| content |
HEADER HYDROLASE 09-AUG-17 5Y5V
TITLE CRYSTAL STRUCTURE OF A NOVEL PYRETHROID HYDROLASE PYTH (S78A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRETHROID HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM FANIAE;
SOURCE 3 ORGANISM_TAXID: 570446;
SOURCE 4 GENE: PYTH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.Q.XU,T.T.RAN,J.HE,W.W.WANG
REVDAT 1 15-AUG-18 5Y5V 0
JRNL AUTH D.Q.XU,Y.Y.GAO,T.T.RAN,L.P.ZENG,J.HE,W.W.WANG
JRNL TITL STRUCTURE AND CATALYTIC MECHANISM OF A NOVEL PYRETHROID
JRNL TITL 2 HYDROLASE FROM SPHINGOBIUM FANIAE JZ-2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2247: ???)
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) : 2.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 36595
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1756
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 19.8230 - 6.9143 1.00 2851 145 0.1903 0.2244
REMARK 3 2 6.9143 - 5.5272 1.00 2759 129 0.2137 0.2737
REMARK 3 3 5.5272 - 4.8402 1.00 2711 118 0.2011 0.2703
REMARK 3 4 4.8402 - 4.4029 1.00 2663 159 0.1787 0.2408
REMARK 3 5 4.4029 - 4.0903 1.00 2677 139 0.1802 0.2619
REMARK 3 6 4.0903 - 3.8510 1.00 2658 151 0.2003 0.2692
REMARK 3 7 3.8510 - 3.6594 1.00 2642 128 0.2172 0.3136
REMARK 3 8 3.6594 - 3.5010 1.00 2693 113 0.2243 0.3447
REMARK 3 9 3.5010 - 3.3669 1.00 2643 121 0.2438 0.3234
REMARK 3 10 3.3669 - 3.2513 1.00 2663 133 0.2516 0.3602
REMARK 3 11 3.2513 - 3.1500 1.00 2654 117 0.2614 0.3397
REMARK 3 12 3.1500 - 3.0603 1.00 2625 139 0.2801 0.3748
REMARK 3 13 3.0603 - 2.9800 1.00 2600 164 0.3098 0.4525
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) : 0.510
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.600
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 : 0.011 11517
REMARK 3 ANGLE : 1.199 15804
REMARK 3 CHIRALITY : 0.062 1792
REMARK 3 PLANARITY : 0.009 2110
REMARK 3 DIHEDRAL : 16.706 6840
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 5Y5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36638
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.980
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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 (%): 47.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.7, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 84.10000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 84.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.81300
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 84.10000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 84.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.81300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 84.10000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.10000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.81300
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 84.10000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.10000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 61.81300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10190 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 350
REMARK 350 BIOMOLECULE: 2
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: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 5
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 350
REMARK 350 BIOMOLECULE: 6
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 MET A 1
REMARK 465 GLU A 162
REMARK 465 GLY A 163
REMARK 465 ARG A 255
REMARK 465 GLN A 256
REMARK 465 THR A 257
REMARK 465 ALA A 258
REMARK 465 THR A 259
REMARK 465 LYS A 260
REMARK 465 ALA A 261
REMARK 465 GLY A 262
REMARK 465 PRO A 263
REMARK 465 ASP A 264
REMARK 465 ARG A 265
REMARK 465 PRO A 266
REMARK 465 ALA A 267
REMARK 465 GLY A 268
REMARK 465 ALA A 269
REMARK 465 ASP A 270
REMARK 465 GLY A 271
REMARK 465 GLY A 272
REMARK 465 ARG A 273
REMARK 465 ALA A 274
REMARK 465 ASP A 275
REMARK 465 ARG A 276
REMARK 465 ALA A 277
REMARK 465 ASP A 278
REMARK 465 LEU A 279
REMARK 465 PRO A 280
REMARK 465 LEU A 281
REMARK 465 GLU A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 MET B 1
