HEADER HYDROLASE/HYDROLASE INHIBITOR 12-JUN-13 4L6B
TITLE ENDOTHIAPEPSIN IN COMPLEX WITH THIOPHEN-BASED INHIBITOR SAP128
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHIAPEPSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 90-419;
COMPND 5 SYNONYM: ASPARTATE PROTEASE;
COMPND 6 EC: 3.4.23.22
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA;
SOURCE 3 ORGANISM_COMMON: CHESNUT BLIGHT FUNGUS;
SOURCE 4 ORGANISM_TAXID: 5116
KEYWDS ASPARTATE PROTEASE, INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PARK,A.HEINE,G.KLEBE
REVDAT 1 18-JUN-14 4L6B 0
JRNL AUTH M.KUHNERT,A.PARK,A.HEINE,G.KLEBE,W.E.DIEDERICH
JRNL TITL ENDOTHIAPEPSIN IN COMPLEX WITH THIOPHEN BASED INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 68853
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3450
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 29.5897 - 3.9967 1.00 2698 135 0.1721 0.2072
REMARK 3 2 3.9967 - 3.1735 1.00 2646 138 0.1860 0.1983
REMARK 3 3 3.1735 - 2.7727 1.00 2646 138 0.1912 0.2023
REMARK 3 4 2.7727 - 2.5193 1.00 2580 162 0.1812 0.2067
REMARK 3 5 2.5193 - 2.3388 1.00 2642 146 0.1738 0.2056
REMARK 3 6 2.3388 - 2.2010 1.00 2611 147 0.1657 0.1716
REMARK 3 7 2.2010 - 2.0908 1.00 2649 123 0.1564 0.1703
REMARK 3 8 2.0908 - 1.9998 1.00 2622 148 0.1515 0.2063
REMARK 3 9 1.9998 - 1.9228 1.00 2592 140 0.1451 0.1521
REMARK 3 10 1.9228 - 1.8565 1.00 2630 140 0.1443 0.1794
REMARK 3 11 1.8565 - 1.7985 1.00 2633 129 0.1522 0.1995
REMARK 3 12 1.7985 - 1.7471 1.00 2581 144 0.1553 0.2005
REMARK 3 13 1.7471 - 1.7011 1.00 2635 130 0.1493 0.2052
REMARK 3 14 1.7011 - 1.6596 1.00 2578 162 0.1511 0.1958
REMARK 3 15 1.6596 - 1.6218 1.00 2611 132 0.1504 0.1908
REMARK 3 16 1.6218 - 1.5873 1.00 2627 135 0.1475 0.1898
REMARK 3 17 1.5873 - 1.5556 1.00 2610 132 0.1524 0.2522
REMARK 3 18 1.5556 - 1.5262 1.00 2619 142 0.1484 0.2146
REMARK 3 19 1.5262 - 1.4990 1.00 2605 129 0.1503 0.1853
REMARK 3 20 1.4990 - 1.4736 1.00 2581 136 0.1489 0.1761
REMARK 3 21 1.4736 - 1.4498 1.00 2680 130 0.1549 0.2012
REMARK 3 22 1.4498 - 1.4275 1.00 2574 160 0.1623 0.2091
REMARK 3 23 1.4275 - 1.4065 1.00 2613 143 0.1662 0.2045
REMARK 3 24 1.4065 - 1.3867 1.00 2615 109 0.1667 0.2406
REMARK 3 25 1.3867 - 1.3700 0.96 2525 120 0.1849 0.2098
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2519
REMARK 3 ANGLE : 1.235 3462
REMARK 3 CHIRALITY : 0.080 408
REMARK 3 PLANARITY : 0.006 441
REMARK 3 DIHEDRAL : 12.369 833
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 4L6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB080235.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68886
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 50.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NH4AC, 0.1M ACETATE-BUFFER, 26%
REMARK 280 PEG4000, , PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.75250
