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HEADER HYDROLASE 20-AUG-20 7CTS
TITLE OPEN FORM OF PET-DEGRADING CUTINASE CUT190 WITH THERMOSTABILITY-
TITLE 2 IMPROVING MUTATIONS OF S226P/R228S/Q138A/D250C-E296C/Q123H/N202H AND
TITLE 3 S176A INACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
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 7CTS 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. 1.10 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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 125695
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6281
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 30.0200 - 3.4100 0.99 4397 234 0.1439 0.1652
REMARK 3 2 3.4100 - 2.7100 0.99 4234 227 0.1413 0.1349
REMARK 3 3 2.7100 - 2.3600 0.99 4206 222 0.1316 0.1371
REMARK 3 4 2.3600 - 2.1500 0.99 4142 220 0.1231 0.1361
REMARK 3 5 2.1500 - 1.9900 0.99 4139 213 0.1190 0.1478
REMARK 3 6 1.9900 - 1.8800 0.98 4095 214 0.1143 0.1564
REMARK 3 7 1.8800 - 1.7800 0.98 4070 217 0.1237 0.1658
REMARK 3 8 1.7800 - 1.7100 0.98 4079 220 0.1168 0.1501
REMARK 3 9 1.7100 - 1.6400 0.98 4047 206 0.1077 0.1427
REMARK 3 10 1.6400 - 1.5800 0.98 4061 214 0.1040 0.1251
REMARK 3 11 1.5800 - 1.5300 0.97 4020 222 0.1030 0.1342
REMARK 3 12 1.5300 - 1.4900 0.97 4049 199 0.1080 0.1476
REMARK 3 13 1.4900 - 1.4500 0.97 4001 218 0.1175 0.1529
REMARK 3 14 1.4500 - 1.4200 0.97 3971 208 0.1257 0.1409
REMARK 3 15 1.4200 - 1.3800 0.97 4005 222 0.1375 0.1717
REMARK 3 16 1.3800 - 1.3500 0.96 3978 198 0.1476 0.1607
REMARK 3 17 1.3500 - 1.3300 0.96 3949 213 0.1520 0.1937
REMARK 3 18 1.3300 - 1.3000 0.96 3950 205 0.1575 0.1668
REMARK 3 19 1.3000 - 1.2800 0.96 3936 215 0.1655 0.2095
REMARK 3 20 1.2800 - 1.2600 0.95 3901 210 0.1765 0.1868
REMARK 3 21 1.2600 - 1.2400 0.95 3954 197 0.1812 0.2266
REMARK 3 22 1.2400 - 1.2200 0.94 3890 213 0.1956 0.2254
REMARK 3 23 1.2200 - 1.2000 0.94 3848 191 0.2073 0.2347
REMARK 3 24 1.2000 - 1.1800 0.94 3823 214 0.2244 0.2450
REMARK 3 25 1.1800 - 1.1700 0.93 3849 198 0.2552 0.2750
REMARK 3 26 1.1700 - 1.1500 0.92 3787 184 0.2598 0.2806
REMARK 3 27 1.1500 - 1.1400 0.93 3806 200 0.2650 0.2573
REMARK 3 28 1.1400 - 1.1200 0.93 3836 206 0.2899 0.3276
REMARK 3 29 1.1200 - 1.1100 0.93 3837 168 0.3026 0.3171
REMARK 3 30 1.1100 - 1.1000 0.88 3554 213 0.3140 0.3445
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) : 0.129
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.735
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.92
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 2117
REMARK 3 ANGLE : 1.164 2885
REMARK 3 CHIRALITY : 0.095 310
REMARK 3 PLANARITY : 0.010 378
REMARK 3 DIHEDRAL : 13.195 788
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 7CTS 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_1300018248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-19
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : NULL
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 : 125717
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
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) : 1.06000
REMARK 200 FOR SHELL : 1.100
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: 4WFJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE, 2% (V/V) 1,4-DIOXANE, 10%
REMARK 280 (W/V) PEG 20000, 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 31.31150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.22650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.49200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.22650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.31150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.49200
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 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 176 -122.27 65.85
REMARK 500 THR A 199 58.34 34.46
REMARK 500 HIS A 230 -84.12 -119.42
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 A1033 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A1034 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A1035 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A1036 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A1037 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1038 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A1039 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A1040 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A1041 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A1042 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A1043 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH A1044 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH A1045 DISTANCE = 9.12 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 106.8
REMARK 620 3 PHE A 81 O 106.2 86.8
REMARK 620 4 HOH A 656 O 151.1 100.9 83.1
REMARK 620 5 HOH A 892 O 89.0 95.7 163.3 80.2
REMARK 620 6 HOH A 894 O 83.0 168.9 85.5 70.3 89.5
REMARK 620 N 1 2 3 4 5
DBREF 7CTS A 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
SEQADV 7CTS GLY A 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTS PRO A 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTS HIS A 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 7CTS ALA A 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 7CTS ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 7CTS HIS A 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 7CTS PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 7CTS SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 7CTS CYS A 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 7CTS CYS A 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 7CTS LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTS LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CTS ASN A 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 ALA 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
HET DIO A 501 6
HET BCN A 502 11
HET CA A 503 1
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM BCN BICINE
HETNAM CA CALCIUM ION
FORMUL 2 DIO C4 H8 O2
FORMUL 3 BCN C6 H13 N O4
FORMUL 4 CA CA 2+
FORMUL 5 HOH *445(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 SER A 109 MET A 113 5 5
HELIX 3 AA3 SER A 114 SER A 122 1 9
HELIX 4 AA4 ALA A 138 ARG A 156 1 19
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 ALA A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O ILE A 86 N GLU A 72
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
SSBOND 1 CYS A 250 CYS A 296 1555 1555 2.05
SSBOND 2 CYS A 287 CYS A 302 1555 1555 2.06
LINK O SER A 76 CA CA A 503 1555 1555 2.26
LINK O ALA A 78 CA CA A 503 1555 1555 2.29
LINK O PHE A 81 CA CA A 503 1555 1555 2.29
LINK CA CA A 503 O HOH A 656 1555 1555 2.39
LINK CA CA A 503 O HOH A 892 1555 1555 2.33
LINK CA CA A 503 O HOH A 894 1555 1555 2.61
CISPEP 1 CYS A 287 PRO A 288 0 -2.27
CISPEP 2 CYS A 302 PRO A 303 0 1.96
CRYST1 62.623 64.984 78.453 90.00 90.00 90.00 P 21 21 21 4
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 0.015969 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015388 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012746 0.00000
TER 2041 ASN A 307
MASTER 289 0 3 11 9 0 0 6 2494 1 29 21
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