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HEADER HYDROLASE 17-FEB-23 8CLP
TITLE ZEARALENONE LACTONASE FROM STREPTOMYCES COELICOFLAVUS MUTANT H286Y
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOFLAVUS;
SOURCE 3 ORGANISM_TAXID: 285562;
SOURCE 4 GENE: SMCF_1294;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ZEARALENONE, MYCOTOXIN, LACTONASE, CARBOXYLESTERASE, ESTERASE,
KEYWDS 2 HYDROLASE, BIODEGRADATION, STREPTOMYCES COELICOFLAVUS
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PUEHRINGER,G.MLYNEK
REVDAT 1 21-FEB-24 8CLP 0
JRNL AUTH S.FRUHAUF,D.PUEHRINGER,M.THAMHESL,P.FAJTL,E.KUNZ-VEKIRO,
JRNL AUTH 2 A.HOEBARTNER-GUSSL,J.PANHOELZL,K.PREM,V.KLINGENBRUNNER,
JRNL AUTH 3 G.SCHATZMAYR,G.ADAM,J.DAMBORSKY,K.DJINOVIC-CARUGO,Z.PROKOP,
JRNL AUTH 4 W.D.MOLL
JRNL TITL BACTERIAL LACTONASES ZENA WITH NONCANONICAL STRUCTURAL
JRNL TITL 2 FEATURES HYDROLYSE THE MYCOTOXIN ZEARALENONE
JRNL REF ACS CATALYSIS 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C00271
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4489
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 76512
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 42.5700 - 4.6300 0.92 5372 140 0.2060 0.2445
REMARK 3 2 4.6300 - 3.6700 0.92 5190 143 0.1481 0.2078
REMARK 3 3 3.6700 - 3.2100 0.94 5287 138 0.1587 0.1936
REMARK 3 4 3.2100 - 2.9200 0.96 5353 142 0.1744 0.2519
REMARK 3 5 2.9100 - 2.7100 0.96 5352 141 0.1830 0.2413
REMARK 3 6 2.7100 - 2.5500 0.97 5319 146 0.1956 0.2465
REMARK 3 7 2.5500 - 2.4200 0.96 5335 140 0.1959 0.2468
REMARK 3 8 2.4200 - 2.3100 0.98 5391 149 0.2110 0.2881
REMARK 3 9 2.3100 - 2.2200 0.97 5347 144 0.2245 0.2568
REMARK 3 10 2.2200 - 2.1500 0.98 5364 143 0.2411 0.3264
REMARK 3 11 2.1500 - 2.0800 0.98 5344 134 0.2526 0.2928
REMARK 3 12 2.0800 - 2.0200 0.97 5362 151 0.2755 0.3417
REMARK 3 13 2.0200 - 1.9700 0.97 5272 145 0.2913 0.3546
REMARK 3 14 1.9700 - 1.9200 0.95 5232 136 0.2998 0.3165
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.880
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 : 0.002 9342
REMARK 3 ANGLE : 0.506 12739
REMARK 3 CHIRALITY : 0.040 1336
REMARK 3 PLANARITY : 0.008 1681
REMARK 3 DIHEDRAL : 4.980 1280
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 8CLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1292126824.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76545
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 42.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.10960
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.76600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MG FORMATE DIHYDRATE, 15% PEG
REMARK 280 3350 (PH 6.9), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 31.78450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.35350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.06400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.35350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.78450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.06400
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 VAL A 2
REMARK 465 THR A 3
REMARK 465 ALA A 188
REMARK 465 SER A 189
REMARK 465 PRO A 190
REMARK 465 MET A 191
REMARK 465 ALA A 192
REMARK 465 ARG A 193
REMARK 465 SER A 194
REMARK 465 PHE A 195
REMARK 465 ALA A 306
REMARK 465 LEU A 307
REMARK 465 ALA A 308
REMARK 465 PRO A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 PRO B 5
REMARK 465 ALA B 6
REMARK 465 LEU B 7
REMARK 465 ARG B 8
REMARK 465 ASP B 9
REMARK 465 VAL B 10
REMARK 465 HIS B 11
REMARK 465 PHE B 195
REMARK 465 VAL B 196
REMARK 465 ALA B 197
REMARK 465 ASP B 198
REMARK 465 GLY B 199
REMARK 465 PRO B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 PRO C 5
REMARK 465 ALA C 6
REMARK 465 LEU C 7
REMARK 465 ARG C 8
REMARK 465 ASP C 9
REMARK 465 GLY C 185
REMARK 465 ALA C 186
REMARK 465 SER C 187
REMARK 465 ALA C 188
REMARK 465 SER C 189
REMARK 465 PRO C 190
REMARK 465 MET C 191
REMARK 465 ALA C 192
REMARK 465 ARG C 193
REMARK 465 SER C 194
REMARK 465 PHE C 195
REMARK 465 VAL C 196
REMARK 465 ALA C 197
REMARK 465 ASP C 198
REMARK 465 ALA C 308
REMARK 465 PRO C 309
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 HIS C 312
REMARK 465 HIS C 313
REMARK 465 HIS C 314
REMARK 465 HIS C 315
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 GLY D 185
REMARK 465 ALA D 186
REMARK 465 SER D 187
REMARK 465 ALA D 188
REMARK 465 SER D 189
REMARK 465 PRO D 190
REMARK 465 MET D 191
REMARK 465 ALA D 192
REMARK 465 ARG D 193
REMARK 465 SER D 194
