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HEADER HYDROLASE 06-AUG-17 5Y51
TITLE CRYSTAL STRUCTURE OF PYTH_H230A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRETHROID HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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 08-AUG-18 5Y51 0
JRNL AUTH D.Q.XU,T.T.RAN,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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 74982
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.330
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 3779
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 19.8163 - 6.8090 0.90 2736 123 0.1699 0.1890
REMARK 3 2 6.8090 - 5.4413 0.92 2632 141 0.2105 0.2559
REMARK 3 3 5.4413 - 4.7644 0.93 2647 132 0.2063 0.3111
REMARK 3 4 4.7644 - 4.3338 0.93 2634 125 0.1962 0.2358
REMARK 3 5 4.3338 - 4.0259 0.94 2633 150 0.2093 0.2793
REMARK 3 6 4.0259 - 3.7903 0.93 2606 151 0.2847 0.3437
REMARK 3 7 3.7903 - 3.6017 0.94 2618 132 0.3023 0.3120
REMARK 3 8 3.6017 - 3.4457 0.95 2610 156 0.2740 0.3454
REMARK 3 9 3.4457 - 3.3137 0.94 2607 145 0.3119 0.3521
REMARK 3 10 3.3137 - 3.1999 0.95 2626 157 0.2871 0.3580
REMARK 3 11 3.1999 - 3.1002 0.95 2670 123 0.2956 0.3750
REMARK 3 12 3.1002 - 3.0119 0.95 2637 126 0.2999 0.3686
REMARK 3 13 3.0119 - 2.9329 0.95 2629 145 0.3057 0.3674
REMARK 3 14 2.9329 - 2.8615 0.95 2637 133 0.3066 0.3579
REMARK 3 15 2.8615 - 2.7966 0.96 2632 136 0.3290 0.4863
REMARK 3 16 2.7966 - 2.7373 0.96 2643 151 0.3237 0.3417
REMARK 3 17 2.7373 - 2.6827 0.96 2611 139 0.3256 0.4487
REMARK 3 18 2.6827 - 2.6322 0.94 2593 131 0.3885 0.4077
REMARK 3 19 2.6322 - 2.5853 0.96 2615 164 0.3178 0.3461
REMARK 3 20 2.5853 - 2.5415 0.96 2631 156 0.3142 0.3719
REMARK 3 21 2.5415 - 2.5006 0.96 2633 153 0.3044 0.3523
REMARK 3 22 2.5006 - 2.4622 0.96 2656 123 0.3054 0.3909
REMARK 3 23 2.4622 - 2.4261 0.97 2666 141 0.3182 0.3993
REMARK 3 24 2.4261 - 2.3919 0.96 2683 120 0.3361 0.4048
REMARK 3 25 2.3919 - 2.3597 0.96 2614 155 0.3448 0.4319
REMARK 3 26 2.3597 - 2.3291 0.97 2667 129 0.3521 0.4587
REMARK 3 27 2.3291 - 2.3000 0.97 2637 142 0.3543 0.4572
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.980
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 11678
REMARK 3 ANGLE : 1.145 15989
REMARK 3 CHIRALITY : 0.059 1801
REMARK 3 PLANARITY : 0.009 2129
REMARK 3 DIHEDRAL : 18.555 6995
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 5Y51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75180
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.900
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 (%): 47.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.5, 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 84.18750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 84.18750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.92900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 84.18750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 84.18750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.92900
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 84.18750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.18750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.92900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 84.18750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.18750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 61.92900
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 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 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 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 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 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 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 137
REMARK 465 GLY A 138
REMARK 465 GLY A 161
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 137
REMARK 465 GLY B 138
REMARK 465 GLY B 161
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 GLU C 162
REMARK 465 GLY C 163
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 GLY D 161
REMARK 465 GLU D 162
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 GLY E 161
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 GLU F 137
