HEADER HYDROLASE 21-AUG-17 5QBZ
TITLE CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN S;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.22.27;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS D3R, CATHEPSIN S, LIGAND DOCKING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,S.K.BURLEY
REVDAT 4 17-NOV-21 5QBZ 1 REMARK
REVDAT 3 10-FEB-21 5QBZ 1 AUTHOR JRNL
REVDAT 2 21-FEB-18 5QBZ 1 REMARK
REVDAT 1 20-DEC-17 5QBZ 0
JRNL AUTH S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,
JRNL AUTH 2 S.K.BURLEY
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 5712
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 273
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 381
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1676
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.399
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.280
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.329
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.876
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1772 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1530 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2405 ; 1.165 ; 1.921
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3560 ; 0.945 ; 2.991
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 216 ; 5.633 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;40.470 ;24.375
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 270 ;15.376 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;17.794 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 239 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2008 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 380 ; 0.001 ; 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5QBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1001401756.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.50
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5712
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 35.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 4.5, 200MM
REMARK 280 AMMONIUM ACETATE, 25% PEG 8000. PROTEIN CONCENTRATION 7 MG/ML,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 4.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 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+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 44.52300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.44700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.44700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.26150
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.44700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.44700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.78450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.44700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.44700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.26150
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.44700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.44700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.78450
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 0.00000
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 44.52300
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 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 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 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 A1036 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 ILE A 0
REMARK 465 LEU A 218
REMARK 465 GLN A 219
REMARK 465 GLY A 220
REMARK 465 GLY A 221
REMARK 465 GLY A 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 LYS A 60 CD CE NZ
REMARK 470 LYS A 82 CE NZ
REMARK 470 LYS A 98 CG CD CE NZ
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 -118.07 -114.23
REMARK 500 TYR A 90 69.30 -155.79
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 residue B8Y A 901
DBREF 5QBZ A 0 217 UNP P25774 CATS_HUMAN 114 331
SEQADV 5QBZ SER A 25 UNP P25774 CYS 139 ENGINEERED MUTATION
SEQADV 5QBZ LEU A 218 UNP P25774 EXPRESSION TAG
SEQADV 5QBZ GLN A 219 UNP P25774 EXPRESSION TAG
SEQADV 5QBZ GLY A 220 UNP P25774 EXPRESSION TAG
SEQADV 5QBZ GLY A 221 UNP P25774 EXPRESSION TAG
SEQADV 5QBZ GLY A 222 UNP P25774 EXPRESSION TAG
SEQRES 1 A 223 ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS
SEQRES 2 A 223 VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER
SEQRES 3 A 223 TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU
SEQRES 4 A 223 LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN
SEQRES 5 A 223 ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS
SEQRES 6 A 223 GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR
SEQRES 7 A 223 ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR
SEQRES 8 A 223 PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER
SEQRES 9 A 223 LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU
SEQRES 10 A 223 PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA
SEQRES 11 A 223 ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS
SEQRES 12 A 223 PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU
SEQRES 13 A 223 PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL
SEQRES 14 A 223 VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU
SEQRES 15 A 223 VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY
SEQRES 16 A 223 TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY
SEQRES 17 A 223 ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY
SEQRES 18 A 223 GLY GLY
HET B8Y A 901 46
HETNAM B8Y N-{[2-CHLORO-5-(4-{3-[4-(6-CHLORO-3-METHYL-2-OXO-2,3-
HETNAM 2 B8Y DIHYDRO-1H-BENZIMIDAZOL-1-YL)PIPERIDIN-1-YL]PROPYL}-3-
HETNAM 3 B8Y OXO-3,4-DIHYDROPYRAZIN-2-YL)PHENYL]METHYL}-4-
HETNAM 4 B8Y FLUOROBENZAMIDE
FORMUL 2 B8Y C34 H33 CL2 F N6 O3
FORMUL 3 HOH *37(H2 O)
HELIX 1 AA1 ALA A 24 GLY A 43 1 20
HELIX 2 AA2 SER A 49 SER A 57 1 9
HELIX 3 AA3 THR A 58 GLY A 62 5 5
HELIX 4 AA4 LYS A 64 GLY A 68 5 5
HELIX 5 AA5 PHE A 70 ASN A 81 1 12
HELIX 6 AA6 ASP A 102 LYS A 104 5 3
HELIX 7 AA7 ARG A 120 LYS A 131 1 12
HELIX 8 AA8 HIS A 142 TYR A 148 1 7
HELIX 9 AA9 ASN A 204 ILE A 208 5 5
SHEET 1 AA1 3 VAL A 5 ASP A 6 0
SHEET 2 AA1 3 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 AA1 3 VAL A 134 VAL A 138 -1 N VAL A 136 O VAL A 166
SHEET 1 AA2 5 VAL A 5 ASP A 6 0
SHEET 2 AA2 5 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 AA2 5 LYS A 177 LYS A 183 -1 O LYS A 183 N LEU A 167
SHEET 4 AA2 5 TYR A 195 ALA A 199 -1 O MET A 198 N TRP A 180
SHEET 5 AA2 5 VAL A 152 TYR A 153 1 N TYR A 153 O ARG A 197
SHEET 1 AA3 2 ILE A 84 ASP A 85 0
SHEET 2 AA3 2 ARG A 106 ALA A 108 -1 O ALA A 107 N ILE A 84
SHEET 1 AA4 2 LYS A 112 GLU A 115 0
SHEET 2 AA4 2 SER A 213 GLU A 216 -1 O TYR A 214 N THR A 114
SSBOND 1 CYS A 22 CYS A 66 1555 1555 2.03
SSBOND 2 CYS A 56 CYS A 99 1555 1555 2.03
SSBOND 3 CYS A 158 CYS A 206 1555 1555 2.03
SITE 1 AC1 18 TYR A 18 GLY A 20 GLY A 62 LYS A 64
SITE 2 AC1 18 ASN A 67 GLY A 68 GLY A 69 PHE A 70
SITE 3 AC1 18 THR A 73 PHE A 146 LEU A 147 VAL A 162
SITE 4 AC1 18 HIS A 164 GLY A 165 TRP A 186 ASN A 189
SITE 5 AC1 18 PHE A 211 HOH A1019
CRYST1 70.894 70.894 89.046 90.00 90.00 90.00 P 41 21 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 0.014106 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
