| content |
HEADER HYDROLASE 17-FEB-23 8CLO
TITLE ZEARALENONE LACTONASE FROM STREPTOMYCES COELICOFLAVUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: 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,I.GRISHKOVSKAYA,G.MLYNEK,J.KOSTAN
REVDAT 1 21-FEB-24 8CLO 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. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 148542
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.350
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 46.3100 - 3.3700 1.00 10702 146 0.1880 0.2008
REMARK 3 2 3.3700 - 2.6800 1.00 10556 144 0.1725 0.1709
REMARK 3 3 2.6800 - 2.3400 1.00 10528 144 0.1611 0.1909
REMARK 3 4 2.3400 - 2.1300 1.00 10489 143 0.1585 0.1893
REMARK 3 5 2.1300 - 1.9700 1.00 10463 143 0.1602 0.1845
REMARK 3 6 1.9700 - 1.8600 1.00 10501 143 0.1616 0.2221
REMARK 3 7 1.8600 - 1.7600 1.00 10492 144 0.1847 0.2712
REMARK 3 8 1.7600 - 1.6900 1.00 10462 142 0.2036 0.2857
REMARK 3 9 1.6900 - 1.6200 1.00 10472 143 0.2167 0.2561
REMARK 3 10 1.6200 - 1.5700 1.00 10436 142 0.2331 0.3027
REMARK 3 11 1.5700 - 1.5200 1.00 10475 143 0.2432 0.2977
REMARK 3 12 1.5200 - 1.4700 1.00 10370 142 0.2683 0.3167
REMARK 3 13 1.4700 - 1.4400 0.99 10354 142 0.2976 0.3412
REMARK 3 14 1.4400 - 1.4000 0.98 10242 139 0.3346 0.3752
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.26
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 : 0.009 5022
REMARK 3 ANGLE : 1.014 6839
REMARK 3 CHIRALITY : 0.078 722
REMARK 3 PLANARITY : 0.014 902
REMARK 3 DIHEDRAL : 6.164 710
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 8CLO 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_1292126823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148595
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 46.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11970
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 1.53400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CRANK2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE / MES PH 6.5, 0.06 M
REMARK 280 MGCL2, CACL2, 30% W/V {40% ETHYLENE GLYCOL, 20% PEG 8000}, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 86.77400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.64850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 86.77400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.64850
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 APPLY THE FOLLOWING TO CHAINS: A, 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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 551 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 643 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 540 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 634 LIES ON A SPECIAL POSITION.
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 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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 48 -2.97 74.98
REMARK 500 SER A 112 -123.02 60.65
REMARK 500 PHE A 141 -52.08 72.46
REMARK 500 HIS A 242 -146.38 -97.87
REMARK 500 MET A 287 68.81 -102.76
REMARK 500 MET A 287 69.22 -103.03
REMARK 500 THR B 48 -4.12 79.02
REMARK 500 SER B 112 -124.36 63.26
REMARK 500 PHE B 141 -51.86 69.89
REMARK 500 HIS B 242 -147.65 -96.50
REMARK 500 MET B 287 70.68 -102.43
REMARK 500 MET B 287 70.56 -102.28
REMARK 500 LEU B 307 -72.18 -73.08
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 A 104 0.14 SIDE CHAIN
REMARK 500 ARG B 104 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CLO A 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLO B 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
SEQADV 8CLO HIS A 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS A 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS A 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS A 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS A 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS A 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS B 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS B 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS B 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS B 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS B 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLO HIS B 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 HIS
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 HIS
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
HET EDO A 401 10
HET EDO A 402 10
HET EDO A 403 10
HET EDO A 404 10
HET EDO A 405 10
HET EDO A 406 10
HET EDO B 401 10
HET EDO B 402 10
HET EDO B 403 10
HET EDO B 404 10
HET EDO B 405 10
HET EDO B 406 10
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 12(C2 H6 O2)
FORMUL 15 HOH *381(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 ALA A 186 1 11
HELIX 9 AA9 SER A 189 PHE A 195 1 7
HELIX 10 AB1 PRO A 201 GLU A 206 1 6
HELIX 11 AB2 PRO A 209 GLU A 217 1 9
HELIX 12 AB3 PRO A 225 GLY A 231 1 7
HELIX 13 AB4 SER A 258 ALA A 272 1 15
HELIX 14 AB5 MET A 287 ALA A 292 1 6
HELIX 15 AB6 ALA A 292 ALA A 305 1 14
HELIX 16 AB7 SER B 4 ARG B 8 5 5
HELIX 17 AB8 SER B 50 SER B 53 5 4
HELIX 18 AB9 TYR B 54 SER B 62 1 9
HELIX 19 AC1 SER B 86 VAL B 101 1 16
HELIX 20 AC2 SER B 112 SER B 125 1 14
HELIX 21 AC3 SER B 152 GLY B 156 5 5
HELIX 22 AC4 ALA B 157 LEU B 168 1 12
HELIX 23 AC5 GLY B 169 SER B 173 5 5
HELIX 24 AC6 ASP B 176 ALA B 186 1 11
HELIX 25 AC7 SER B 189 PHE B 195 1 7
HELIX 26 AC8 PRO B 201 GLU B 206 1 6
HELIX 27 AC9 PRO B 209 GLU B 217 1 9
HELIX 28 AD1 PRO B 225 GLY B 231 1 7
HELIX 29 AD2 SER B 258 GLY B 273 1 16
HELIX 30 AD3 MET B 287 ALA B 292 1 6
HELIX 31 AD4 ALA B 292 ALA B 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 VAL A 67 N ALA A 33
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 LEU A 42
SHEET 6 AA1 8 LEU A 130 GLU A 136 1 O GLU A 136 N GLY A 110
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 VAL B 67 N ALA B 33
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 LEU B 42
SHEET 6 AA3 8 LEU B 130 GLU B 136 1 O GLU B 136 N GLY B 110
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 VAL B 237
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
CRYST1 173.548 69.297 64.423 90.00 96.06 90.00 C 1 2 1 8
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 0.005762 0.000000 0.000612 0.00000
SCALE2 0.000000 0.014431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015610 0.00000
TER 4768 ALA A 308
TER 9500 ALA B 308
MASTER 284 0 12 31 20 0 0 6 5205 2 120 50
END |