HEADER HYDROLASE 19-SEP-16 5LWU
TITLE STRUCTURE RESULTING FROM AN ENDOTHIAPEPSIN CRYSTAL SOAKED WITH A
TITLE 2 DIMERIC DERIVATIVE OF FRAGMENT 177
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHIAPEPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ASPARTATE PROTEASE;
COMPND 5 EC: 3.4.23.22
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA;
SOURCE 3 ORGANISM_COMMON: CHESTNUT BLIGHT FUNGUS;
SOURCE 4 ORGANISM_TAXID: 5116
KEYWDS FRAGMENT SCREENING, ASPARTIC PROTEASE, INHIBITION, REACTIVITY,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SCHIEBEL,A.HEINE,G.KLEBE
REVDAT 2 17-JAN-24 5LWU 1 REMARK
REVDAT 1 09-AUG-17 5LWU 0
JRNL AUTH J.CRAMER,J.SCHIEBEL,T.WULSDORF,K.GROHE,E.E.NAJBAUER,
JRNL AUTH 2 F.R.EHRMANN,N.RADEVA,N.ZITZER,U.LINNE,R.LINSER,A.HEINE,
JRNL AUTH 3 G.KLEBE
JRNL TITL A FALSE-POSITIVE SCREENING HIT IN FRAGMENT-BASED LEAD
JRNL TITL 2 DISCOVERY: WATCH OUT FOR THE RED HERRING.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 1908 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28097765
JRNL DOI 10.1002/ANIE.201609824
REMARK 2
REMARK 2 RESOLUTION. 1.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 128248
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.124
REMARK 3 R VALUE (WORKING SET) : 0.123
REMARK 3 FREE R VALUE : 0.143
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6413
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 39.7911 - 3.4464 1.00 4158 220 0.1495 0.1666
REMARK 3 2 3.4464 - 2.7357 1.00 4101 215 0.1284 0.1499
REMARK 3 3 2.7357 - 2.3900 1.00 4076 215 0.1209 0.1411
REMARK 3 4 2.3900 - 2.1715 1.00 4101 216 0.1099 0.1302
REMARK 3 5 2.1715 - 2.0158 1.00 4056 213 0.1023 0.1235
REMARK 3 6 2.0158 - 1.8970 1.00 4067 214 0.0980 0.1047
REMARK 3 7 1.8970 - 1.8020 1.00 4097 216 0.0967 0.1211
REMARK 3 8 1.8020 - 1.7235 1.00 4058 213 0.0974 0.1131
REMARK 3 9 1.7235 - 1.6572 1.00 4057 214 0.0936 0.1143
REMARK 3 10 1.6572 - 1.6000 1.00 4088 215 0.0905 0.1093
REMARK 3 11 1.6000 - 1.5500 1.00 4073 215 0.0871 0.1114
REMARK 3 12 1.5500 - 1.5057 1.00 4065 214 0.0889 0.1066
REMARK 3 13 1.5057 - 1.4660 1.00 4047 213 0.0914 0.1205
REMARK 3 14 1.4660 - 1.4303 1.00 4070 214 0.0955 0.1246
REMARK 3 15 1.4303 - 1.3977 1.00 4068 214 0.1023 0.1333
REMARK 3 16 1.3977 - 1.3680 1.00 4051 213 0.1072 0.1347
REMARK 3 17 1.3680 - 1.3406 1.00 4087 215 0.1211 0.1383
REMARK 3 18 1.3406 - 1.3153 1.00 4045 213 0.1250 0.1500
REMARK 3 19 1.3153 - 1.2918 1.00 4016 212 0.1362 0.1485
REMARK 3 20 1.2918 - 1.2699 1.00 4079 214 0.1407 0.1658
REMARK 3 21 1.2699 - 1.2495 1.00 4084 215 0.1491 0.1676
REMARK 3 22 1.2495 - 1.2302 1.00 4017 212 0.1499 0.1780
REMARK 3 23 1.2302 - 1.2121 1.00 4088 215 0.1515 0.1827
REMARK 3 24 1.2121 - 1.1951 1.00 4023 211 0.1615 0.1939
REMARK 3 25 1.1951 - 1.1789 1.00 4065 214 0.1660 0.1840
REMARK 3 26 1.1789 - 1.1636 1.00 4017 212 0.1713 0.1839