REMARK 465 GLY F 138
REMARK 465 GLY F 161
REMARK 465 GLU F 162
REMARK 465 GLY F 163
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 C 188 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 188 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 117 CG CD1 CD2
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 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 OE2 GLU E 149 NH2 ARG E 152 1.87
REMARK 500 OH TYR D 31 OD1 ASP D 249 2.09
REMARK 500 OH TYR E 31 OD1 ASP E 249 2.11
REMARK 500 O PRO E 121 NE2 GLN E 212 2.11
REMARK 500 NH1 ARG E 194 CE1 PHE E 217 2.13
REMARK 500 NE2 HIS F 41 OH TYR F 57 2.13
REMARK 500 O LEU A 49 NH1 ARG D 139 2.16
REMARK 500 OE1 GLU D 55 O HOH D 401 2.18
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 D 160 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 PRO F 134 C - N - CA ANGL. DEV. = 10.4 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 SER A 78 -111.21 42.56
REMARK 500 THR A 102 49.75 33.24
REMARK 500 SER A 229 -137.86 -100.45
REMARK 500 MET A 236 65.81 -150.09
REMARK 500 ALA A 250 81.22 -166.49
REMARK 500 SER B 78 -124.82 54.32
REMARK 500 THR B 102 45.63 32.27
REMARK 500 THR B 125 67.24 -112.15
REMARK 500 SER B 229 -138.79 -95.48
REMARK 500 MET B 236 68.98 -153.71
REMARK 500 ALA B 250 79.35 -161.01
REMARK 500 SER C 78 -122.70 52.70
REMARK 500 THR C 102 49.74 32.69
REMARK 500 ASP C 144 94.78 -69.36
REMARK 500 PRO C 160 105.45 -55.04
REMARK 500 PRO C 184 31.35 -94.55
REMARK 500 SER C 229 -150.48 -108.14
REMARK 500 MET C 236 65.07 -151.62
REMARK 500 ALA C 250 82.10 -159.53
REMARK 500 ASP D 53 -173.34 -170.13
REMARK 500 SER D 78 -130.49 50.75
REMARK 500 TYR D 100 71.45 -110.16
REMARK 500 THR D 102 48.63 33.51
REMARK 500 ASP D 136 65.22 63.58
REMARK 500 SER D 229 -153.01 -95.14
REMARK 500 ALA D 250 76.70 -174.16
REMARK 500 ALA E 12 133.06 -32.07
REMARK 500 PRO E 43 127.43 -33.59
REMARK 500 SER E 78 -120.95 54.75
REMARK 500 HIS E 91 49.15 -144.63
REMARK 500 THR E 102 59.83 33.02
REMARK 500 ASN E 122 74.02 42.86
REMARK 500 GLU E 168 -5.39 -55.45
REMARK 500 THR E 176 -9.08 -59.45
REMARK 500 LEU E 200 -31.87 -38.04
REMARK 500 PRO E 227 46.34 -80.49
REMARK 500 SER E 229 -140.06 -93.59
REMARK 500 TYR E 233 -9.36 -59.74
REMARK 500 ALA E 250 65.62 -158.94
REMARK 500 LEU F 13 12.78 59.31
REMARK 500 VAL F 52 -70.12 -80.59
REMARK 500 SER F 78 -116.14 60.27
REMARK 500 THR F 102 53.33 30.79
REMARK 500 PRO F 108 134.36 -39.78
REMARK 500 SER F 229 -135.64 -88.58
REMARK 500 ALA F 250 78.33 -167.07
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 E 404 DISTANCE = 7.59 ANGSTROMS
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 5Y51 A 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y51 B 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y51 C 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y51 D 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y51 E 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
DBREF 5Y51 F 1 280 UNP D0VUS3 D0VUS3_9SPHN 1 280
SEQADV 5Y51 ALA A 230 UNP D0VUS3 HIS 230 ENGINEERED MUTATION
SEQADV 5Y51 LEU A 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 GLU A 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS A 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS A 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS A 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS A 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS A 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS A 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 ALA B 230 UNP D0VUS3 HIS 230 ENGINEERED MUTATION
SEQADV 5Y51 LEU B 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 GLU B 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS B 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS B 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS B 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS B 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS B 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS B 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 ALA C 230 UNP D0VUS3 HIS 230 ENGINEERED MUTATION
