HEADER HYDROLASE/HYDROLASE INHIBITOR 19-SEP-16 5TDI
TITLE CRYSTAL STRUCTURE OF CATHEPSIN K WITH A COVALENTLY-LINKED INHIBITOR AT
TITLE 2 1.4 ANGSTROM RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN K;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CATHEPSIN O,CATHEPSIN O2,CATHEPSIN X;
COMPND 5 EC: 3.4.22.38;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: CTSK, CTSO, CTSO2;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS GS115;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 644223
KEYWDS CATHEPSIN K, COVALENT, INHIBITOR, HYDROLASE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LAW,A.AGUDA,N.NGUYEN,G.BRAYER,D.BROMME
REVDAT 6 04-OCT-23 5TDI 1 COMPND HETNAM
REVDAT 5 08-JAN-20 5TDI 1 REMARK
REVDAT 4 27-SEP-17 5TDI 1 REMARK
REVDAT 3 08-MAR-17 5TDI 1 JRNL
REVDAT 2 01-FEB-17 5TDI 1 TITLE
REVDAT 1 25-JAN-17 5TDI 0
JRNL AUTH S.LAW,P.M.ANDRAULT,A.H.AGUDA,N.T.NGUYEN,N.KRUGLYAK,
JRNL AUTH 2 G.D.BRAYER,D.BROMME
JRNL TITL IDENTIFICATION OF MOUSE CATHEPSIN K STRUCTURAL ELEMENTS THAT
JRNL TITL 2 REGULATE THE POTENCY OF ODANACATIB.
JRNL REF BIOCHEM. J. V. 474 851 2017
JRNL REFN ESSN 1470-8728
JRNL PMID 28049758
JRNL DOI 10.1042/BCJ20160985
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 39559
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1939
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.1859 - 3.3738 0.99 2887 128 0.1547 0.1511
REMARK 3 2 3.3738 - 2.6780 0.98 2717 142 0.1527 0.1493
REMARK 3 3 2.6780 - 2.3395 0.99 2728 142 0.1494 0.1610
REMARK 3 4 2.3395 - 2.1256 1.00 2715 144 0.1341 0.1635
REMARK 3 5 2.1256 - 1.9732 0.99 2686 145 0.1334 0.1766
REMARK 3 6 1.9732 - 1.8569 0.98 2668 133 0.1316 0.1902
REMARK 3 7 1.8569 - 1.7639 0.99 2649 137 0.1306 0.1715
REMARK 3 8 1.7639 - 1.6871 0.99 2676 140 0.1275 0.1738
REMARK 3 9 1.6871 - 1.6222 0.99 2663 134 0.1268 0.1848
REMARK 3 10 1.6222 - 1.5662 0.99 2654 152 0.1287 0.1946
REMARK 3 11 1.5662 - 1.5172 0.98 2604 134 0.1330 0.2080
REMARK 3 12 1.5172 - 1.4738 0.99 2657 126 0.1397 0.2037
REMARK 3 13 1.4738 - 1.4350 0.99 2665 142 0.1457 0.1945
REMARK 3 14 1.4350 - 1.4000 0.99 2651 140 0.1577 0.2577
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.20
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1737
REMARK 3 ANGLE : 1.018 2347
REMARK 3 CHIRALITY : 0.072 235
REMARK 3 PLANARITY : 0.004 307
REMARK 3 DIHEDRAL : 13.678 635
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000224065.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI(111) AND SI(220) DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.2.1
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39625
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.162
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.8.1_1168
REMARK 200 STARTING MODEL: 4X6H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M CADMIUM SULFATE HYDRATE, 0.1 M
REMARK 280 HEPES PH 7.5, 1.0 M SODIUM ACETATE TRIHYDRATE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
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 22.62450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.62450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.31000
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 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 O HOH A 660 O HOH A 677 1.92
REMARK 500 O HOH A 634 O HOH A 664 1.97
REMARK 500 O HOH A 571 O HOH A 626 1.98
REMARK 500 O HOH A 600 O HOH A 658 2.07
REMARK 500 O HOH A 514 O HOH A 624 2.07