REMARK 3 27 1.1636 - 1.1491 1.00 4081 215 0.1798 0.1949
REMARK 3 28 1.1491 - 1.1352 0.99 4029 212 0.1846 0.1946
REMARK 3 29 1.1352 - 1.1220 1.00 4084 215 0.1944 0.2170
REMARK 3 30 1.1220 - 1.1094 0.96 3887 204 0.2084 0.2143
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) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.30
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 : 0.006 2638
REMARK 3 ANGLE : 0.968 3641
REMARK 3 CHIRALITY : 0.081 423
REMARK 3 PLANARITY : 0.007 476
REMARK 3 DIHEDRAL : 14.847 867
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 5LWU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-16
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 : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128260
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.109
REMARK 200 RESOLUTION RANGE LOW (A) : 42.629
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.712
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.62
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.340
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: 4Y5L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 0.1 M SODIUM
REMARK 280 ACETATE, 24-30% PEG 4000; CRYSTALS OBTAINED BY STREAK-SEEDING,
REMARK 280 PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 36.67000
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 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12880 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 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 63 CD CE NZ
REMARK 470 LYS A 68 CD CE NZ
REMARK 470 LYS A 110 CE NZ
REMARK 470 LYS A 111 CE NZ
REMARK 470 LYS A 142 CE NZ
REMARK 470 LYS A 149 CE NZ
REMARK 470 LYS A 191 CD CE NZ
REMARK 470 LYS A 243 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 HZ2 LYS A 311 O HOH A 501 1.48
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 320 172.13 -58.33
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 826 DISTANCE = 5.89 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 TFA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TFA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 408
DBREF 5LWU 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 TFA A 403 14
HET TFA A 404 7
HET GOL A 405 6
HET GOL A 406 6
HET ACT A 407 4
HET ACT A 408 4
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM TFA TRIFLUOROACETIC ACID
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 DMS 2(C2 H6 O S)
FORMUL 4 TFA 2(C2 H F3 O2)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 8 ACT 2(C2 H3 O2 1-)
FORMUL 10 HOH *326(H2 O)
HELIX 1 AA1 THR A 49 VAL A 53 5 5
HELIX 2 AA2 THR A 60 SER A 64 5 5
HELIX 3 AA3 SER A 113 GLU A 118 1 6
HELIX 4 AA4 PHE A 130 ASN A 134 5 5
HELIX 5 AA5 THR A 143 LYS A 149 1 7
HELIX 6 AA6 ALA A 150 LEU A 152 5 3
HELIX 7 AA7 PRO A 228 ALA A 237 1 10
HELIX 8 AA8 PRO A 274 TYR A 277 5 4