REMARK 465 GLU B 162
REMARK 465 ARG B 255
REMARK 465 GLN B 256
REMARK 465 THR B 257
REMARK 465 ALA B 258
REMARK 465 THR B 259
REMARK 465 LYS B 260
REMARK 465 ALA B 261
REMARK 465 GLY B 262
REMARK 465 PRO B 263
REMARK 465 ASP B 264
REMARK 465 ARG B 265
REMARK 465 PRO B 266
REMARK 465 ALA B 267
REMARK 465 GLY B 268
REMARK 465 ALA B 269
REMARK 465 ASP B 270
REMARK 465 GLY B 271
REMARK 465 GLY B 272
REMARK 465 ARG B 273
REMARK 465 ALA B 274
REMARK 465 ASP B 275
REMARK 465 ARG B 276
REMARK 465 ALA B 277
REMARK 465 ASP B 278
REMARK 465 LEU B 279
REMARK 465 PRO B 280
REMARK 465 LEU B 281
REMARK 465 GLU B 282
REMARK 465 HIS B 283
REMARK 465 HIS B 284
REMARK 465 HIS B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 MET C 1
REMARK 465 GLY C 161
REMARK 465 GLU C 162
REMARK 465 ARG C 255
REMARK 465 GLN C 256
REMARK 465 THR C 257
REMARK 465 ALA C 258
REMARK 465 THR C 259
REMARK 465 LYS C 260
REMARK 465 ALA C 261
REMARK 465 GLY C 262
REMARK 465 PRO C 263
REMARK 465 ASP C 264
REMARK 465 ARG C 265
REMARK 465 PRO C 266
REMARK 465 ALA C 267
REMARK 465 GLY C 268
REMARK 465 ALA C 269
REMARK 465 ASP C 270
REMARK 465 GLY C 271
REMARK 465 GLY C 272
REMARK 465 ARG C 273
REMARK 465 ALA C 274
REMARK 465 ASP C 275
REMARK 465 ARG C 276
REMARK 465 ALA C 277
REMARK 465 ASP C 278
REMARK 465 LEU C 279
REMARK 465 PRO C 280
REMARK 465 LEU C 281
REMARK 465 GLU C 282
REMARK 465 HIS C 283
REMARK 465 HIS C 284
REMARK 465 HIS C 285
REMARK 465 HIS C 286
REMARK 465 HIS C 287
REMARK 465 HIS C 288
REMARK 465 MET D 1
REMARK 465 GLU D 162
REMARK 465 GLY D 163
REMARK 465 ARG D 255
REMARK 465 GLN D 256
REMARK 465 THR D 257
REMARK 465 ALA D 258
REMARK 465 THR D 259
REMARK 465 LYS D 260
REMARK 465 ALA D 261
REMARK 465 GLY D 262
REMARK 465 PRO D 263
REMARK 465 ASP D 264
REMARK 465 ARG D 265
REMARK 465 PRO D 266
REMARK 465 ALA D 267
REMARK 465 GLY D 268
REMARK 465 ALA D 269
REMARK 465 ASP D 270
REMARK 465 GLY D 271
REMARK 465 GLY D 272
REMARK 465 ARG D 273
REMARK 465 ALA D 274
REMARK 465 ASP D 275
REMARK 465 ARG D 276
REMARK 465 ALA D 277
REMARK 465 ASP D 278
REMARK 465 LEU D 279
REMARK 465 PRO D 280
REMARK 465 LEU D 281
REMARK 465 GLU D 282
REMARK 465 HIS D 283
REMARK 465 HIS D 284
REMARK 465 HIS D 285
REMARK 465 HIS D 286
REMARK 465 HIS D 287
REMARK 465 HIS D 288
REMARK 465 MET E 1
REMARK 465 GLU E 162
REMARK 465 GLY E 163
REMARK 465 ARG E 255
REMARK 465 GLN E 256
REMARK 465 THR E 257
REMARK 465 ALA E 258
REMARK 465 THR E 259
REMARK 465 LYS E 260
REMARK 465 ALA E 261
REMARK 465 GLY E 262
REMARK 465 PRO E 263
REMARK 465 ASP E 264
REMARK 465 ARG E 265
REMARK 465 PRO E 266
REMARK 465 ALA E 267
REMARK 465 GLY E 268
REMARK 465 ALA E 269
REMARK 465 ASP E 270
REMARK 465 GLY E 271
REMARK 465 GLY E 272
REMARK 465 ARG E 273
REMARK 465 ALA E 274
REMARK 465 ASP E 275
REMARK 465 ARG E 276
REMARK 465 ALA E 277
REMARK 465 ASP E 278
REMARK 465 LEU E 279
REMARK 465 PRO E 280
REMARK 465 LEU E 281
REMARK 465 GLU E 282
REMARK 465 HIS E 283
REMARK 465 HIS E 284
REMARK 465 HIS E 285
REMARK 465 HIS E 286
REMARK 465 HIS E 287
REMARK 465 HIS E 288
REMARK 465 MET F 1
REMARK 465 GLY F 161
REMARK 465 GLU F 162
REMARK 465 GLY F 187
REMARK 465 ARG F 188
REMARK 465 ARG F 255
REMARK 465 GLN F 256
REMARK 465 THR F 257
REMARK 465 ALA F 258
REMARK 465 THR F 259
REMARK 465 LYS F 260
REMARK 465 ALA F 261
REMARK 465 GLY F 262
REMARK 465 PRO F 263
REMARK 465 ASP F 264
REMARK 465 ARG F 265
REMARK 465 PRO F 266
REMARK 465 ALA F 267
REMARK 465 GLY F 268
REMARK 465 ALA F 269
REMARK 465 ASP F 270
REMARK 465 GLY F 271
REMARK 465 GLY F 272
REMARK 465 ARG F 273
REMARK 465 ALA F 274
REMARK 465 ASP F 275
REMARK 465 ARG F 276
REMARK 465 ALA F 277
REMARK 465 ASP F 278
REMARK 465 LEU F 279
REMARK 465 PRO F 280
REMARK 465 LEU F 281
REMARK 465 GLU F 282
REMARK 465 HIS F 283
REMARK 465 HIS F 284
REMARK 465 HIS F 285
REMARK 465 HIS F 286
REMARK 465 HIS F 287
REMARK 465 HIS F 288
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 ARG A 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 69 CG CD OE1 OE2
