HEADER HYDROLASE 19-MAY-11 2YJ8
TITLE CATHEPSIN L WITH A NITRILE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN L1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 114-333;
COMPND 5 SYNONYM: MAJOR EXCRETED PROTEIN, MEP, CATHEPSIN L1 HEAVY CHAIN,
COMPND 6 CATHEPSIN L1 LIGHT CHAIN;
COMPND 7 EC: 3.4.22.15;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, DRUG DESIGN, THIOL PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.BANNER,J.M.BENZ,W.HAAP
REVDAT 1 23-NOV-11 2YJ8 0
JRNL AUTH L.A.HARDEGGER,B.KUHN,B.SPINNLER,L.ANSELM,R.ECABERT,M.STIHLE,
JRNL AUTH 2 B.GSELL,R.THOMA,J.DIEZ,J.M.BENZ,J.PLANCHER,G.HARTMANN,
JRNL AUTH 3 Y.ISSHIKI,K.MORIKAMI,N.SHIMMA,W.HAAP,D.W.BANNER,F.DIEDERICH
JRNL TITL HALOGEN BONDING AT THE ACTIVE SITES OF HUMAN CATHEPSIN L
JRNL TITL 2 AND MEK1 KINASE: EFFICIENT INTERACTIONS IN DIFFERENT
JRNL TITL 3 ENVIRONMENTS.
JRNL REF CHEMMEDCHEM V. 6 2048 2011
JRNL REFN ISSN 1860-7179
JRNL PMID 21898833
JRNL DOI 10.1002/CMDC.201100353
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0112
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.46
REMARK 3 NUMBER OF REFLECTIONS : 45543
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 + TEST SET) : 0.14264
REMARK 3 R VALUE (WORKING SET) : 0.14055
REMARK 3 FREE R VALUE : 0.18159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2417
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.300
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.334
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2964
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.326
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.318
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1795
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.877
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.02
REMARK 3 B22 (A**2) : -1.15
REMARK 3 B33 (A**2) : 2.18
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.053
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.052
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.766
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1897 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1269 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2589 ; 1.414 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3097 ; 0.889 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 242 ; 5.584 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 92 ;35.595 ;25.217
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 300 ;12.362 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;13.137 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 255 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2213 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 398 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3166 ; 2.738 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 74 ;39.661 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3302 ;17.631 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. HYDROGENS GENERATED IN REFMAC, THOSE WITH ZERO
REMARK 3 OCCUPANCY REMOVED. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 2YJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-11.
REMARK 100 THE PDBE ID CODE IS EBI-48337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.7
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50228
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.30
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.59
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.57
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.8
REMARK 200 R MERGE FOR SHELL (I) : 0.78
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.46
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: ISOMORPHOUS TO PDB ENTRY 2YJ2
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 0.2M
REMARK 280 SODIUM ACETATE, 25 % PEG 3350
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 22.98750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.10900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.63250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.10900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.98750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.63250
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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLU A 176
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 GLN A 21 50.96 -92.88
REMARK 500 ASP A 160 70.73 -109.11
REMARK 500 ASP A 162 15.70 -140.09
REMARK 500 ALA A 214 61.36 -151.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE NITRILE (2S,4R)-4-(2-CHLORO-BENZENESULFONYL)-1-[1-(4-IODO-PHENYL)
REMARK 600 -CYCLOPROPANECARBONYL]-PYRROLIDINE-2-CARBOXYLIC ACID (1-CYANO-
REMARK 600 CYCLOPROPYL)-AMIDE MAKES A COVALENT LINK TO THE ENZYME
