HEADER HYDROLASE 27-NOV-15 5F02
TITLE CATHEPSIN L IN COMPLEX WITH (2S,4R)-4-(2-CHLORO-4-METHOXY-
TITLE 2 BENZENESULFONYL)-1-[3-(5-CHLORO-PYRIDIN-2-YL)-AZETIDINE-3-CARBONYL]-
TITLE 3 PYRROLIDINE-2-CARBOXYLIC ACID (1-CYANO-CYCLOPROPYL)-AMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN L1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 114-333;
COMPND 5 SYNONYM: CATHEPSIN L,MAJOR EXCRETED PROTEIN,MEP;
COMPND 6 EC: 3.4.22.15;
COMPND 7 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: CTSL, CTSL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEASE INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BANNER,J.BENZ,M.STIHLE,A.KUGLSTATTER
REVDAT 2 25-MAY-16 5F02 1 JRNL
REVDAT 1 24-FEB-16 5F02 0
JRNL AUTH B.KUHN,W.GUBA,J.HERT,D.BANNER,C.BISSANTZ,S.CECCARELLI,
JRNL AUTH 2 W.HAAP,M.KORNER,A.KUGLSTATTER,C.LERNER,P.MATTEI,W.NEIDHART,
JRNL AUTH 3 E.PINARD,M.G.RUDOLPH,T.SCHULZ-GASCH,T.WOLTERING,M.STAHL
JRNL TITL A REAL-WORLD PERSPECTIVE ON MOLECULAR DESIGN.
JRNL REF J.MED.CHEM. V. 59 4087 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26878596
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01875
REMARK 2
REMARK 2 RESOLUTION. 1.43 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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 34024
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1865
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) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2172
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1688
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.92000
REMARK 3 B22 (A**2) : -1.53000
REMARK 3 B33 (A**2) : 2.45000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.649
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1858 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1249 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2529 ; 1.257 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3044 ; 0.849 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 234 ; 5.352 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;34.528 ;24.943
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 295 ;12.266 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;10.465 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 251 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2131 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 382 ; 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): 3107 ; 2.442 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 59 ;28.714 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3213 ;11.159 ; 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 5F02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34024
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 45.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.450
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.16
REMARK 200 R MERGE FOR SHELL (I) : 0.69410
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.490
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MAGNESIUM FORMATE, 15 % PEG 3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 22.96850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.84550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.74600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.84550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.96850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.74600
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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: 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 497 O HOH A 598 3645 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 ALA A 202 125.98 -39.56
REMARK 500 ALA A 214 62.56 -150.81
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5T9 A 302
DBREF 5F02 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 GOL A 301 12
HET 5T9 A 302 60
HETNAM GOL GLYCEROL
HETNAM 5T9 (2~{S},4~{R})-4-[(2-CHLORANYL-4-METHOXY-PHENYL)-
HETNAM 2 5T9 BIS(OXIDANYL)-$L^{4}-SULFANYL]-1-[3-(5-
HETNAM 3 5T9 CHLORANYLPYRIDIN-2-YL)AZETIDIN-3-YL]CARBONYL-~{N}-[1-
HETNAM 4 5T9 (IMINOMETHYL)CYCLOPROPYL]PYRROLIDINE-2-CARBOXAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 5T9 C25 H29 CL2 N5 O5 S
FORMUL 4 HOH *222(H2 O)
HELIX 1 AA1 ARG A 8 GLY A 11 5 4
HELIX 2 AA2 SER A 24 GLY A 43 1 20
HELIX 3 AA3 SER A 49 SER A 57 1 9
HELIX 4 AA4 GLY A 58 GLY A 61 5 4
HELIX 5 AA5 GLU A 63 GLY A 67 5 5
HELIX 6 AA6 LEU A 69 GLY A 81 1 13
HELIX 7 AA7 ASN A 101 LYS A 103 5 3
HELIX 8 AA8 GLN A 118 VAL A 129 1 12
HELIX 9 AA9 HIS A 140 PHE A 145 1 6
HELIX 10 AB1 ASN A 207 ILE A 211 5 5
SHEET 1 AA1 3 VAL A 5 ASP A 6 0
SHEET 2 AA1 3 HIS A 163 PHE A 172 -1 O TYR A 170 N VAL A 5
SHEET 3 AA1 3 ILE A 132 ILE A 136 -1 N ILE A 132 O VAL A 167
SHEET 1 AA2 5 VAL A 5 ASP A 6 0
SHEET 2 AA2 5 HIS A 163 PHE A 172 -1 O TYR A 170 N VAL A 5
SHEET 3 AA2 5 LYS A 181 LYS A 186 -1 O LYS A 186 N LEU A 166
SHEET 4 AA2 5 TYR A 198 ALA A 202 -1 O MET A 201 N TRP A 183
SHEET 5 AA2 5 ILE A 150 TYR A 151 1 N TYR A 151 O LYS A 200
SHEET 1 AA3 2 LEU A 83 ASP A 84 0
SHEET 2 AA3 2 SER A 105 ALA A 107 -1 O VAL A 106 N LEU A 83
SHEET 1 AA4 2 PHE A 112 ASP A 114 0
SHEET 2 AA4 2 SER A 216 PRO A 218 -1 O TYR A 217 N VAL A 113
SSBOND 1 CYS A 22 CYS A 65 1555 1555 2.04
SSBOND 2 CYS A 56 CYS A 98 1555 1555 2.10
SSBOND 3 CYS A 156 CYS A 209 1555 1555 2.04
LINK SG CYS A 25 C11 5T9 A 302 1555 1555 1.76
SITE 1 AC1 5 ASN A 18 GLN A 19 GLY A 20 TRP A 189
SITE 2 AC1 5 HOH A 528
SITE 1 AC2 22 GLN A 19 GLY A 23 SER A 24 CYS A 25
SITE 2 AC2 22 TRP A 26 GLY A 61 GLU A 63 GLY A 67
SITE 3 AC2 22 GLY A 68 LEU A 69 MET A 70 ALA A 135
SITE 4 AC2 22 MET A 161 ASP A 162 HIS A 163 GLY A 164
SITE 5 AC2 22 ASP A 178 ARG A 206 ALA A 214 HOH A 525
SITE 6 AC2 22 HOH A 581 HOH A 592
CRYST1 45.937 57.492 75.691 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 0.021769 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017394 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013212 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
