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HEADER HYDROLASE 10-MAY-22 7XRI
TITLE FERULOYL ESTERASE MUTANT -S106A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINNAMOYL ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: PROTEIN WITH TAG SEQUENCE AT N-TERMINAL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS ACIDOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1579;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERULOYL ESTERASE MUTANT (S101A) COMPLEXED WITH ETHYL FERULATE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.HWANG,J.H.LEE,H.DO,C.W.LEE
REVDAT 1 17-MAY-23 7XRI 0
JRNL AUTH J.S.HWANG,J.H.LEE,H.DO,C.W.LEE
JRNL TITL FERULOYL ESTERASE MUTANT -S106A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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 : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 71873
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) : 0.186
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3603
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 45.8500 - 6.4800 0.99 2714 141 0.1848 0.2115
REMARK 3 2 6.4800 - 5.1500 1.00 2686 147 0.2034 0.2344
REMARK 3 3 5.1500 - 4.5000 1.00 2688 122 0.1733 0.1937
REMARK 3 4 4.5000 - 4.0900 0.99 2655 133 0.1645 0.2137
REMARK 3 5 4.0900 - 3.7900 0.99 2663 147 0.1730 0.1871
REMARK 3 6 3.7900 - 3.5700 0.99 2643 141 0.1756 0.1969
REMARK 3 7 3.5700 - 3.3900 0.99 2686 113 0.1785 0.1772
REMARK 3 8 3.3900 - 3.2400 0.99 2621 139 0.1924 0.2301
REMARK 3 9 3.2400 - 3.1200 0.99 2654 147 0.1901 0.1977
REMARK 3 10 3.1200 - 3.0100 0.99 2656 149 0.1903 0.1881
REMARK 3 11 3.0100 - 2.9200 0.99 2614 152 0.1885 0.2361
REMARK 3 12 2.9200 - 2.8300 0.99 2627 140 0.1881 0.2214
REMARK 3 13 2.8300 - 2.7600 0.99 2633 153 0.2017 0.2368
REMARK 3 14 2.7600 - 2.6900 0.99 2669 121 0.1965 0.2504
REMARK 3 15 2.6900 - 2.6300 0.99 2640 133 0.1921 0.2132
REMARK 3 16 2.6300 - 2.5700 0.99 2601 143 0.1932 0.2197
REMARK 3 17 2.5700 - 2.5200 0.99 2609 133 0.1954 0.2145
REMARK 3 18 2.5200 - 2.4800 0.99 2664 131 0.1890 0.2498
REMARK 3 19 2.4800 - 2.4300 0.99 2636 128 0.1915 0.1760
REMARK 3 20 2.4300 - 2.3900 0.98 2621 138 0.1810 0.2113
REMARK 3 21 2.3900 - 2.3500 0.99 2573 159 0.1917 0.2401
REMARK 3 22 2.3500 - 2.3200 0.98 2614 159 0.1928 0.2438
REMARK 3 23 2.3200 - 2.2800 0.98 2599 162 0.1972 0.2163
REMARK 3 24 2.2800 - 2.2500 0.98 2606 139 0.1895 0.2515
REMARK 3 25 2.2500 - 2.2200 0.98 2626 128 0.1904 0.2307
REMARK 3 26 2.2200 - 2.1900 0.85 2272 105 0.1946 0.2185
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) : 0.203
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.263
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.99
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 : 0.019 8105
REMARK 3 ANGLE : 2.045 11003
REMARK 3 CHIRALITY : 0.112 1211
REMARK 3 PLANARITY : 0.013 1465
REMARK 3 DIHEDRAL : 21.419 2952
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 7XRI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029450.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71881
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
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) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3PF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M MAGNESIUM CHLORIDE, 0.1 M
REMARK 280 HEPES:NAOH PH 7.5 AND 22 % (W/V) POLYACRYLIC ACID 5100, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 296K
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 65.18800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.69550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.18800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 76.69550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 LEU A 246
REMARK 465 PHE A 247
REMARK 465 LEU B 246
REMARK 465 PHE B 247
REMARK 465 LEU C 246
REMARK 465 PHE C 247
REMARK 465 GLY D -10
REMARK 465 THR D -9
REMARK 465 THR D -8
REMARK 465 GLU D -7
REMARK 465 ASN D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 LEU D 246
REMARK 465 PHE D 247
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 PHE A 21 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE C 21 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET D 219 CG SD CE
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 N GLN B 107 CAA ZYC B 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 19 CD GLU A 19 OE1 -0.077