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YJ8 A1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1222
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CJL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM
REMARK 900 RELATED ID: 1CS8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROCATHEPSIN L
REMARK 900 RELATED ID: 2XU4 RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 2VHS RELATED DB: PDB
REMARK 900 CATHSILICATEIN, A CHIMERA
REMARK 900 RELATED ID: 1ICF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II
REMARK 900 FRAGMENT IN COMPLEX WITH CATHEPSIN L
REMARK 900 RELATED ID: 2XU3 RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 1MHW RELATED DB: PDB
REMARK 900 DESIGN OF NON-COVALENT INHIBITORS OF HUMAN CATHEPSIN L
REMARK 900 .FROM THE 96-RESIDUE PROREGION TO OPTIMIZED TRIPEPTIDES
REMARK 900 RELATED ID: 2XU5 RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 2XU1 RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 2YJ9 RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 2YJB RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 2YJ2 RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
REMARK 900 RELATED ID: 2YJC RELATED DB: PDB
REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR
DBREF 2YJ8 A 1 220 UNP P07711 CATL1_HUMAN 114 333
SEQRES 1 A 220 ALA PRO ARG SER VAL ASP TRP ARG GLU LYS GLY TYR VAL
SEQRES 2 A 220 THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP
SEQRES 3 A 220 ALA PHE SER ALA THR GLY ALA LEU GLU GLY GLN MET PHE
SEQRES 4 A 220 ARG LYS THR GLY ARG LEU ILE SER LEU SER GLU GLN ASN
SEQRES 5 A 220 LEU VAL ASP CYS SER GLY PRO GLN GLY ASN GLU GLY CYS
SEQRES 6 A 220 ASN GLY GLY LEU MET ASP TYR ALA PHE GLN TYR VAL GLN
SEQRES 7 A 220 ASP ASN GLY GLY LEU ASP SER GLU GLU SER TYR PRO TYR
SEQRES 8 A 220 GLU ALA THR GLU GLU SER CYS LYS TYR ASN PRO LYS TYR
SEQRES 9 A 220 SER VAL ALA ASN ASP THR GLY PHE VAL ASP ILE PRO LYS
SEQRES 10 A 220 GLN GLU LYS ALA LEU MET LYS ALA VAL ALA THR VAL GLY
SEQRES 11 A 220 PRO ILE SER VAL ALA ILE ASP ALA GLY HIS GLU SER PHE
SEQRES 12 A 220 LEU PHE TYR LYS GLU GLY ILE TYR PHE GLU PRO ASP CYS
SEQRES 13 A 220 SER SER GLU ASP MET ASP HIS GLY VAL LEU VAL VAL GLY
SEQRES 14 A 220 TYR GLY PHE GLU SER THR GLU SER ASP ASN ASN LYS TYR
SEQRES 15 A 220 TRP LEU VAL LYS ASN SER TRP GLY GLU GLU TRP GLY MET
SEQRES 16 A 220 GLY GLY TYR VAL LYS MET ALA LYS ASP ARG ARG ASN HIS
SEQRES 17 A 220 CYS GLY ILE ALA SER ALA ALA SER TYR PRO THR VAL
HET YJ8 A1221 58
HET GOL A1222 12
HETNAM YJ8 (2S,4R)-4-(2-CHLORO-BENZENESULFONYL)-1-[1-(4-
HETNAM 2 YJ8 IODO-PHENYL)-CYCLOPROPANECARBONYL]-
HETNAM 3 YJ8 PYRROLIDINE-2-CARBOXYLIC ACID (1-IMINOMETHYL-
HETNAM 4 YJ8 CYCLOPROPYL)-AMIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN
FORMUL 2 YJ8 C25 H25 CL I N3 O4 S
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *271(H2 O)
HELIX 1 1 ARG A 8 GLY A 11 5 4
HELIX 2 2 SER A 24 GLY A 43 1 20
HELIX 3 3 SER A 49 SER A 57 1 9
HELIX 4 4 GLU A 63 CYS A 65 5 3
HELIX 5 5 LEU A 69 GLY A 81 1 13
HELIX 6 6 ASN A 101 LYS A 103 5 3
HELIX 7 7 GLN A 118 GLY A 130 1 13
HELIX 8 8 HIS A 140 PHE A 145 1 6
HELIX 9 9 ASN A 207 ILE A 211 5 5
SHEET 1 AA 2 VAL A 5 ASP A 6 0
SHEET 2 AA 2 HIS A 163 PHE A 172 1 O TYR A 170 N VAL A 5
SHEET 1 AB 2 ILE A 132 ILE A 136 0
SHEET 2 AB 2 HIS A 163 PHE A 172 -1 O HIS A 163 N ILE A 136
SHEET 1 AC 5 ILE A 150 TYR A 151 0
SHEET 2 AC 5 TYR A 198 ALA A 202 1 O LYS A 200 N TYR A 151
SHEET 3 AC 5 LYS A 181 LYS A 186 -1 O TRP A 183 N MET A 201
SHEET 4 AC 5 HIS A 163 PHE A 172 -1 O LEU A 166 N LYS A 186
SHEET 5 AC 5 ILE A 132 ILE A 136 -1 O ILE A 132 N VAL A 167
SHEET 1 AD 5 ILE A 150 TYR A 151 0
SHEET 2 AD 5 TYR A 198 ALA A 202 1 O LYS A 200 N TYR A 151
SHEET 3 AD 5 LYS A 181 LYS A 186 -1 O TRP A 183 N MET A 201
SHEET 4 AD 5 HIS A 163 PHE A 172 -1 O LEU A 166 N LYS A 186
SHEET 5 AD 5 VAL A 5 ASP A 6 1 O VAL A 5 N TYR A 170
SHEET 1 AE 2 LEU A 83 ASP A 84 0
SHEET 2 AE 2 SER A 105 ALA A 107 -1 N VAL A 106 O LEU A 83
SHEET 1 AF 2 GLY A 111 ASP A 114 0
SHEET 2 AF 2 SER A 216 THR A 219 -1 O TYR A 217 N VAL A 113
SSBOND 1 CYS A 22 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 56 CYS A 98 1555 1555 2.08
SSBOND 3 CYS A 156 CYS A 209 1555 1555 2.04
LINK SG CYS A 25 C18 YJ8 A1221 1555 1555 1.78
SITE 1 AC1 19 GLN A 19 GLY A 23 SER A 24 CYS A 25
SITE 2 AC1 19 TRP A 26 GLY A 61 GLY A 67 GLY A 68
SITE 3 AC1 19 LEU A 69 MET A 70 ALA A 135 MET A 161
SITE 4 AC1 19 ASP A 162 HIS A 163 GLY A 164 ARG A 206
SITE 5 AC1 19 ALA A 214 HOH A2131 HOH A2271
SITE 1 AC2 2 ASN A 18 HOH A2064
CRYST1 45.975 57.265 76.218 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 0.021751 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013120 0.00000
(ATOM LINES ARE NOT SHOWN.)
END