REMARK 470 GLU A 191 CG CD OE1 OE2
REMARK 470 GLU A 253 CG CD OE1 OE2
REMARK 470 ARG B 32 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 ARG B 139 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 29 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 32 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 63 CG OD1 OD2
REMARK 470 ARG C 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 69 CG CD OE1 OE2
REMARK 470 ARG D 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 191 CG CD OE1 OE2
REMARK 470 LYS D 215 CG CD CE NZ
REMARK 470 GLU D 253 CG CD OE1 OE2
REMARK 470 ARG E 32 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 59 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 65 CG CD1 CD2
REMARK 470 ARG E 67 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 84 CG1 CG2 CD1
REMARK 470 GLN E 89 CG CD OE1 NE2
REMARK 470 ASP E 93 CG OD1 OD2
REMARK 470 LEU E 98 CG CD1 CD2
REMARK 470 VAL E 110 CG1 CG2
REMARK 470 LEU E 117 CG CD1 CD2
REMARK 470 GLU E 120 CG CD OE1 OE2
REMARK 470 ARG E 139 CG CD NE CZ NH1 NH2
REMARK 470 THR E 181 OG1 CG2
REMARK 470 MET E 185 CG SD CE
REMARK 470 GLU E 186 CG CD OE1 OE2
REMARK 470 ARG E 188 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 190 CG CD1 CD2
REMARK 470 GLU E 191 CG CD OE1 OE2
REMARK 470 ILE E 192 CG1 CG2 CD1
REMARK 470 ARG E 194 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 215 CG CD CE NZ
REMARK 470 GLU E 242 CG CD OE1 OE2
REMARK 470 GLU E 253 CG CD OE1 OE2
REMARK 470 THR F 4 OG1 CG2
REMARK 470 ILE F 7 CG1 CG2 CD1
REMARK 470 ARG F 32 CG CD NE CZ NH1 NH2
REMARK 470 THR F 39 OG1 CG2
REMARK 470 ASP F 53 CG OD1 OD2
REMARK 470 GLU F 55 CG CD OE1 OE2
REMARK 470 ARG F 59 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 61 CG1 CG2
REMARK 470 ASP F 63 CG OD1 OD2
REMARK 470 ILE F 64 CG1 CG2 CD1
REMARK 470 LEU F 65 CG CD1 CD2
REMARK 470 ARG F 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 69 CG CD OE1 OE2
REMARK 470 GLN F 71 CG CD OE1 NE2
REMARK 470 SER F 72 OG
REMARK 470 LEU F 74 CG CD1 CD2
REMARK 470 TRP F 86 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP F 86 CZ3 CH2
REMARK 470 ASP F 93 CG OD1 OD2
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 GLU F 113 CG CD OE1 OE2
REMARK 470 LEU F 117 CG CD1 CD2
REMARK 470 ARG F 139 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 149 CG CD OE1 OE2
REMARK 470 MET F 185 CG SD CE
REMARK 470 LEU F 190 CG CD1 CD2
REMARK 470 GLU F 191 CG CD OE1 OE2
REMARK 470 ARG F 194 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 253 CG CD OE1 OE2
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 OD2 ASP F 158 O ALA F 231 1.84
REMARK 500 NE ARG F 15 OD2 ASP F 37 1.87
REMARK 500 NH2 ARG D 123 OE1 GLU D 216 1.88
REMARK 500 OH TYR F 31 OD1 ASP F 249 1.95
REMARK 500 NH1 ARG B 123 OE2 GLU B 216 1.98
REMARK 500 OD1 ASP F 158 OG SER F 229 2.03
REMARK 500 OG1 THR E 102 OD2 ASP E 202 2.04
REMARK 500 OD2 ASP E 130 NH2 ARG E 147 2.05
REMARK 500 O GLY E 81 OG SER E 85 2.07
REMARK 500 OD2 ASP F 158 C ALA F 231 2.10
REMARK 500 OG1 THR F 111 O PHE F 179 2.11
REMARK 500 OD1 ASP E 144 OG SER E 146 2.11
REMARK 500 NH2 ARG E 15 OD2 ASP E 37 2.15
REMARK 500 OD1 ASP A 144 OG SER A 146 2.16
REMARK 500 OD1 ASP D 158 OG SER D 229 2.16
REMARK 500 NE2 HIS F 41 OH TYR F 57 2.16
REMARK 500 O GLN A 172 O HOH A 401 2.19
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 OE2 GLU E 149 N MET F 164 8554 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 121 C - N - CD ANGL. DEV. = 16.8 DEGREES
REMARK 500 PRO D 121 C - N - CD ANGL. DEV. = 15.3 DEGREES
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 78 -129.64 40.08
REMARK 500 THR A 102 47.28 39.01
REMARK 500 ALA A 107 152.80 -49.07
REMARK 500 SER A 229 -154.76 -84.48
REMARK 500 MET A 236 64.55 -151.00
REMARK 500 ALA A 250 82.98 -154.88
REMARK 500 ALA B 78 -124.98 55.37
REMARK 500 PHE B 145 -0.15 -59.60
REMARK 500 ARG B 147 59.41 -114.70
REMARK 500 SER B 229 -155.49 -83.39
REMARK 500 ALA B 250 85.80 -168.29
REMARK 500 LEU C 13 -4.40 62.23
REMARK 500 ALA C 78 -128.66 50.30
REMARK 500 HIS C 91 45.06 -147.61