SEQADV 5Y51 LEU C 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 GLU C 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS C 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS C 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS C 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS C 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS C 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS C 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 ALA D 230 UNP D0VUS3 HIS 230 ENGINEERED MUTATION
SEQADV 5Y51 LEU D 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 GLU D 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS D 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS D 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS D 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS D 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS D 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS D 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 ALA E 230 UNP D0VUS3 HIS 230 ENGINEERED MUTATION
SEQADV 5Y51 LEU E 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 GLU E 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS E 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS E 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS E 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS E 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS E 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS E 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 ALA F 230 UNP D0VUS3 HIS 230 ENGINEERED MUTATION
SEQADV 5Y51 LEU F 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 GLU F 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS F 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS F 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS F 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS F 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 HIS F 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y51 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 SER
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 ALA 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 SER
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 ALA 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 SER
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 ALA 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 SER
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 ALA 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 SER
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 ALA 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 SER
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 ALA 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 *33(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 LEU A 79 HIS A 91 1 13
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 ARG A 147 MET A 156 1 10
HELIX 9 AA9 PRO A 166 PHE A 170 5 5
HELIX 10 AB1 THR A 176 THR A 181 1 6
HELIX 11 AB2 GLU A 186 ILE A 192 5 7
HELIX 12 AB3 PRO A 206 PHE A 217 1 12
HELIX 13 AB4 ALA A 231 MET A 236 1 6
HELIX 14 AB5 MET A 236 ALA A 250 1 15
HELIX 15 AB6 PRO A 251 TYR A 254 5 4
HELIX 16 AB7 ARG B 15 ASP B 20 5 6
HELIX 17 AB8 VAL B 22 ALA B 28 1 7
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 ALA B 66 1 9
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 MET B 156 1 10
HELIX 25 AC7 PRO B 166 PHE B 170 5 5
HELIX 26 AC8 VAL B 177 GLY B 180 5 4
HELIX 27 AC9 GLU B 186 ILE B 192 5 7
HELIX 28 AD1 PRO B 206 PHE B 217 1 12
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 PRO B 251 TYR B 254 5 4
HELIX 32 AD5 ARG C 15 ASP C 20 5 6
HELIX 33 AD6 VAL C 22 ALA C 28 1 7
HELIX 34 AD7 GLY C 46 VAL C 51 5 6
HELIX 35 AD8 ASP C 53 THR C 58 1 6
HELIX 36 AD9 THR C 58 ALA C 68 1 11
HELIX 37 AE1 LEU C 79 HIS C 91 1 13
HELIX 38 AE2 PRO C 112 LEU C 117 1 6
HELIX 39 AE3 THR C 125 LEU C 131 1 7
HELIX 40 AE4 ARG C 147 MET C 156 1 10
HELIX 41 AE5 PRO C 166 PHE C 170 5 5
HELIX 42 AE6 THR C 176 THR C 181 1 6
HELIX 43 AE7 GLU C 186 ILE C 192 5 7
HELIX 44 AE8 PRO C 206 PHE C 217 1 12
HELIX 45 AE9 ALA C 231 MET C 236 1 6
HELIX 46 AF1 MET C 236 ALA C 250 1 15
HELIX 47 AF2 PRO C 251 TYR C 254 5 4
HELIX 48 AF3 ARG D 15 ASP D 20 5 6
HELIX 49 AF4 VAL D 22 ARG D 29 1 8
HELIX 50 AF5 GLY D 47 VAL D 51 5 5
HELIX 51 AF6 ASP D 53 THR D 58 1 6