REMARK 500
REMARK 500 REMARK: NULL
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 619 O HOH A 635 4445 2.10
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 SER A 146 -51.86 -130.35
REMARK 500 ASN A 159 56.14 -111.06
REMARK 500 LYS A 200 60.99 -116.73
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 7AS A 301
DBREF 5TDI A 1 215 UNP P43235 CATK_HUMAN 115 329
SEQADV 5TDI ALA A 49 UNP P43235 SER 163 ENGINEERED MUTATION
SEQRES 1 A 215 ALA PRO ASP SER VAL ASP TYR ARG LYS LYS GLY TYR VAL
SEQRES 2 A 215 THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP
SEQRES 3 A 215 ALA PHE SER SER VAL GLY ALA LEU GLU GLY GLN LEU LYS
SEQRES 4 A 215 LYS LYS THR GLY LYS LEU LEU ASN LEU ALA PRO GLN ASN
SEQRES 5 A 215 LEU VAL ASP CYS VAL SER GLU ASN ASP GLY CYS GLY GLY
SEQRES 6 A 215 GLY TYR MET THR ASN ALA PHE GLN TYR VAL GLN LYS ASN
SEQRES 7 A 215 ARG GLY ILE ASP SER GLU ASP ALA TYR PRO TYR VAL GLY
SEQRES 8 A 215 GLN GLU GLU SER CYS MET TYR ASN PRO THR GLY LYS ALA
SEQRES 9 A 215 ALA LYS CYS ARG GLY TYR ARG GLU ILE PRO GLU GLY ASN
SEQRES 10 A 215 GLU LYS ALA LEU LYS ARG ALA VAL ALA ARG VAL GLY PRO
SEQRES 11 A 215 VAL SER VAL ALA ILE ASP ALA SER LEU THR SER PHE GLN
SEQRES 12 A 215 PHE TYR SER LYS GLY VAL TYR TYR ASP GLU SER CYS ASN
SEQRES 13 A 215 SER ASP ASN LEU ASN HIS ALA VAL LEU ALA VAL GLY TYR
SEQRES 14 A 215 GLY ILE GLN LYS GLY ASN LYS HIS TRP ILE ILE LYS ASN
SEQRES 15 A 215 SER TRP GLY GLU ASN TRP GLY ASN LYS GLY TYR ILE LEU
SEQRES 16 A 215 MET ALA ARG ASN LYS ASN ASN ALA CYS GLY ILE ALA ASN
SEQRES 17 A 215 LEU ALA SER PHE PRO LYS MET
HET 7AS A 301 36
HETNAM 7AS 4-FLUORO-N-{1-[(Z)-IMINOMETHYL]CYCLOPROPYL}-N~2~-{(1S)-
HETNAM 2 7AS 2,2,2-TRIFLUORO-1-[4'-(METHYLSULFONYL)[1,1'-BIPHENYL]-
HETNAM 3 7AS 4-YL]ETHYL }-L-LEUCINAMIDE
HETSYN 7AS COVALENTLY LINKED ODANACATIB
FORMUL 2 7AS C25 H29 F4 N3 O3 S
FORMUL 3 HOH *278(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 ALA A 49 VAL A 57 1 9
HELIX 4 AA4 ASP A 61 GLY A 65 5 5
HELIX 5 AA5 TYR A 67 ARG A 79 1 13
HELIX 6 AA6 ASN A 99 THR A 101 5 3
HELIX 7 AA7 ASN A 117 VAL A 128 1 12
HELIX 8 AA8 LEU A 139 PHE A 144 1 6
HELIX 9 AA9 ASN A 202 ILE A 206 5 5
SHEET 1 AA1 3 VAL A 5 ASP A 6 0
SHEET 2 AA1 3 HIS A 162 GLN A 172 -1 O TYR A 169 N VAL A 5
SHEET 3 AA1 3 VAL A 131 ILE A 135 -1 N VAL A 131 O ALA A 166
SHEET 1 AA2 5 VAL A 5 ASP A 6 0
SHEET 2 AA2 5 HIS A 162 GLN A 172 -1 O TYR A 169 N VAL A 5
SHEET 3 AA2 5 ASN A 175 LYS A 181 -1 O LYS A 181 N LEU A 165
SHEET 4 AA2 5 TYR A 193 ALA A 197 -1 O ILE A 194 N ILE A 180
SHEET 5 AA2 5 VAL A 149 TYR A 150 1 N TYR A 150 O LEU A 195
SHEET 1 AA3 2 ILE A 81 ASP A 82 0
SHEET 2 AA3 2 LYS A 103 ALA A 105 -1 O ALA A 104 N ILE A 81
SHEET 1 AA4 2 GLY A 109 GLU A 112 0
SHEET 2 AA4 2 SER A 211 LYS A 214 -1 O LYS A 214 N GLY A 109
SSBOND 1 CYS A 22 CYS A 63 1555 1555 2.03
SSBOND 2 CYS A 56 CYS A 96 1555 1555 2.02
SSBOND 3 CYS A 155 CYS A 204 1555 1555 2.02
LINK SG CYS A 25 C12 7AS A 301 1555 1555 1.78
SITE 1 AC1 22 GLN A 19 GLY A 23 SER A 24 CYS A 25
SITE 2 AC1 22 TRP A 26 GLU A 59 ASN A 60 ASP A 61
SITE 3 AC1 22 GLY A 64 GLY A 65 GLY A 66 TYR A 67
SITE 4 AC1 22 MET A 68 ALA A 134 THR A 140 SER A 141
SITE 5 AC1 22 PHE A 144 LEU A 160 ASN A 161 HIS A 162
SITE 6 AC1 22 ALA A 163 HOH A 456
CRYST1 45.249 54.620 80.300 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 0.022100 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012453 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
