HEADER HYDROLASE 13-SEP-07 2R9N
TITLE CATHEPSIN S COMPLEXED WITH COMPOUND 26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN S;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.22.27;
COMPND 5 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: CTSS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, CATHEPSIN, PROTEASE, GLYCOPROTEIN, LYSOSOME, POLYMORPHISM,
KEYWDS 2 THIOL PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.D.WARD,M.J.EMMANUEL,D.S.THOMSON,W.LIU,Y.BEKKALI,L.L.FRYE,
AUTHOR 2 M.GIRARDOT,T.MORWICK,E.R.R.YOUNG,R.ZINDELL,M.HRAPCHAK,M.DETURI,
AUTHOR 3 A.WHITE,K.M.CRANE,D.M.WHITE,Y.WANG,M.-H.HAO,C.A.GRYGON,M.E.LABADIA,
AUTHOR 4 J.WILDESON,D.FREEMAN,R.NELSON,A.CAPOLINO,J.D.PETERSON,E.L.RAYMOND,
AUTHOR 5 M.L.BROWN,D.M.SPERO
REVDAT 4 30-AUG-23 2R9N 1 SEQADV
REVDAT 3 24-JUL-19 2R9N 1 REMARK
REVDAT 2 24-FEB-09 2R9N 1 VERSN
REVDAT 1 18-DEC-07 2R9N 0
JRNL AUTH Y.D.WARD,M.J.EMMANUEL,D.S.THOMSON,W.LIU,Y.BEKKALI,L.L.FRYE,
JRNL AUTH 2 M.GIRARDOT,T.MORWICK,E.R.R.YOUNG,R.ZINDELL,M.HRAPCHAK,
JRNL AUTH 3 M.DETURI,A.WHITE,K.M.CRANE,D.M.WHITE,Y.WANG,M.-H.HAO,
JRNL AUTH 4 C.A.GRYGON,M.E.LABADIA,J.WILDESON,D.FREEMAN,R.NELSON,
JRNL AUTH 5 A.CAPOLINO,J.D.PETERSON,E.L.RAYMOND,M.L.BROWN,D.M.SPERO
JRNL TITL DESIGN AND SYNTHESIS OF REVERSIBLE INHIBITORS OF CATHEPSIN
JRNL TITL 2 S: ALPHA,ALPHA-DISUBSTITUTION AT THE P1 RESIDUE PROVIDES
JRNL TITL 3 POTENT INHIBITORS IN CELLULAR ASSAYS AND IN VIVO MODELS OF
JRNL TITL 4 ANTIGEN PRESENTATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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 : 38137
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) : 0.183
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1965
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 : 3364
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 312
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.16
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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 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 2R9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044598.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC FOCUSSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38189
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08100
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1MS6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NAOAC, 18-35% PEG MME (500
REMARK 280 -8000), 2 M (NH4)2SO4 WITH OR WITHOUT 15% GLYCEROL, PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 74.98050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.49025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 112.47075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 74.98050
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.47075
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 37.49025
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 B 376 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 390 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 433 LIES ON A SPECIAL POSITION.
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 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
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 ARG A 149 CG CD NE CZ NH1 NH2
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 DISTANCE
REMARK 500 SG CYS B 25 C32 Y14 B 281 1.91
REMARK 500 SG CYS A 25 C32 Y14 A 281 1.93
REMARK 500 O HOH A 324 O HOH A 343 2.17
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 THR A 58 -125.31 -110.00
REMARK 500 ASN A 163 -1.94 -145.97
REMARK 500 THR B 58 -131.18 -109.41
REMARK 500 ARG B 141 47.11 -82.94
REMARK 500 ASN B 163 1.11 -151.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R9M RELATED DB: PDB
REMARK 900 RELATED ID: 2R9O RELATED DB: PDB
DBREF 2R9N A 1 217 UNP P25774 CATS_HUMAN 115 331
DBREF 2R9N B 1 217 UNP P25774 CATS_HUMAN 115 331
SEQADV 2R9N HIS A 218 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS A 219 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS A 220 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS A 221 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS A 222 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS B 218 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS B 219 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS B 220 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS B 221 UNP P25774 EXPRESSION TAG
SEQADV 2R9N HIS B 222 UNP P25774 EXPRESSION TAG
SEQRES 1 A 222 LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS VAL
SEQRES 2 A 222 THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA CYS TRP
SEQRES 3 A 222 ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU LYS
SEQRES 4 A 222 LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN ASN
SEQRES 5 A 222 LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS GLY