REMARK 500 ASP C 93 -0.87 -57.85
REMARK 500 GLU C 186 111.41 155.42
REMARK 500 LEU C 190 -3.13 -56.81
REMARK 500 SER C 229 -152.33 -106.74
REMARK 500 PRO D 43 140.23 -39.73
REMARK 500 ALA D 78 -127.55 54.21
REMARK 500 HIS D 91 46.09 -140.72
REMARK 500 VAL D 104 109.60 -58.52
REMARK 500 ASN D 122 61.90 35.52
REMARK 500 GLU D 186 146.86 -173.11
REMARK 500 SER D 229 -153.92 -90.91
REMARK 500 MET D 236 60.47 -116.82
REMARK 500 ALA D 250 85.10 -172.08
REMARK 500 LEU E 13 9.97 51.73
REMARK 500 ASP E 53 -167.49 -166.23
REMARK 500 ALA E 78 -123.39 62.27
REMARK 500 HIS E 91 50.55 -146.98
REMARK 500 GLU E 168 -8.61 -52.48
REMARK 500 PRO E 182 168.09 -49.65
REMARK 500 SER E 229 -153.60 -86.05
REMARK 500 ALA E 250 59.99 -151.21
REMARK 500 LEU F 13 9.08 53.50
REMARK 500 CYS F 18 9.86 -65.84
REMARK 500 VAL F 52 -70.48 -108.46
REMARK 500 ALA F 78 -128.31 55.01
REMARK 500 THR F 102 59.64 37.01
REMARK 500 ALA F 107 -172.44 -69.42
REMARK 500 ASN F 122 74.66 47.62
REMARK 500 ALA F 128 -70.39 -60.41
REMARK 500 PRO F 165 -173.78 -63.56
REMARK 500 PHE F 217 132.61 -177.43
REMARK 500 SER F 229 -154.35 -90.45
REMARK 500 ALA F 231 71.00 -108.66
REMARK 500 MET F 236 57.46 -140.68
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 301
DBREF 5Y5V A 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y5V B 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y5V C 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y5V D 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y5V E 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y5V F 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
SEQADV 5Y5V ALA A 78 UNP D0VUS3 SER 78 ENGINEERED MUTATION
SEQADV 5Y5V LEU A 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V GLU A 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS A 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS A 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS A 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS A 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS A 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS A 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V ALA B 78 UNP D0VUS3 SER 78 ENGINEERED MUTATION
SEQADV 5Y5V LEU B 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V GLU B 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS B 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS B 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS B 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS B 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS B 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS B 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V ALA C 78 UNP D0VUS3 SER 78 ENGINEERED MUTATION
SEQADV 5Y5V LEU C 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V GLU C 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS C 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS C 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS C 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS C 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS C 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS C 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V ALA D 78 UNP D0VUS3 SER 78 ENGINEERED MUTATION
SEQADV 5Y5V LEU D 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V GLU D 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS D 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS D 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS D 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS D 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS D 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS D 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V ALA E 78 UNP D0VUS3 SER 78 ENGINEERED MUTATION
SEQADV 5Y5V LEU E 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V GLU E 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS E 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS E 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS E 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS E 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS E 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS E 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V ALA F 78 UNP D0VUS3 SER 78 ENGINEERED MUTATION