HELIX 52 AF7 THR D 58 ALA D 68 1 11
HELIX 53 AF8 LEU D 79 HIS D 91 1 13
HELIX 54 AF9 PRO D 112 LEU D 117 1 6
HELIX 55 AG1 THR D 125 LEU D 131 1 7
HELIX 56 AG2 ARG D 147 MET D 156 1 10
HELIX 57 AG3 PRO D 166 PHE D 170 5 5
HELIX 58 AG4 VAL D 177 GLY D 180 5 4
HELIX 59 AG5 GLU D 186 ILE D 192 5 7
HELIX 60 AG6 PRO D 206 PHE D 217 1 12
HELIX 61 AG7 ALA D 231 MET D 236 1 6
HELIX 62 AG8 MET D 236 ASP D 249 1 14
HELIX 63 AG9 ARG E 15 ASP E 20 5 6
HELIX 64 AH1 VAL E 22 ALA E 28 1 7
HELIX 65 AH2 GLY E 47 VAL E 51 5 5
HELIX 66 AH3 ASP E 53 THR E 58 1 6
HELIX 67 AH4 THR E 58 ARG E 67 1 10
HELIX 68 AH5 GLY E 80 HIS E 91 1 12
HELIX 69 AH6 PRO E 112 LEU E 117 1 6
HELIX 70 AH7 THR E 125 LEU E 131 1 7
HELIX 71 AH8 ARG E 147 PHE E 155 1 9
HELIX 72 AH9 PRO E 166 PHE E 170 5 5
HELIX 73 AI1 THR E 176 THR E 181 1 6
HELIX 74 AI2 GLU E 186 ILE E 192 5 7
HELIX 75 AI3 PRO E 206 LYS E 215 1 10
HELIX 76 AI4 ALA E 231 MET E 236 1 6
HELIX 77 AI5 MET E 236 ASP E 249 1 14
HELIX 78 AI6 ALA E 250 TYR E 254 5 5
HELIX 79 AI7 ARG F 15 ASP F 20 5 6
HELIX 80 AI8 VAL F 22 ALA F 28 1 7
HELIX 81 AI9 GLY F 47 VAL F 51 5 5
HELIX 82 AJ1 ASP F 53 ALA F 68 1 16
HELIX 83 AJ2 LEU F 79 HIS F 91 1 13
HELIX 84 AJ3 PRO F 112 LEU F 117 1 6
HELIX 85 AJ4 THR F 125 LEU F 131 1 7
HELIX 86 AJ5 ARG F 147 MET F 156 1 10
HELIX 87 AJ6 PRO F 166 PHE F 170 5 5
HELIX 88 AJ7 THR F 176 THR F 181 1 6
HELIX 89 AJ8 GLU F 186 LEU F 190 5 5
HELIX 90 AJ9 PRO F 206 GLU F 216 1 11
HELIX 91 AK1 ALA F 231 MET F 236 1 6
HELIX 92 AK2 MET F 236 ALA F 250 1 15
HELIX 93 AK3 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 GLN A 71 N THR A 4
SHEET 4 AA1 6 VAL A 95 LEU A 101 1 O ILE A 99 N LEU A 74
SHEET 5 AA1 6 ARG A 194 ALA A 199 1 O LEU A 195 N TYR A 100
SHEET 6 AA1 6 ALA A 222 LEU A 226 1 O LEU A 226 N GLU A 198
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 GLN A 174 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 ILE B 6 O HIS B 34
SHEET 3 AA3 6 GLN B 71 HIS B 77 1 O LEU B 75 N ILE B 7
SHEET 4 AA3 6 VAL B 95 LEU B 101 1 O ILE B 99 N GLY B 76
SHEET 5 AA3 6 ARG B 194 ALA B 199 1 O LEU B 195 N LEU B 98
SHEET 6 AA3 6 ALA B 222 LEU B 226 1 O LEU B 226 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 GLN B 174 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 LEU C 75 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 LEU C 226 N GLU C 198
SHEET 1 AA6 3 ILE C 132 VAL C 135 0
SHEET 2 AA6 3 GLY C 140 ALA C 143 -1 O GLY C 140 N VAL C 135
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 HIS D 77 1 O ILE D 73 N ILE D 7
SHEET 4 AA7 6 VAL D 95 LEU D 101 1 O ILE D 99 N GLY D 76
SHEET 5 AA7 6 ARG D 194 ALA D 199 1 O LEU D 195 N TYR D 100
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 ILE E 6 O ARG E 32
SHEET 3 AA9 6 GLN E 71 HIS E 77 1 O GLN E 71 N THR E 4
SHEET 4 AA9 6 VAL E 95 LEU E 101 1 O ILE E 99 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 GLY E 140 N VAL E 135
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 ILE F 9 1 N LEU F 8 O HIS F 34
SHEET 3 AB2 6 GLN F 71 HIS F 77 1 O GLN F 71 N THR F 4
SHEET 4 AB2 6 VAL F 95 LEU F 101 1 O LEU F 101 N GLY F 76
SHEET 5 AB2 6 ARG F 194 ALA F 199 1 O LEU F 195 N TYR F 100
SHEET 6 AB2 6 ALA F 222 LEU F 226 1 O ALA F 222 N TYR F 196
SHEET 1 AB3 3 ILE F 132 VAL F 135 0
SHEET 2 AB3 3 GLY F 140 ALA F 143 -1 O GLY F 140 N VAL F 135
SHEET 3 AB3 3 GLN F 174 SER F 175 -1 O GLN F 174 N LEU F 141
CISPEP 1 GLU A 120 PRO A 121 0 -3.64
CISPEP 2 GLU B 120 PRO B 121 0 -2.43
CISPEP 3 GLU C 120 PRO C 121 0 -6.37
CISPEP 4 GLU D 120 PRO D 121 0 2.52
CISPEP 5 GLU E 120 PRO E 121 0 -10.43
CISPEP 6 GLU F 120 PRO F 121 0 2.66
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 5 SER C 235 MET C 236 PRO C 237 GLU C 238
SITE 2 AC3 5 ARG C 239
SITE 1 AC4 5 SER D 235 MET D 236 PRO D 237 GLU D 238
SITE 2 AC4 5 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 168.375 168.375 123.858 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 0.005939 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008074 0.00000
TER 1889 TYR A 254
TER 3782 TYR B 254
TER 5682 TYR C 254
TER 7582 TYR D 254
TER 9468 TYR E 254
TER 11357 TYR F 254
MASTER 652 0 6 93 54 0 11 611414 6 30 138
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