SEQRES 6 A 222 CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR ILE
SEQRES 7 A 222 ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR PRO
SEQRES 8 A 222 TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER LYS
SEQRES 9 A 222 TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU PRO
SEQRES 10 A 222 TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA ASN
SEQRES 11 A 222 LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS PRO
SEQRES 12 A 222 SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU PRO
SEQRES 13 A 222 SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL VAL
SEQRES 14 A 222 GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU VAL
SEQRES 15 A 222 LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY TYR
SEQRES 16 A 222 ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY ILE
SEQRES 17 A 222 ALA SER PHE PRO SER TYR PRO GLU ILE HIS HIS HIS HIS
SEQRES 18 A 222 HIS
SEQRES 1 B 222 LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS VAL
SEQRES 2 B 222 THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA CYS TRP
SEQRES 3 B 222 ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU LYS
SEQRES 4 B 222 LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN ASN
SEQRES 5 B 222 LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS GLY
SEQRES 6 B 222 CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR ILE
SEQRES 7 B 222 ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR PRO
SEQRES 8 B 222 TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER LYS
SEQRES 9 B 222 TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU PRO
SEQRES 10 B 222 TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA ASN
SEQRES 11 B 222 LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS PRO
SEQRES 12 B 222 SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU PRO
SEQRES 13 B 222 SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL VAL
SEQRES 14 B 222 GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU VAL
SEQRES 15 B 222 LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY TYR
SEQRES 16 B 222 ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY ILE
SEQRES 17 B 222 ALA SER PHE PRO SER TYR PRO GLU ILE HIS HIS HIS HIS
SEQRES 18 B 222 HIS
HET Y14 A 281 34
HET Y14 B 281 34
HETNAM Y14 N-[(1S)-2-{[(3S)-1-BENZYL-3-CYANOPYRROLIDIN-3-
HETNAM 2 Y14 YL]AMINO}-1-(CYCLOHEXYLMETHYL)-2-OXOETHYL]MORPHOLINE-
HETNAM 3 Y14 4-CARBOXAMIDE
FORMUL 3 Y14 2(C26 H37 N5 O3)
FORMUL 5 HOH *312(H2 O)
HELIX 1 1 ARG A 8 GLY A 11 5 4
HELIX 2 2 ALA A 24 GLY A 43 1 20
HELIX 3 3 SER A 49 SER A 57 1 9
HELIX 4 4 THR A 58 GLY A 62 5 5
HELIX 5 5 LYS A 64 GLY A 68 5 5
HELIX 6 6 PHE A 70 LYS A 82 1 13
HELIX 7 7 ASP A 102 LYS A 104 5 3
HELIX 8 8 ARG A 120 LYS A 131 1 12
HELIX 9 9 HIS A 142 LEU A 147 1 6
HELIX 10 10 ASN A 204 ILE A 208 5 5
HELIX 11 11 ARG B 8 GLY B 11 5 4
HELIX 12 12 ALA B 24 GLY B 43 1 20
HELIX 13 13 SER B 49 SER B 57 1 9
HELIX 14 14 THR B 58 GLY B 62 5 5
HELIX 15 15 LYS B 64 GLY B 68 5 5
HELIX 16 16 PHE B 70 LYS B 82 1 13
HELIX 17 17 ASP B 102 LYS B 104 5 3
HELIX 18 18 ARG B 120 LYS B 131 1 12
HELIX 19 19 HIS B 142 TYR B 148 1 7
HELIX 20 20 ASN B 204 ILE B 208 5 5
SHEET 1 A 3 VAL A 5 ASP A 6 0
SHEET 2 A 3 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 A 3 VAL A 134 VAL A 138 -1 N VAL A 136 O VAL A 166
SHEET 1 B 4 VAL A 5 ASP A 6 0
SHEET 2 B 4 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 B 4 LYS A 177 LYS A 183 -1 O LYS A 183 N LEU A 167
SHEET 4 B 4 TYR A 195 ALA A 199 -1 O ILE A 196 N VAL A 182
SHEET 1 C 2 ILE A 84 ASP A 85 0
SHEET 2 C 2 ARG A 106 ALA A 108 -1 O ALA A 107 N ILE A 84
SHEET 1 D 2 LYS A 112 GLU A 115 0
SHEET 2 D 2 SER A 213 GLU A 216 -1 O TYR A 214 N THR A 114
SHEET 1 E 3 VAL B 5 ASP B 6 0
SHEET 2 E 3 HIS B 164 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 E 3 VAL B 134 VAL B 138 -1 N VAL B 136 O VAL B 166
SHEET 1 F 5 VAL B 5 ASP B 6 0
SHEET 2 F 5 HIS B 164 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 F 5 LYS B 177 LYS B 183 -1 O LYS B 183 N LEU B 167
SHEET 4 F 5 TYR B 195 ALA B 199 -1 O MET B 198 N TRP B 180
SHEET 5 F 5 VAL B 152 TYR B 153 1 N TYR B 153 O ARG B 197
SHEET 1 G 2 ILE B 84 ASP B 85 0
SHEET 2 G 2 ARG B 106 ALA B 108 -1 O ALA B 107 N ILE B 84
SHEET 1 H 2 LYS B 112 GLU B 115 0
SHEET 2 H 2 SER B 213 GLU B 216 -1 O TYR B 214 N THR B 114
SSBOND 1 CYS A 22 CYS A 66 1555 1555 2.05
SSBOND 2 CYS A 56 CYS A 99 1555 1555 2.04
SSBOND 3 CYS A 158 CYS A 206 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 66 1555 1555 2.03
SSBOND 5 CYS B 56 CYS B 99 1555 1555 2.04
SSBOND 6 CYS B 158 CYS B 206 1555 1555 2.04
CRYST1 85.296 85.296 149.961 90.00 90.00 90.00 P 41 2 2 16
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 0.011724 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011724 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END