SEQADV 5Y5V LEU F 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V GLU F 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS F 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS F 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS F 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS F 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS F 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5V HIS F 288 UNP D0VUS3 EXPRESSION TAG
SEQRES 1 A 288 MET THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 A 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 A 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 A 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 A 288 ASP MET GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 A 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS ALA
SEQRES 7 A 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 A 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 A 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 A 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 A 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 A 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MET
SEQRES 13 A 288 GLY ASP TYR PRO GLY GLU GLY MET PRO PRO ALA GLU HIS
SEQRES 14 A 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 A 288 ASN PRO MET GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 A 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 A 288 VAL GLN ARG GLN MET GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 A 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 A 288 SER MET PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 A 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 A 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 A 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 A 288 HIS HIS
SEQRES 1 B 288 MET THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 B 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 B 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 B 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 B 288 ASP MET GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 B 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS ALA
SEQRES 7 B 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 B 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 B 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 B 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 B 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 B 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MET
SEQRES 13 B 288 GLY ASP TYR PRO GLY GLU GLY MET PRO PRO ALA GLU HIS
SEQRES 14 B 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 B 288 ASN PRO MET GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 B 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 B 288 VAL GLN ARG GLN MET GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 B 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 B 288 SER MET PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 B 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 B 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 B 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 B 288 HIS HIS
SEQRES 1 C 288 MET THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 C 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 C 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 C 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 C 288 ASP MET GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 C 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS ALA
SEQRES 7 C 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 C 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 C 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 C 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 C 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 C 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MET