REMARK 465 PHE D 195
REMARK 465 VAL D 196
REMARK 465 ALA D 197
REMARK 465 ASP D 198
REMARK 465 ALA D 308
REMARK 465 PRO D 309
REMARK 465 HIS D 310
REMARK 465 HIS D 311
REMARK 465 HIS D 312
REMARK 465 HIS D 313
REMARK 465 HIS D 314
REMARK 465 HIS D 315
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 ASP A 9 73.19 -106.14
REMARK 500 VAL A 10 -11.00 -144.23
REMARK 500 THR A 48 -4.98 77.50
REMARK 500 SER A 112 -130.06 55.48
REMARK 500 PHE A 141 -44.51 70.63
REMARK 500 ALA A 197 22.15 -163.47
REMARK 500 ASP A 198 30.97 -170.66
REMARK 500 HIS A 242 -145.59 -94.05
REMARK 500 MET A 287 61.03 -105.18
REMARK 500 THR B 48 -8.58 75.05
REMARK 500 SER B 112 -120.97 56.67
REMARK 500 PHE B 141 -51.51 68.96
REMARK 500 HIS B 242 -153.52 -94.21
REMARK 500 MET B 287 75.43 -111.38
REMARK 500 LEU B 307 -74.57 -77.18
REMARK 500 SER C 112 -120.99 52.04
REMARK 500 PHE C 141 -50.40 73.98
REMARK 500 CYS C 224 65.43 -151.29
REMARK 500 HIS C 242 -149.24 -93.59
REMARK 500 MET C 287 74.10 -105.27
REMARK 500 THR D 48 -0.23 74.66
REMARK 500 VAL D 101 -63.15 -101.37
REMARK 500 SER D 112 -126.74 54.31
REMARK 500 PHE D 141 -48.95 71.27
REMARK 500 HIS D 242 -151.20 -83.86
REMARK 500 MET D 287 66.92 -112.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 193 0.08 SIDE CHAIN
REMARK 500 ARG C 38 0.10 SIDE CHAIN
REMARK 500 ARG C 104 0.09 SIDE CHAIN
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 D 570 DISTANCE = 6.89 ANGSTROMS
DBREF 8CLP A 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLP B 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLP C 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLP D 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
SEQADV 8CLP TYR A 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLP HIS A 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS A 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS A 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS A 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS A 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS A 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP TYR B 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLP HIS B 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS B 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS B 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS B 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS B 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS B 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP TYR C 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLP HIS C 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS C 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS C 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS C 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS C 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS C 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP TYR D 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLP HIS D 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS D 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS D 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS D 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS D 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLP HIS D 315 UNP H1Q8U7 EXPRESSION TAG
SEQRES 1 A 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 A 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 A 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 A 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 A 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 A 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 A 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 A 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 A 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 A 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 A 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 A 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 A 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 A 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 A 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 A 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 A 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 A 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 A 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 A 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 A 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 A 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 A 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 A 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 A 315 HIS HIS HIS