HELIX 9 AA9 GLY A 306 LYS A 311 1 6
SHEET 1 AA1 9 LYS A 68 SER A 78 0
SHEET 2 AA1 9 SER A 84 VAL A 96 -1 O VAL A 89 N LEU A 70
SHEET 3 AA1 9 TYR A 17 ILE A 23 -1 N GLN A 22 O SER A 95
SHEET 4 AA1 9 GLY A 3 PRO A 9 -1 N THR A 8 O ILE A 18
SHEET 5 AA1 9 GLY A 167 PHE A 171 -1 O PHE A 171 N GLY A 3
SHEET 6 AA1 9 VAL A 156 ASP A 160 -1 N THR A 158 O ASN A 170
SHEET 7 AA1 9 PHE A 314 ASN A 318 -1 O PHE A 317 N PHE A 157
SHEET 8 AA1 9 THR A 324 ALA A 328 -1 O GLY A 326 N VAL A 316
SHEET 9 AA1 9 THR A 184 ALA A 187 -1 N THR A 186 O LEU A 325
SHEET 1 AA213 LYS A 68 SER A 78 0
SHEET 2 AA213 SER A 84 VAL A 96 -1 O VAL A 89 N LEU A 70
SHEET 3 AA213 LEU A 99 VAL A 112 -1 O VAL A 106 N TYR A 90
SHEET 4 AA213 LEU A 41 VAL A 43 1 N LEU A 41 O GLU A 107
SHEET 5 AA213 GLY A 124 GLY A 127 -1 O LEU A 125 N TRP A 42
SHEET 6 AA213 GLN A 28 ASP A 35 1 N ASP A 35 O LEU A 126
SHEET 7 AA213 TYR A 17 ILE A 23 -1 N VAL A 21 O LEU A 30
SHEET 8 AA213 GLY A 3 PRO A 9 -1 N THR A 8 O ILE A 18
SHEET 9 AA213 GLY A 167 PHE A 171 -1 O PHE A 171 N GLY A 3
SHEET 10 AA213 VAL A 156 ASP A 160 -1 N THR A 158 O ASN A 170
SHEET 11 AA213 PHE A 314 ASN A 318 -1 O PHE A 317 N PHE A 157
SHEET 12 AA213 THR A 324 ALA A 328 -1 O GLY A 326 N VAL A 316
SHEET 13 AA213 THR A 184 ALA A 187 -1 N THR A 186 O LEU A 325
SHEET 1 AA3 7 ALA A 269 ILE A 273 0
SHEET 2 AA3 7 PHE A 262 VAL A 266 -1 N PHE A 262 O ILE A 273
SHEET 3 AA3 7 GLU A 196 VAL A 204 -1 N ALA A 203 O THR A 263
SHEET 4 AA3 7 LYS A 210 ALA A 218 -1 O LYS A 210 N TYR A 202
SHEET 5 AA3 7 ASN A 303 PHE A 305 1 O PHE A 305 N ILE A 217
SHEET 6 AA3 7 LEU A 225 LEU A 227 -1 N TYR A 226 O ILE A 304
SHEET 7 AA3 7 ILE A 294 SER A 296 1 O GLN A 295 N LEU A 225
SHEET 1 AA4 4 LYS A 243 SER A 245 0
SHEET 2 AA4 4 GLY A 250 PRO A 254 -1 O GLY A 250 N SER A 245
SHEET 3 AA4 4 SER A 289 GLY A 292 -1 O CYS A 290 N PHE A 253
SHEET 4 AA4 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 2.05
CISPEP 1 THR A 25 PRO A 26 0 -10.18
CISPEP 2 SER A 137 PRO A 138 0 6.15
SITE 1 AC1 4 SER A 233 ALA A 237 HOH A 508 HOH A 716
SITE 1 AC2 2 PRO A 26 ALA A 27
SITE 1 AC3 10 GLY A 241 LYS A 243 VAL A 252 PHE A 253
SITE 2 AC3 10 PRO A 254 SER A 288 SER A 289 HOH A 526
SITE 3 AC3 10 HOH A 546 HOH A 674
SITE 1 AC4 8 PHE A 130 SER A 131 PHE A 145 ASP A 146
SITE 2 AC4 8 LYS A 149 HOH A 537 HOH A 654 HOH A 710
SITE 1 AC5 6 VAL A 272 TYR A 277 ALA A 312 SER A 329
SITE 2 AC5 6 LYS A 330 HOH A 606
SITE 1 AC6 7 TYR A 202 ALA A 203 VAL A 204 GLY A 207
SITE 2 AC6 7 THR A 208 LYS A 210 HOH A 502
SITE 1 AC7 8 CYS A 255 ASP A 279 GLY A 281 PRO A 282
SITE 2 AC7 8 CYS A 290 HOH A 503 HOH A 507 HOH A 801
SITE 1 AC8 3 GLY A 167 THR A 168 HOH A 513
CRYST1 45.325 73.340 53.063 90.00 109.86 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 0.022063 0.000000 0.007970 0.00000
SCALE2 0.000000 0.013635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