SEQRES 13 C 288 GLY ASP TYR PRO GLY GLU GLY MET PRO PRO ALA GLU HIS
SEQRES 14 C 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 C 288 ASN PRO MET GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 C 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 C 288 VAL GLN ARG GLN MET GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 C 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 C 288 SER MET PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 C 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 C 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 C 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 C 288 HIS HIS
SEQRES 1 D 288 MET THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 D 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 D 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 D 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 D 288 ASP MET GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 D 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS ALA
SEQRES 7 D 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 D 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 D 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 D 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 D 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 D 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MET
SEQRES 13 D 288 GLY ASP TYR PRO GLY GLU GLY MET PRO PRO ALA GLU HIS
SEQRES 14 D 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 D 288 ASN PRO MET GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 D 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 D 288 VAL GLN ARG GLN MET GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 D 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 D 288 SER MET PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 D 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 D 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 D 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 D 288 HIS HIS
SEQRES 1 E 288 MET THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 E 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 E 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 E 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 E 288 ASP MET GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 E 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS ALA
SEQRES 7 E 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 E 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 E 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 E 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 E 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 E 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MET
SEQRES 13 E 288 GLY ASP TYR PRO GLY GLU GLY MET PRO PRO ALA GLU HIS
SEQRES 14 E 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 E 288 ASN PRO MET GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 E 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 E 288 VAL GLN ARG GLN MET GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 E 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 E 288 SER MET PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 E 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 E 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 E 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 E 288 HIS HIS
SEQRES 1 F 288 MET THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 F 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 F 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 F 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 F 288 ASP MET GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 F 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS ALA
