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HEADER HYDROLASE 20-AUG-20 7CTR
TITLE CLOSED FORM OF PET-DEGRADING CUTINASE CUT190 WITH THERMOSTABILITY-
TITLE 2 IMPROVING MUTATIONS OF S226P/R228S/Q138A/D250C-E296C/Q123H/N202H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 GENE: CUT190, SAMN02982918_2340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80L
KEYWDS PROTEIN ENGINEERING, POLYESTERASE, DISULFIDE BOND, METAL BINDING,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.EMORI,N.NUMOTO,A.SENGA,G.J.BEKKER,N.KAMIYA,N.ITO,F.KAWAI,M.ODA
REVDAT 1 03-FEB-21 7CTR 0
JRNL AUTH M.EMORI,N.NUMOTO,A.SENGA,G.J.BEKKER,N.KAMIYA,Y.KOBAYASHI,
JRNL AUTH 2 N.ITO,F.KAWAI,M.ODA
JRNL TITL STRUCTURAL BASIS OF MUTANTS OF PET-DEGRADING ENZYME FROM
JRNL TITL 2 SACCHAROMONOSPORA VIRIDIS AHK190 WITH HIGH ACTIVITY AND
JRNL TITL 3 THERMAL STABILITY.
JRNL REF PROTEINS 2020
JRNL REFN ESSN 1097-0134
JRNL PMID 33340163
JRNL DOI 10.1002/PROT.26034
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 144092
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7199
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 42.7800 - 3.7300 0.99 5007 263 0.1754 0.1883
REMARK 3 2 3.7300 - 2.9600 0.99 4785 252 0.1650 0.1920
REMARK 3 3 2.9600 - 2.5800 0.99 4775 257 0.1761 0.1825
REMARK 3 4 2.5800 - 2.3500 0.99 4737 248 0.1727 0.2049
REMARK 3 5 2.3500 - 2.1800 0.98 4678 244 0.1609 0.1895
REMARK 3 6 2.1800 - 2.0500 0.98 4688 244 0.1554 0.1930
REMARK 3 7 2.0500 - 1.9500 0.98 4632 248 0.1492 0.1746
REMARK 3 8 1.9500 - 1.8600 0.97 4607 231 0.1484 0.1843
REMARK 3 9 1.8600 - 1.7900 0.98 4624 254 0.1548 0.1927
REMARK 3 10 1.7900 - 1.7300 0.97 4618 242 0.1551 0.1910
REMARK 3 11 1.7300 - 1.6800 0.97 4592 241 0.1470 0.1899
REMARK 3 12 1.6800 - 1.6300 0.97 4602 235 0.1439 0.1703
REMARK 3 13 1.6300 - 1.5900 0.97 4543 244 0.1452 0.1849
REMARK 3 14 1.5900 - 1.5500 0.97 4585 243 0.1483 0.2039
REMARK 3 15 1.5500 - 1.5100 0.97 4592 227 0.1604 0.2009
REMARK 3 16 1.5100 - 1.4800 0.97 4512 245 0.1655 0.2212
REMARK 3 17 1.4800 - 1.4500 0.96 4529 244 0.1825 0.2235
REMARK 3 18 1.4500 - 1.4200 0.96 4507 243 0.1915 0.2162
REMARK 3 19 1.4200 - 1.4000 0.96 4541 224 0.2132 0.2732
REMARK 3 20 1.4000 - 1.3700 0.96 4485 239 0.2243 0.3015
REMARK 3 21 1.3700 - 1.3500 0.96 4487 223 0.2427 0.2715
REMARK 3 22 1.3500 - 1.3300 0.95 4479 244 0.2485 0.2514
REMARK 3 23 1.3300 - 1.3100 0.96 4460 234 0.2516 0.2639
REMARK 3 24 1.3100 - 1.2900 0.95 4494 224 0.2639 0.2933
REMARK 3 25 1.2900 - 1.2800 0.95 4405 239 0.2783 0.2975
REMARK 3 26 1.2800 - 1.2600 0.95 4442 239 0.2872 0.3058
REMARK 3 27 1.2600 - 1.2400 0.94 4431 227 0.3047 0.3064
REMARK 3 28 1.2400 - 1.2300 0.94 4424 242 0.3126 0.3136
REMARK 3 29 1.2300 - 1.2100 0.95 4431 231 0.3200 0.3644
REMARK 3 30 1.2100 - 1.2000 0.90 4201 228 0.3500 0.3729
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) : 0.137
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.63
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 : 0.005 4166
REMARK 3 ANGLE : 0.815 5674
REMARK 3 CHIRALITY : 0.082 608
REMARK 3 PLANARITY : 0.006 742
REMARK 3 DIHEDRAL : 13.118 1552
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 7CTR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1300018231.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 144266
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17900
REMARK 200 FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.44000
REMARK 200 FOR SHELL : 1.200
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: 4WFI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 45% (V/V) 1,4-DIOXANE, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 34.06400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.77800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.84850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.77800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.06400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.84850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 GLY A 45