SEQRES 1 B 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 B 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 B 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 B 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 B 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 B 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 B 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 B 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 B 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 B 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 B 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 B 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 B 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 B 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 B 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 B 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 B 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 B 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 B 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 B 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 B 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 B 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 B 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 B 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 B 315 HIS HIS HIS
SEQRES 1 C 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 C 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 C 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 C 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 C 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 C 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 C 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 C 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 C 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 C 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 C 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 C 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 C 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 C 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 C 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 C 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 C 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 C 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 C 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 C 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 C 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 C 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 C 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 C 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 C 315 HIS HIS HIS
SEQRES 1 D 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 D 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 D 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 D 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 D 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 D 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 D 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 D 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 D 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 D 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 D 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 D 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 D 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 D 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 D 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 D 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 D 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 D 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 D 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 D 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 D 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 D 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 D 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 D 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 D 315 HIS HIS HIS
FORMUL 5 HOH *589(H2 O)
HELIX 1 AA1 SER A 50 SER A 53 5 4
HELIX 2 AA2 TYR A 54 SER A 62 1 9
HELIX 3 AA3 SER A 86 VAL A 101 1 16
HELIX 4 AA4 SER A 112 SER A 125 1 14
HELIX 5 AA5 SER A 152 GLY A 156 5 5