SEQRES 7 F 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 F 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 F 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 F 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 F 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 F 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MET
SEQRES 13 F 288 GLY ASP TYR PRO GLY GLU GLY MET PRO PRO ALA GLU HIS
SEQRES 14 F 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 F 288 ASN PRO MET GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 F 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 F 288 VAL GLN ARG GLN MET GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 F 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 F 288 SER MET PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 F 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 F 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 F 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 F 288 HIS HIS
HET SO4 A 301 5
HET SO4 B 301 5
HET SO4 C 301 5
HET SO4 D 301 5
HET SO4 E 301 5
HET SO4 F 301 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 6(O4 S 2-)
FORMUL 13 HOH *43(H2 O)
HELIX 1 AA1 ARG A 15 ASP A 20 5 6
HELIX 2 AA2 VAL A 22 ARG A 29 1 8
HELIX 3 AA3 GLY A 47 VAL A 51 5 5
HELIX 4 AA4 ASP A 53 ALA A 68 1 16
HELIX 5 AA5 GLY A 80 HIS A 91 1 12
HELIX 6 AA6 PRO A 112 LEU A 117 1 6
HELIX 7 AA7 THR A 125 LEU A 131 1 7
HELIX 8 AA8 ASP A 136 GLY A 138 5 3
HELIX 9 AA9 ARG A 147 MET A 156 1 10
HELIX 10 AB1 PRO A 166 PHE A 170 5 5
HELIX 11 AB2 THR A 176 THR A 181 1 6
HELIX 12 AB3 GLY A 187 ILE A 192 1 6
HELIX 13 AB4 PRO A 206 PHE A 217 1 12
HELIX 14 AB5 ALA A 231 MET A 236 1 6
HELIX 15 AB6 MET A 236 ALA A 250 1 15
HELIX 16 AB7 ARG B 15 ASP B 20 5 6
HELIX 17 AB8 VAL B 22 ARG B 29 1 8
HELIX 18 AB9 GLY B 47 VAL B 51 5 5
HELIX 19 AC1 ASP B 53 THR B 58 1 6
HELIX 20 AC2 THR B 58 ARG B 67 1 10
HELIX 21 AC3 LEU B 79 HIS B 91 1 13
HELIX 22 AC4 PRO B 112 LEU B 117 1 6
HELIX 23 AC5 THR B 125 LEU B 131 1 7
HELIX 24 AC6 ARG B 147 GLY B 157 1 11
HELIX 25 AC7 PRO B 166 PHE B 170 5 5
HELIX 26 AC8 THR B 176 THR B 181 1 6
HELIX 27 AC9 ARG B 188 ILE B 192 5 5
HELIX 28 AD1 PRO B 206 GLU B 216 1 11
HELIX 29 AD2 ALA B 231 MET B 236 1 6
HELIX 30 AD3 MET B 236 ALA B 250 1 15
HELIX 31 AD4 ARG C 15 ASP C 20 5 6
HELIX 32 AD5 VAL C 22 ALA C 28 1 7
HELIX 33 AD6 ASP C 53 THR C 58 1 6
HELIX 34 AD7 THR C 58 ALA C 68 1 11
HELIX 35 AD8 LEU C 79 HIS C 91 1 13
HELIX 36 AD9 THR C 111 VAL C 116 5 6
HELIX 37 AE1 THR C 125 LEU C 131 1 7
HELIX 38 AE2 ARG C 147 MET C 156 1 10
HELIX 39 AE3 THR C 176 THR C 181 1 6
HELIX 40 AE4 ARG C 188 ILE C 192 5 5
HELIX 41 AE5 PRO C 206 GLU C 216 1 11
HELIX 42 AE6 ALA C 231 MET C 236 1 6
HELIX 43 AE7 MET C 236 ALA C 250 1 15
HELIX 44 AE8 ARG D 15 ASP D 20 5 6
HELIX 45 AE9 ALA D 21 ALA D 28 1 8
HELIX 46 AF1 GLY D 46 VAL D 51 1 6
HELIX 47 AF2 ASP D 53 THR D 58 1 6
HELIX 48 AF3 THR D 58 ALA D 68 1 11
HELIX 49 AF4 LEU D 79 HIS D 91 1 13
HELIX 50 AF5 PRO D 112 LEU D 117 1 6
HELIX 51 AF6 THR D 125 LEU D 131 1 7
HELIX 52 AF7 ARG D 147 MET D 156 1 10
HELIX 53 AF8 PRO D 166 PHE D 170 5 5
HELIX 54 AF9 THR D 176 THR D 181 1 6
HELIX 55 AG1 GLU D 186 ILE D 192 5 7
HELIX 56 AG2 PRO D 206 PHE D 217 1 12
HELIX 57 AG3 ALA D 231 MET D 236 1 6
HELIX 58 AG4 MET D 236 ALA D 250 1 15
HELIX 59 AG5 ARG E 15 ASP E 20 5 6
HELIX 60 AG6 VAL E 22 GLY E 30 1 9
HELIX 61 AG7 GLY E 47 VAL E 51 5 5
HELIX 62 AG8 ASP E 53 THR E 58 1 6
HELIX 63 AG9 THR E 58 ALA E 68 1 11
HELIX 64 AH1 LEU E 79 HIS E 91 1 13
HELIX 65 AH2 PRO E 112 LEU E 117 1 6
HELIX 66 AH3 THR E 125 LEU E 131 1 7
HELIX 67 AH4 ARG E 147 PHE E 155 1 9
HELIX 68 AH5 PRO E 166 PHE E 170 5 5
HELIX 69 AH6 THR E 176 THR E 181 1 6
HELIX 70 AH7 GLY E 187 ILE E 192 1 6
HELIX 71 AH8 PRO E 206 PHE E 217 1 12
HELIX 72 AH9 ALA E 231 MET E 236 1 6
HELIX 73 AI1 MET E 236 ALA E 250 1 15
HELIX 74 AI2 PRO E 251 TYR E 254 5 4
HELIX 75 AI3 ARG F 15 ASP F 20 5 6
HELIX 76 AI4 ALA F 21 ARG F 29 1 9
HELIX 77 AI5 ASP F 53 THR F 58 1 6
HELIX 78 AI6 THR F 58 ALA F 68 1 11
HELIX 79 AI7 LEU F 79 HIS F 91 1 13
HELIX 80 AI8 PRO F 112 LEU F 117 1 6
HELIX 81 AI9 THR F 125 ILE F 132 1 8