REMARK 290 SMTRY3 2 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 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 68 CG CD CE NZ
REMARK 470 LYS A 149 CG CD CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 LYS A 243 CG CD CE NZ
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 OG SER A 120 O HOH A 806 2.13
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 129 -167.69 -79.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 758 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A 766 DISTANCE = 5.01 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3T7X RELATED DB: PDB
REMARK 900 RELATED ID: 4LAP RELATED DB: PDB
DBREF 4L6B A 1 330 UNP P11838 CARP_CRYPA 90 419
SEQRES 1 A 330 SER THR GLY SER ALA THR THR THR PRO ILE ASP SER LEU
SEQRES 2 A 330 ASP ASP ALA TYR ILE THR PRO VAL GLN ILE GLY THR PRO
SEQRES 3 A 330 ALA GLN THR LEU ASN LEU ASP PHE ASP THR GLY SER SER
SEQRES 4 A 330 ASP LEU TRP VAL PHE SER SER GLU THR THR ALA SER GLU
SEQRES 5 A 330 VAL ASP GLY GLN THR ILE TYR THR PRO SER LYS SER THR
SEQRES 6 A 330 THR ALA LYS LEU LEU SER GLY ALA THR TRP SER ILE SER
SEQRES 7 A 330 TYR GLY ASP GLY SER SER SER SER GLY ASP VAL TYR THR
SEQRES 8 A 330 ASP THR VAL SER VAL GLY GLY LEU THR VAL THR GLY GLN
SEQRES 9 A 330 ALA VAL GLU SER ALA LYS LYS VAL SER SER SER PHE THR
SEQRES 10 A 330 GLU ASP SER THR ILE ASP GLY LEU LEU GLY LEU ALA PHE
SEQRES 11 A 330 SER THR LEU ASN THR VAL SER PRO THR GLN GLN LYS THR
SEQRES 12 A 330 PHE PHE ASP ASN ALA LYS ALA SER LEU ASP SER PRO VAL
SEQRES 13 A 330 PHE THR ALA ASP LEU GLY TYR HIS ALA PRO GLY THR TYR
SEQRES 14 A 330 ASN PHE GLY PHE ILE ASP THR THR ALA TYR THR GLY SER
SEQRES 15 A 330 ILE THR TYR THR ALA VAL SER THR LYS GLN GLY PHE TRP
SEQRES 16 A 330 GLU TRP THR SER THR GLY TYR ALA VAL GLY SER GLY THR
SEQRES 17 A 330 PHE LYS SER THR SER ILE ASP GLY ILE ALA ASP THR GLY
SEQRES 18 A 330 THR THR LEU LEU TYR LEU PRO ALA THR VAL VAL SER ALA
SEQRES 19 A 330 TYR TRP ALA GLN VAL SER GLY ALA LYS SER SER SER SER
SEQRES 20 A 330 VAL GLY GLY TYR VAL PHE PRO CYS SER ALA THR LEU PRO
SEQRES 21 A 330 SER PHE THR PHE GLY VAL GLY SER ALA ARG ILE VAL ILE
SEQRES 22 A 330 PRO GLY ASP TYR ILE ASP PHE GLY PRO ILE SER THR GLY
SEQRES 23 A 330 SER SER SER CYS PHE GLY GLY ILE GLN SER SER ALA GLY
SEQRES 24 A 330 ILE GLY ILE ASN ILE PHE GLY ASP VAL ALA LEU LYS ALA
SEQRES 25 A 330 ALA PHE VAL VAL PHE ASN GLY ALA THR THR PRO THR LEU
SEQRES 26 A 330 GLY PHE ALA SER LYS
HET DMS A 401 4
HET DMS A 402 4
HET 1VS A 403 32
HET GOL A 404 6
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 1VS N-ETHYL-2-({N-[2-(1H-INDOL-3-YL)ETHYL]GLYCYL}AMINO)-4-
HETNAM 2 1VS PHENYLTHIOPHENE-3-CARBOXAMIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 DMS 2(C2 H6 O S)
FORMUL 4 1VS C25 H26 N4 O2 S
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *324(H2 O)
HELIX 1 1 THR A 49 VAL A 53 5 5
HELIX 2 2 THR A 60 SER A 64 5 5
