500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.99500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 486 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE INHIBITOR IS COVALENTLY CONNECTED TO CYS OF THE ENZYME TO FORM
REMARK 400 A HEMITHIOKETAL
REMARK 400
REMARK 400 THE AC-ASP-GLU-VAL-ASP-ALDEHYDE IS PEPTIDE-LIKE, A MEMBER OF
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: AC-ASP-GLU-VAL-ASP-ALDEHYDE
REMARK 400 CHAIN: C
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 CYS B 184
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF AC-DEV(ASJ)
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H5J RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH AC-DMQD-CHO
REMARK 900 RELATED ID: 2H65 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH AC-VDVAD-CHO
DBREF 2H5I A 29 174 UNP P42574 CASP3_HUMAN 29 174
DBREF 2H5I B 184 277 UNP P42574 CASP3_HUMAN 184 277
DBREF 2H5I C 1 5 PDB 2H5I 2H5I 1 5
SEQADV 2H5I HIS B 278 UNP P42574 EXPRESSION TAG
SEQRES 1 A 146 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 A 146 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 A 146 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 A 146 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 A 146 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 A 146 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 A 146 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 A 146 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 A 146 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 A 146 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 A 146 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP CYS GLY
SEQRES 12 A 146 ILE GLU THR
SEQRES 1 B 95 CYS HIS LYS ILE PRO VAL GLU ALA ASP PHE LEU TYR ALA
SEQRES 2 B 95 TYR SER THR ALA PRO GLY TYR TYR SER TRP ARG ASN SER
SEQRES 3 B 95 LYS ASP GLY SER TRP PHE ILE GLN SER LEU CYS ALA MET
SEQRES 4 B 95 LEU LYS GLN TYR ALA ASP LYS LEU GLU PHE MET HIS ILE
SEQRES 5 B 95 LEU THR ARG VAL ASN ARG LYS VAL ALA THR GLU PHE GLU
SEQRES 6 B 95 SER PHE SER PHE ASP ALA THR PHE HIS ALA LYS LYS GLN
SEQRES 7 B 95 ILE PRO CYS ILE VAL SER MET LEU THR LYS GLU LEU TYR
SEQRES 8 B 95 PHE TYR HIS HIS
SEQRES 1 C 5 ACE ASP GLU VAL ASJ
HET ACE C 1 3
HET ASJ C 5 8
HETNAM ACE ACETYL GROUP
HETNAM ASJ (3S)-3-AMINO-4-HYDROXYBUTANOIC ACID
FORMUL 3 ACE C2 H4 O
FORMUL 3 ASJ C4 H9 N O3
FORMUL 4 HOH *224(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 PHE A 142 1 7
HELIX 5 5 CYS A 148 THR A 152 5 5
HELIX 6 6 TRP B 214 ALA B 227 1 14
HELIX 7 7 GLU B 231 PHE B 247 1 17
HELIX 8 8 ASP B 253 HIS B 257 5 5
SHEET 1 A 6 GLU A 84 ASN A 89 0
SHEET 2 A 6 LEU A 46 ASN A 51 1 N ASN A 51 O LYS A 88
SHEET 3 A 6 PHE A 114 LEU A 119 1 O VAL A 117 N ILE A 48
SHEET 4 A 6 LYS A 156 GLN A 161 1 O ILE A 159 N CYS A 116
SHEET 5 A 6 PHE B 193 TYR B 197 1 O LEU B 194 N PHE A 158
SHEET 6 A 6 CYS B 264 SER B 267 -1 O VAL B 266 N TYR B 195
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 3 GLY B 212 SER B 213 0
SHEET 2 C 3 TRP B 206 ASN B 208 -1 N ASN B 208 O GLY B 212
SHEET 3 C 3 GLU C 3 VAL C 4 -1 O GLU C 3 N ARG B 207
LINK SG CYS A 163 C ASJ C 5 1555 1555 1.82
LINK C ACE C 1 N ASP C 2 1555 1555 1.33
LINK C VAL C 4 N ASJ C 5 1555 1555 1.34
SITE 1 AC1 22 SER A 58 ARG A 64 HIS A 121 GLY A 122
SITE 2 AC1 22 GLN A 161 CYS A 163 HOH A 414 SER B 205
SITE 3 AC1 22 TRP B 206 ARG B 207 ASN B 208 SER B 209
SITE 4 AC1 22 TRP B 214 SER B 249 PHE B 250 HOH B 324
SITE 5 AC1 22 HOH C 327 HOH C 378 HOH C 394 HOH C 427
SITE 6 AC1 22 HOH C 468 HOH C 480
CRYST1 69.920 86.050 97.990 90.00 90.00 90.00 I 2 2 2 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 0.014302 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