HELIX 82 AJ1 ARG F 147 GLY F 157 1 11
HELIX 83 AJ2 PRO F 166 PHE F 170 5 5
HELIX 84 AJ3 THR F 176 THR F 181 1 6
HELIX 85 AJ4 PRO F 206 GLU F 216 1 11
HELIX 86 AJ5 ALA F 231 MET F 236 1 6
HELIX 87 AJ6 MET F 236 ALA F 250 1 15
HELIX 88 AJ7 PRO F 251 TYR F 254 5 4
SHEET 1 AA1 6 ARG A 32 HIS A 34 0
SHEET 2 AA1 6 VAL A 3 ILE A 9 1 N LEU A 8 O HIS A 34
SHEET 3 AA1 6 GLN A 71 HIS A 77 1 O ILE A 73 N ILE A 7
SHEET 4 AA1 6 VAL A 95 LEU A 101 1 O ALA A 96 N SER A 72
SHEET 5 AA1 6 ARG A 194 ALA A 199 1 O LEU A 195 N LEU A 98
SHEET 6 AA1 6 ALA A 222 LEU A 226 1 O VAL A 224 N TYR A 196
SHEET 1 AA2 3 ILE A 132 VAL A 135 0
SHEET 2 AA2 3 GLY A 140 ALA A 143 -1 O GLN A 142 N GLN A 133
SHEET 3 AA2 3 THR A 173 SER A 175 -1 O GLN A 174 N LEU A 141
SHEET 1 AA3 6 ARG B 32 HIS B 34 0
SHEET 2 AA3 6 VAL B 3 ILE B 9 1 N LEU B 8 O HIS B 34
SHEET 3 AA3 6 GLN B 71 ALA B 78 1 O ILE B 73 N ILE B 7
SHEET 4 AA3 6 VAL B 95 ALA B 103 1 O ALA B 96 N SER B 72
SHEET 5 AA3 6 ARG B 194 ALA B 199 1 O LEU B 195 N TYR B 100
SHEET 6 AA3 6 ALA B 222 LEU B 226 1 O VAL B 224 N GLU B 198
SHEET 1 AA4 3 ILE B 132 VAL B 135 0
SHEET 2 AA4 3 GLY B 140 ALA B 143 -1 O GLN B 142 N GLN B 133
SHEET 3 AA4 3 THR B 173 SER B 175 -1 O GLN B 174 N LEU B 141
SHEET 1 AA5 6 ARG C 32 HIS C 34 0
SHEET 2 AA5 6 VAL C 3 ILE C 9 1 N LEU C 8 O HIS C 34
SHEET 3 AA5 6 GLN C 71 HIS C 77 1 O ILE C 73 N ILE C 7
SHEET 4 AA5 6 VAL C 95 LEU C 101 1 O ALA C 96 N SER C 72
SHEET 5 AA5 6 ARG C 194 ALA C 199 1 O LEU C 195 N TYR C 100
SHEET 6 AA5 6 ALA C 222 LEU C 226 1 O ALA C 222 N TYR C 196
SHEET 1 AA6 3 ILE C 132 VAL C 135 0
SHEET 2 AA6 3 GLY C 140 ALA C 143 -1 O GLN C 142 N GLN C 133
SHEET 3 AA6 3 GLN C 174 SER C 175 -1 O GLN C 174 N LEU C 141
SHEET 1 AA7 6 ARG D 32 HIS D 34 0
SHEET 2 AA7 6 VAL D 3 ILE D 9 1 N LEU D 8 O HIS D 34
SHEET 3 AA7 6 GLN D 71 ALA D 78 1 O ILE D 73 N ILE D 7
SHEET 4 AA7 6 VAL D 95 ALA D 103 1 O ALA D 96 N SER D 72
SHEET 5 AA7 6 ARG D 194 ALA D 199 1 O LEU D 195 N LEU D 98
SHEET 6 AA7 6 ALA D 222 LEU D 226 1 O ALA D 222 N TYR D 196
SHEET 1 AA8 3 ILE D 132 VAL D 135 0
SHEET 2 AA8 3 GLY D 140 ALA D 143 -1 O GLY D 140 N VAL D 135
SHEET 3 AA8 3 GLN D 174 SER D 175 -1 O GLN D 174 N LEU D 141
SHEET 1 AA9 6 ARG E 32 HIS E 34 0
SHEET 2 AA9 6 VAL E 3 ILE E 9 1 N LEU E 8 O HIS E 34
SHEET 3 AA9 6 GLN E 71 HIS E 77 1 O LEU E 75 N ILE E 9
SHEET 4 AA9 6 VAL E 95 LEU E 101 1 O LEU E 101 N GLY E 76
SHEET 5 AA9 6 ARG E 194 ALA E 199 1 O ILE E 197 N TYR E 100
SHEET 6 AA9 6 ALA E 222 LEU E 226 1 O ALA E 222 N TYR E 196
SHEET 1 AB1 3 ILE E 132 VAL E 135 0
SHEET 2 AB1 3 GLY E 140 ALA E 143 -1 O GLN E 142 N GLN E 133
SHEET 3 AB1 3 THR E 173 SER E 175 -1 O GLN E 174 N LEU E 141
SHEET 1 AB2 6 ARG F 32 HIS F 34 0
SHEET 2 AB2 6 VAL F 3 LEU F 8 1 N ILE F 6 O ARG F 32
SHEET 3 AB2 6 GLN F 71 ALA F 78 1 O ILE F 73 N ILE F 7
SHEET 4 AB2 6 VAL F 95 ALA F 103 1 O ILE F 99 N GLY F 76
SHEET 5 AB2 6 ARG F 194 ALA F 199 1 O ILE F 197 N TYR F 100
SHEET 6 AB2 6 ALA F 222 LEU F 226 1 O ALA F 222 N TYR F 196
LINK NH1 ARG A 123 OE1 GLU A 216 1555 1555 1.41
CISPEP 1 GLU A 120 PRO A 121 0 0.34
CISPEP 2 GLU B 120 PRO B 121 0 1.53
CISPEP 3 GLU C 120 PRO C 121 0 0.23
CISPEP 4 GLU D 120 PRO D 121 0 0.21
CISPEP 5 GLU E 120 PRO E 121 0 -7.39
CISPEP 6 GLU F 120 PRO F 121 0 6.79
SITE 1 AC1 5 SER A 235 MET A 236 PRO A 237 GLU A 238
SITE 2 AC1 5 ARG A 239
SITE 1 AC2 5 SER B 235 MET B 236 PRO B 237 GLU B 238
SITE 2 AC2 5 ARG B 239
SITE 1 AC3 6 SER C 235 MET C 236 PRO C 237 GLU C 238
SITE 2 AC3 6 ARG C 239 HOH C 405
SITE 1 AC4 4 SER D 235 MET D 236 GLU D 238 ARG D 239
SITE 1 AC5 5 SER E 235 MET E 236 PRO E 237 GLU E 238
SITE 2 AC5 5 ARG E 239
SITE 1 AC6 4 MET F 236 PRO F 237 GLU F 238 ARG F 239
CRYST1 168.200 168.200 123.626 90.00 90.00 90.00 P 42 21 2 48
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 0.005945 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008089 0.00000
TER 1892 TYR A 254
TER 3784 TYR B 254
TER 5669 TYR C 254
TER 7561 TYR D 254
TER 9379 TYR E 254
TER 11166 TYR F 254
MASTER 740 0 6 88 51 0 10 611233 6 32 138
END |