HELIX 3 3 SER A 113 ASP A 119 1 7
HELIX 4 4 PHE A 130 ASN A 134 5 5
HELIX 5 5 THR A 143 LYS A 149 1 7
HELIX 6 6 ALA A 150 LEU A 152 5 3
HELIX 7 7 PRO A 228 ALA A 237 1 10
HELIX 8 8 PRO A 274 TYR A 277 5 4
HELIX 9 9 GLY A 306 LYS A 311 1 6
SHEET 1 A 9 LYS A 68 SER A 78 0
SHEET 2 A 9 SER A 84 VAL A 96 -1 O SER A 85 N ILE A 77
SHEET 3 A 9 TYR A 17 ILE A 23 -1 N GLN A 22 O SER A 95
SHEET 4 A 9 GLY A 3 PRO A 9 -1 N THR A 8 O ILE A 18
SHEET 5 A 9 GLY A 167 PHE A 171 -1 O PHE A 171 N GLY A 3
SHEET 6 A 9 VAL A 156 ASP A 160 -1 N THR A 158 O ASN A 170
SHEET 7 A 9 PHE A 314 ASN A 318 -1 O PHE A 317 N PHE A 157
SHEET 8 A 9 THR A 324 ALA A 328 -1 O GLY A 326 N VAL A 316
SHEET 9 A 9 THR A 184 ALA A 187 -1 N THR A 184 O PHE A 327
SHEET 1 B13 LYS A 68 SER A 78 0
SHEET 2 B13 SER A 84 VAL A 96 -1 O SER A 85 N ILE A 77
SHEET 3 B13 LEU A 99 VAL A 112 -1 O VAL A 106 N TYR A 90
SHEET 4 B13 TRP A 42 VAL A 43 1 N VAL A 43 O ALA A 109
SHEET 5 B13 GLY A 124 GLY A 127 -1 O LEU A 125 N TRP A 42
SHEET 6 B13 GLN A 28 ASP A 35 1 N ASP A 35 O LEU A 126
SHEET 7 B13 TYR A 17 ILE A 23 -1 N VAL A 21 O LEU A 30
SHEET 8 B13 GLY A 3 PRO A 9 -1 N THR A 8 O ILE A 18
SHEET 9 B13 GLY A 167 PHE A 171 -1 O PHE A 171 N GLY A 3
SHEET 10 B13 VAL A 156 ASP A 160 -1 N THR A 158 O ASN A 170
SHEET 11 B13 PHE A 314 ASN A 318 -1 O PHE A 317 N PHE A 157
SHEET 12 B13 THR A 324 ALA A 328 -1 O GLY A 326 N VAL A 316
SHEET 13 B13 THR A 184 ALA A 187 -1 N THR A 184 O PHE A 327
SHEET 1 C 7 ALA A 269 ILE A 273 0
SHEET 2 C 7 PHE A 262 VAL A 266 -1 N PHE A 262 O ILE A 273
SHEET 3 C 7 GLU A 196 VAL A 204 -1 N ALA A 203 O THR A 263
SHEET 4 C 7 LYS A 210 ALA A 218 -1 O LYS A 210 N TYR A 202
SHEET 5 C 7 ASN A 303 PHE A 305 1 O PHE A 305 N ILE A 217
SHEET 6 C 7 LEU A 225 LEU A 227 -1 N TYR A 226 O ILE A 304
SHEET 7 C 7 ILE A 294 SER A 296 1 O GLN A 295 N LEU A 225
SHEET 1 D 4 LYS A 243 SER A 245 0
SHEET 2 D 4 GLY A 250 PRO A 254 -1 O GLY A 250 N SER A 245
SHEET 3 D 4 SER A 289 GLY A 292 -1 O CYS A 290 N PHE A 253
SHEET 4 D 4 ASP A 279 PRO A 282 -1 N GLY A 281 O PHE A 291
SSBOND 1 CYS A 255 CYS A 290 1555 1555 2.04
CISPEP 1 THR A 25 PRO A 26 0 -6.15
CISPEP 2 SER A 137 PRO A 138 0 5.97
SITE 1 AC1 6 ASP A 81 GLY A 221 THR A 222 THR A 223
SITE 2 AC1 6 1VS A 403 HOH A 512
SITE 1 AC2 6 GLY A 37 ILE A 77 SER A 78 PHE A 194
SITE 2 AC2 6 HOH A 535 HOH A 745
SITE 1 AC3 15 ASP A 33 ASP A 35 GLY A 37 TYR A 79
SITE 2 AC3 15 GLY A 80 ASP A 81 SER A 83 PHE A 116
SITE 3 AC3 15 ASP A 119 ILE A 217 ASP A 219 GLY A 221
SITE 4 AC3 15 THR A 222 DMS A 401 HOH A 546
SITE 1 AC4 7 VAL A 272 TYR A 277 ALA A 312 SER A 329
SITE 2 AC4 7 LYS A 330 HOH A 536 HOH A 688
CRYST1 45.420 73.505 52.996 90.00 109.83 90.00 P 1 21 1 2
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 0.022017 0.000000 0.007940 0.00000
SCALE2 0.000000 0.013605 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END