HELIX 6 AA6 ALA A 157 LEU A 168 1 12
HELIX 7 AA7 GLY A 169 SER A 173 5 5
HELIX 8 AA8 ASP A 176 GLY A 185 1 10
HELIX 9 AA9 PRO A 201 GLU A 206 1 6
HELIX 10 AB1 PRO A 209 GLU A 217 1 9
HELIX 11 AB2 PRO A 225 GLY A 231 1 7
HELIX 12 AB3 SER A 258 ALA A 272 1 15
HELIX 13 AB4 MET A 287 ALA A 292 1 6
HELIX 14 AB5 ALA A 292 ALA A 305 1 14
HELIX 15 AB6 SER B 50 SER B 53 5 4
HELIX 16 AB7 TYR B 54 SER B 62 1 9
HELIX 17 AB8 SER B 86 VAL B 101 1 16
HELIX 18 AB9 SER B 112 SER B 125 1 14
HELIX 19 AC1 SER B 152 GLY B 156 5 5
HELIX 20 AC2 ALA B 157 LEU B 168 1 12
HELIX 21 AC3 GLY B 169 SER B 173 5 5
HELIX 22 AC4 ASP B 176 ALA B 186 1 11
HELIX 23 AC5 SER B 189 SER B 194 1 6
HELIX 24 AC6 PRO B 201 GLU B 206 1 6
HELIX 25 AC7 PRO B 209 GLU B 217 1 9
HELIX 26 AC8 PRO B 225 GLY B 231 1 7
HELIX 27 AC9 SER B 258 ALA B 272 1 15
HELIX 28 AD1 MET B 287 ALA B 292 1 6
HELIX 29 AD2 ALA B 292 ALA B 305 1 14
HELIX 30 AD3 SER C 50 SER C 53 5 4
HELIX 31 AD4 TYR C 54 SER C 62 1 9
HELIX 32 AD5 SER C 86 VAL C 101 1 16
HELIX 33 AD6 SER C 112 SER C 125 1 14
HELIX 34 AD7 SER C 152 GLY C 156 5 5
HELIX 35 AD8 ALA C 157 LEU C 168 1 12
HELIX 36 AD9 GLY C 169 SER C 173 5 5
HELIX 37 AE1 ASP C 176 ALA C 184 1 9
HELIX 38 AE2 PRO C 201 GLU C 206 1 6
HELIX 39 AE3 PRO C 209 GLU C 217 1 9
HELIX 40 AE4 PRO C 225 GLY C 231 1 7
HELIX 41 AE5 SER C 258 GLY C 273 1 16
HELIX 42 AE6 MET C 287 ALA C 292 1 6
HELIX 43 AE7 ALA C 292 ALA C 306 1 15
HELIX 44 AE8 SER D 4 ARG D 8 5 5
HELIX 45 AE9 SER D 50 SER D 53 5 4
HELIX 46 AF1 TYR D 54 SER D 62 1 9
HELIX 47 AF2 SER D 86 VAL D 101 1 16
HELIX 48 AF3 SER D 112 SER D 125 1 14
HELIX 49 AF4 SER D 152 GLY D 156 5 5
HELIX 50 AF5 ALA D 157 LEU D 168 1 12
HELIX 51 AF6 GLY D 169 SER D 173 5 5
HELIX 52 AF7 ASP D 176 ALA D 184 1 9
HELIX 53 AF8 PRO D 201 GLU D 206 1 6
HELIX 54 AF9 PRO D 209 GLU D 217 1 9
HELIX 55 AG1 PRO D 225 GLY D 231 1 7
HELIX 56 AG2 SER D 258 GLY D 273 1 16
HELIX 57 AG3 MET D 287 ALA D 292 1 6
HELIX 58 AG4 ALA D 292 ALA D 306 1 15
SHEET 1 AA1 8 GLU A 18 ASP A 22 0
SHEET 2 AA1 8 THR A 27 ALA A 33 -1 O TYR A 30 N GLN A 19
SHEET 3 AA1 8 HIS A 66 VAL A 70 -1 O ALA A 69 N ALA A 31
SHEET 4 AA1 8 ALA A 40 ILE A 44 1 N LEU A 43 O TYR A 68
SHEET 5 AA1 8 VAL A 106 ASN A 111 1 O ALA A 109 N ILE A 44
SHEET 6 AA1 8 LEU A 130 GLU A 136 1 O LEU A 134 N VAL A 108
SHEET 7 AA1 8 VAL A 237 HIS A 241 1 O LEU A 238 N CYS A 135
SHEET 8 AA1 8 VAL A 276 SER A 280 1 O ASP A 277 N VAL A 237
SHEET 1 AA2 2 ARG A 244 ILE A 246 0
SHEET 2 AA2 2 LEU A 253 GLY A 255 -1 O LEU A 254 N GLY A 245
SHEET 1 AA3 8 GLU B 18 ASP B 22 0
SHEET 2 AA3 8 THR B 27 ALA B 33 -1 O TYR B 30 N GLN B 19
SHEET 3 AA3 8 HIS B 66 VAL B 70 -1 O ALA B 69 N ALA B 31
SHEET 4 AA3 8 ALA B 40 ILE B 44 1 N LEU B 43 O TYR B 68
SHEET 5 AA3 8 VAL B 106 ASN B 111 1 O ALA B 109 N ILE B 44
SHEET 6 AA3 8 LEU B 130 GLU B 136 1 O LEU B 134 N VAL B 108
SHEET 7 AA3 8 VAL B 237 HIS B 241 1 O LEU B 238 N CYS B 135
SHEET 8 AA3 8 VAL B 276 SER B 280 1 O ASP B 277 N LEU B 239
SHEET 1 AA4 2 ARG B 244 ILE B 246 0
SHEET 2 AA4 2 LEU B 253 GLY B 255 -1 O LEU B 254 N GLY B 245
SHEET 1 AA5 8 GLU C 18 ASP C 22 0
SHEET 2 AA5 8 THR C 27 ALA C 33 -1 O TYR C 30 N GLN C 19
SHEET 3 AA5 8 HIS C 66 VAL C 70 -1 O ALA C 69 N ALA C 31
SHEET 4 AA5 8 ALA C 40 ILE C 44 1 N LEU C 43 O TYR C 68
SHEET 5 AA5 8 VAL C 106 ASN C 111 1 O ALA C 109 N ILE C 44
SHEET 6 AA5 8 LEU C 130 GLU C 136 1 O GLU C 136 N GLY C 110
SHEET 7 AA5 8 VAL C 237 HIS C 241 1 O LEU C 238 N CYS C 135
SHEET 8 AA5 8 VAL C 276 SER C 280 1 O ASP C 277 N LEU C 239
SHEET 1 AA6 2 ARG C 244 ILE C 246 0
SHEET 2 AA6 2 LEU C 253 GLY C 255 -1 O LEU C 254 N GLY C 245
SHEET 1 AA7 8 GLU D 18 ASP D 22 0
SHEET 2 AA7 8 THR D 27 ALA D 33 -1 O TYR D 30 N GLN D 19
SHEET 3 AA7 8 HIS D 66 VAL D 70 -1 O VAL D 67 N ALA D 33
SHEET 4 AA7 8 ALA D 40 ILE D 44 1 N VAL D 41 O TYR D 68
SHEET 5 AA7 8 VAL D 106 ASN D 111 1 O ALA D 109 N LEU D 42
SHEET 6 AA7 8 LEU D 130 GLU D 136 1 O LEU D 134 N VAL D 108
SHEET 7 AA7 8 VAL D 237 HIS D 241 1 O LEU D 238 N CYS D 135
SHEET 8 AA7 8 VAL D 276 SER D 280 1 O ASP D 277 N LEU D 239
SHEET 1 AA8 2 ARG D 244 ILE D 246 0
SHEET 2 AA8 2 LEU D 253 GLY D 255 -1 O LEU D 254 N GLY D 245
CRYST1 63.569 126.128 128.707 90.00 90.00 90.00 P 21 21 21 16
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 0.015731 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007770 0.00000
TER 4443 ALA A 305
TER 8902 ALA B 308
TER 13244 LEU C 307
TER 17704 LEU D 307
MASTER 385 0 0 58 40 0 0 6 9651 4 0 100
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