REMARK 465 LYS A 305
REMARK 465 LEU A 306
REMARK 465 ASN A 307
REMARK 465 GLY B 45
REMARK 465 LYS B 305
REMARK 465 LEU B 306
REMARK 465 ASN B 307
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 78 146.05 -170.16
REMARK 500 ALA A 108 142.61 -172.67
REMARK 500 SER A 176 -122.47 67.47
REMARK 500 THR A 199 60.04 31.71
REMARK 500 HIS A 230 -84.39 -120.28
REMARK 500 ALA B 78 145.21 -170.72
REMARK 500 ALA B 108 136.74 -173.10
REMARK 500 SER B 176 -122.56 65.71
REMARK 500 THR B 199 60.28 31.76
REMARK 500 HIS B 230 -84.06 -120.20
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 A 817 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B 817 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 818 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B 819 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B 820 DISTANCE = 7.95 ANGSTROMS
DBREF 7CTR A 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
DBREF 7CTR B 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
SEQADV 7CTR GLY A 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR PRO A 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR HIS A 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 7CTR ALA A 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 7CTR HIS A 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 7CTR PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 7CTR SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 7CTR CYS A 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 7CTR CYS A 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 7CTR LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR GLY B 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR PRO B 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR HIS B 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 7CTR ALA B 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 7CTR HIS B 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 7CTR PRO B 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 7CTR SER B 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 7CTR CYS B 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 7CTR CYS B 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 7CTR LYS B 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR LEU B 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTR ASN B 307 UNP W0TJ64 EXPRESSION TAG
SEQRES 1 A 263 GLY PRO ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 263 ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER VAL ALA
SEQRES 3 A 263 THR GLU ARG VAL SER SER PHE ALA SER GLY PHE GLY GLY
SEQRES 4 A 263 GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU GLY THR
SEQRES 5 A 263 PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR ALA SER
SEQRES 6 A 263 GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL ALA SER
SEQRES 7 A 263 HIS GLY PHE ILE VAL PHE THR ILE ASP THR ASN THR ARG
SEQRES 8 A 263 LEU ASP ALA PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA
SEQRES 9 A 263 ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG LYS VAL
SEQRES 10 A 263 ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL MET GLY
SEQRES 11 A 263 HIS SER MET GLY GLY GLY GLY SER LEU GLU ALA THR VAL
SEQRES 12 A 263 MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU THR PRO
SEQRES 13 A 263 TRP HIS LEU ASP LYS THR TRP GLY GLN VAL GLN VAL PRO
SEQRES 14 A 263 THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE ALA PRO
SEQRES 15 A 263 VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 A 263 SER SER LEU PRO LYS ALA TYR MET GLU LEU CYS GLY ALA
SEQRES 17 A 263 THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR ILE ALA
SEQRES 18 A 263 LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL ASP GLU
SEQRES 19 A 263 ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN PRO THR
SEQRES 20 A 263 ASP ARG ALA ILE CYS GLU TYR ARG SER THR CYS PRO TYR
SEQRES 21 A 263 LYS LEU ASN
SEQRES 1 B 263 GLY PRO ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 263 ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER VAL ALA
