HEADER HYDROLASE 28-JUN-16 5P3A
TITLE AUTOMATED REFINEMENT OF DIFFRACTION DATA OBTAINED FROM AN
TITLE 2 ENDOTHIAPEPSIN CRYSTAL TREATED WITH FRAGMENT 163
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHIAPEPSIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.23.22
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA;
SOURCE 3 ORGANISM_TAXID: 5116
KEYWDS FRAGMENT SCREENING, METHOD DEVELOPMENT, ASPARTIC PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SCHIEBEL,A.HEINE,G.KLEBE
REVDAT 5 17-NOV-21 5P3A 1 REMARK
REVDAT 4 21-FEB-18 5P3A 1 REMARK
REVDAT 3 11-JAN-17 5P3A 1 JRNL
REVDAT 2 10-AUG-16 5P3A 1 JRNL
REVDAT 1 03-AUG-16 5P3A 0
JRNL AUTH J.SCHIEBEL,S.G.KRIMMER,K.ROWER,A.KNORLEIN,X.WANG,A.Y.PARK,
JRNL AUTH 2 M.STIELER,F.R.EHRMANN,K.FU,N.RADEVA,M.KRUG,F.U.HUSCHMANN,
JRNL AUTH 3 S.GLOCKNER,M.S.WEISS,U.MUELLER,G.KLEBE,A.HEINE
JRNL TITL HIGH-THROUGHPUT CRYSTALLOGRAPHY: RELIABLE AND EFFICIENT
JRNL TITL 2 IDENTIFICATION OF FRAGMENT HITS.
JRNL REF STRUCTURE V. 24 1398 2016
JRNL REFN ISSN 1878-4186
JRNL PMID 27452405
JRNL DOI 10.1016/J.STR.2016.06.010
REMARK 2
REMARK 2 RESOLUTION. 1.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 102583
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5130
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 42.7764 - 3.6568 1.00 3483 184 0.1847 0.2062
REMARK 3 2 3.6568 - 2.9027 1.00 3417 180 0.1505 0.1663
REMARK 3 3 2.9027 - 2.5358 1.00 3405 179 0.1382 0.1260
REMARK 3 4 2.5358 - 2.3040 1.00 3432 180 0.1284 0.1325
REMARK 3 5 2.3040 - 2.1389 1.00 3411 180 0.1133 0.1385
REMARK 3 6 2.1389 - 2.0128 1.00 3403 179 0.1073 0.1377
REMARK 3 7 2.0128 - 1.9120 1.00 3404 179 0.1080 0.1226
REMARK 3 8 1.9120 - 1.8287 1.00 3399 179 0.1099 0.1340
REMARK 3 9 1.8287 - 1.7583 1.00 3390 179 0.1082 0.1364
REMARK 3 10 1.7583 - 1.6977 1.00 3400 179 0.1071 0.1209
REMARK 3 11 1.6977 - 1.6446 1.00 3393 178 0.1036 0.1420
REMARK 3 12 1.6446 - 1.5976 1.00 3374 178 0.1010 0.1256
REMARK 3 13 1.5976 - 1.5555 1.00 3379 178 0.1019 0.1306
REMARK 3 14 1.5555 - 1.5175 1.00 3418 179 0.1129 0.1524
REMARK 3 15 1.5175 - 1.4830 1.00 3405 180 0.1216 0.1596
REMARK 3 16 1.4830 - 1.4515 1.00 3352 176 0.1210 0.1276
REMARK 3 17 1.4515 - 1.4224 0.99 3379 178 0.1204 0.1503
REMARK 3 18 1.4224 - 1.3956 0.99 3369 177 0.1240 0.1460
REMARK 3 19 1.3956 - 1.3707 0.99 3333 176 0.1250 0.1405
REMARK 3 20 1.3707 - 1.3474 0.99 3399 179 0.1299 0.1486
REMARK 3 21 1.3474 - 1.3257 1.00 3372 177 0.1347 0.1741
REMARK 3 22 1.3257 - 1.3053 0.99 3386 178 0.1410 0.1446
REMARK 3 23 1.3053 - 1.2861 0.99 3358 177 0.1499 0.1759
REMARK 3 24 1.2861 - 1.2680 0.99 3321 175 0.1676 0.2068
REMARK 3 25 1.2680 - 1.2509 0.95 3241 170 0.1866 0.2550
REMARK 3 26 1.2509 - 1.2346 0.90 3062 162 0.2049 0.2071
REMARK 3 27 1.2346 - 1.2192 0.85 2878 151 0.2107 0.2002
REMARK 3 28 1.2192 - 1.2045 0.78 2633 139 0.2251 0.2424
REMARK 3 29 1.2045 - 1.1905 0.71 2391 125 0.2291 0.2620
REMARK 3 30 1.1905 - 1.1771 0.55 1866 99 0.2433 0.2395
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) : 13.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.80
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 2426
REMARK 3 ANGLE : 1.205 3329
REMARK 3 CHIRALITY : 0.072 399
REMARK 3 PLANARITY : 0.006 424
REMARK 3 DIHEDRAL : 10.773 783
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: ALL 364 STRUCTURES OF THIS SERIES WERE
REMARK 3 GENERATED BY AN AUTOMATED REFINEMENT PIPELINE AND, THUS, NOT
REMARK 3 REFINED TO FULL CONVERGENCE (E.G. SINCE NO MANUAL (RE-)BUILDING
REMARK 3 WAS PERFORMED, FRAGMENTS ARE MISSING IN THE STRUCTURAL MODEL
REMARK 3 EVEN WHEN PRESENT AS INDICATED BY THE ELECTRON DENSITY)
REMARK 4
REMARK 4 5P3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1001400163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-13
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 : 102585
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.180
REMARK 200 RESOLUTION RANGE LOW (A) : 42.748
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 3.512
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 4Y5L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.71
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; CRYSTAL OBTAINED BY STREAK-SEEDING AND
REMARK 280 SOAKED WITH 90 MM OF FRAGMENT 163 WITH THE SMILES CODE CN(CC(=O)
REMARK 280 NC1CC1)S(=O)(=O)C1=CC=C(BR)S1, PH 4.6, VAPOR DIFFUSION, SITTING
REMARK 280 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 36.69350
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 63 CE NZ
REMARK 470 LYS A 68 CD CE NZ
REMARK 470 LYS A 110 CE NZ
REMARK 470 LYS A 111 CD CE NZ
REMARK 470 LYS A 142 CE NZ
REMARK 470 LYS A 149 CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 LYS A 243 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 O HOH A 510 O HOH A 593 1.76
REMARK 500 O HOH A 520 O HOH A 595 1.87
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 599 O HOH A 600 2555 2.17
REMARK 500 O HOH A 569 O HOH A 596 1655 2.18
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 THR A 49 121.23 -38.85
REMARK 500 ALA A 129 -169.54 -79.13
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5OYQ 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
FORMUL 2 HOH *213(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 ASP A 119 1 7
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 GLY A 167 N THR A 7
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 184 O PHE A 327
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 33 O GLY A 124
SHEET 7 AA213 TYR A 17 ILE A 23 -1 N ILE A 23 O GLN A 28
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 GLY A 167 N THR A 7
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 184 O PHE A 327
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 VAL A 252 N LYS A 243
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 2.04
CISPEP 1 THR A 25 PRO A 26 0 -9.20
CISPEP 2 SER A 137 PRO A 138 0 6.19
CRYST1 45.271 73.387 52.723 90.00 109.22 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 0.022089 0.000000 0.007700 0.00000
SCALE2 0.000000 0.013626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020086 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