SEQRES 3 B 263 THR GLU ARG VAL SER SER PHE ALA SER GLY PHE GLY GLY
SEQRES 4 B 263 GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU GLY THR
SEQRES 5 B 263 PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR ALA SER
SEQRES 6 B 263 GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL ALA SER
SEQRES 7 B 263 HIS GLY PHE ILE VAL PHE THR ILE ASP THR ASN THR ARG
SEQRES 8 B 263 LEU ASP ALA PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA
SEQRES 9 B 263 ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG LYS VAL
SEQRES 10 B 263 ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL MET GLY
SEQRES 11 B 263 HIS SER MET GLY GLY GLY GLY SER LEU GLU ALA THR VAL
SEQRES 12 B 263 MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU THR PRO
SEQRES 13 B 263 TRP HIS LEU ASP LYS THR TRP GLY GLN VAL GLN VAL PRO
SEQRES 14 B 263 THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE ALA PRO
SEQRES 15 B 263 VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 B 263 SER SER LEU PRO LYS ALA TYR MET GLU LEU CYS GLY ALA
SEQRES 17 B 263 THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR ILE ALA
SEQRES 18 B 263 LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL ASP GLU
SEQRES 19 B 263 ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN PRO THR
SEQRES 20 B 263 ASP ARG ALA ILE CYS GLU TYR ARG SER THR CYS PRO TYR
SEQRES 21 B 263 LYS LEU ASN
HET DIO A 401 6
HET DIO B 401 6
HET DIO B 402 6
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
FORMUL 3 DIO 3(C4 H8 O2)
FORMUL 6 HOH *638(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 ALA A 108 SER A 112 5 5
HELIX 3 AA3 MET A 113 SER A 114 5 2
HELIX 4 AA4 TRP A 115 SER A 122 1 8
HELIX 5 AA5 ALA A 138 ARG A 156 1 19
HELIX 6 AA6 ASP A 158 GLU A 163 1 6
HELIX 7 AA7 SER A 176 ARG A 189 1 14
HELIX 8 AA8 HIS A 230 LEU A 238 1 9
HELIX 9 AA9 PHE A 255 ILE A 259 5 5
HELIX 10 AB1 ASN A 261 ASP A 277 1 17
HELIX 11 AB2 ASP A 279 ARG A 281 5 3
HELIX 12 AB3 TYR A 282 CYS A 287 1 6
HELIX 13 AB4 THR B 56 ALA B 62 1 7
HELIX 14 AB5 ALA B 108 SER B 112 5 5
HELIX 15 AB6 MET B 113 SER B 114 5 2
HELIX 16 AB7 TRP B 115 SER B 122 1 8
HELIX 17 AB8 ALA B 138 ARG B 156 1 19
HELIX 18 AB9 ASP B 158 GLU B 163 1 6
HELIX 19 AC1 SER B 176 ARG B 189 1 14
HELIX 20 AC2 HIS B 230 LEU B 238 1 9
HELIX 21 AC3 PHE B 255 ILE B 259 5 5
HELIX 22 AC4 ASN B 261 ASP B 277 1 17
HELIX 23 AC5 ASP B 279 ARG B 281 5 3
HELIX 24 AC6 TYR B 282 CYS B 287 1 6
SHEET 1 AA1 6 VAL A 69 ALA A 78 0
SHEET 2 AA1 6 GLY A 82 PRO A 89 -1 O GLY A 84 N VAL A 74
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N VAL A 102 O PHE A 128
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O ASP A 166 N PHE A 97
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O MET A 247 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O CYS A 296 N GLU A 248
SHEET 1 AA3 6 VAL B 69 ALA B 78 0
SHEET 2 AA3 6 GLY B 82 PRO B 89 -1 O ILE B 86 N GLU B 72
SHEET 3 AA3 6 ILE B 126 ILE B 130 -1 O VAL B 127 N TYR B 87
SHEET 4 AA3 6 PHE B 97 ALA B 103 1 N VAL B 102 O PHE B 128
SHEET 5 AA3 6 LEU B 165 HIS B 175 1 O ASP B 166 N PHE B 97
SHEET 6 AA3 6 ALA B 194 LEU B 198 1 O LEU B 198 N GLY B 174
SHEET 1 AA4 3 THR B 214 ALA B 219 0
SHEET 2 AA4 3 LYS B 244 LEU B 249 1 O MET B 247 N GLY B 218
SHEET 3 AA4 3 ILE B 295 SER B 300 -1 O CYS B 296 N GLU B 248
SSBOND 1 CYS A 250 CYS A 296 1555 1555 2.03
SSBOND 2 CYS A 287 CYS A 302 1555 1555 2.03
SSBOND 3 CYS B 250 CYS B 296 1555 1555 2.05
SSBOND 4 CYS B 287 CYS B 302 1555 1555 2.03
CISPEP 1 CYS A 287 PRO A 288 0 -2.92
CISPEP 2 CYS A 302 PRO A 303 0 -6.13
CISPEP 3 CYS B 287 PRO B 288 0 -4.84
CISPEP 4 CYS B 302 PRO B 303 0 -6.67
CRYST1 68.128 81.697 85.556 90.00 90.00 90.00 P 21 21 21 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 0.014678 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012240 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011688 0.00000
TER 2015 TYR A 304
TER 4030 TYR B 304
MASTER 283 0 3 24 18 0 0 6 4668 2 26 42
END |