REMARK 500 GLU B 19 CD GLU B 19 OE1 -0.070
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 ARG A 98 -91.12 -99.06
REMARK 500 ALA A 106 -117.44 64.44
REMARK 500 ALA A 132 51.58 -94.28
REMARK 500 ALA A 157 146.69 -172.15
REMARK 500 HIS A 161 58.37 37.00
REMARK 500 ASP A 222 -5.32 76.68
REMARK 500 ASP B 9 54.91 38.67
REMARK 500 ARG B 98 -89.44 -89.07
REMARK 500 ALA B 106 -122.96 62.06
REMARK 500 ALA B 132 48.98 -91.75
REMARK 500 ASP B 222 -13.06 76.14
REMARK 500 ARG C 98 -86.01 -93.50
REMARK 500 ALA C 106 -110.73 57.22
REMARK 500 ASP C 222 -5.95 73.07
REMARK 500 ARG D 3 116.90 -20.64
REMARK 500 THR D 35 -4.60 72.68
REMARK 500 ARG D 98 -93.12 -96.09
REMARK 500 ALA D 106 -108.92 70.72
REMARK 500 ALA D 132 47.48 -85.18
REMARK 500 GLN D 145 -126.34 56.79
REMARK 500 HIS D 153 67.26 -150.70
REMARK 500 ALA D 157 143.26 -175.41
REMARK 500 ASN D 196 -71.54 -90.08
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 C 510 DISTANCE = 5.87 ANGSTROMS
DBREF1 7XRI A 1 247 UNP A0A060IN49_LACAI
DBREF2 7XRI A A0A060IN49 1 247
DBREF1 7XRI B 1 247 UNP A0A060IN49_LACAI
DBREF2 7XRI B A0A060IN49 1 247
DBREF1 7XRI C 1 247 UNP A0A060IN49_LACAI
DBREF2 7XRI C A0A060IN49 1 247
DBREF1 7XRI D 1 247 UNP A0A060IN49_LACAI
DBREF2 7XRI D A0A060IN49 1 247
SEQADV 7XRI GLY A -10 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR A -9 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR A -8 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLU A -7 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ASN A -6 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI LEU A -5 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI TYR A -4 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI PHE A -3 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLN A -2 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLY A -1 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI SER A 0 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ALA A 106 UNP A0A060IN4 SER 106 ENGINEERED MUTATION
SEQADV 7XRI GLY B -10 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR B -9 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR B -8 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLU B -7 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ASN B -6 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI LEU B -5 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI TYR B -4 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI PHE B -3 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLN B -2 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLY B -1 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI SER B 0 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ALA B 106 UNP A0A060IN4 SER 106 ENGINEERED MUTATION
SEQADV 7XRI GLY C -10 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR C -9 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR C -8 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLU C -7 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ASN C -6 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI LEU C -5 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI TYR C -4 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI PHE C -3 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLN C -2 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLY C -1 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI SER C 0 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ALA C 106 UNP A0A060IN4 SER 106 ENGINEERED MUTATION
SEQADV 7XRI GLY D -10 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR D -9 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI THR D -8 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLU D -7 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ASN D -6 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI LEU D -5 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI TYR D -4 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI PHE D -3 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLN D -2 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI GLY D -1 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI SER D 0 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRI ALA D 106 UNP A0A060IN4 SER 106 ENGINEERED MUTATION
SEQRES 1 A 258 GLY THR THR GLU ASN LEU TYR PHE GLN GLY SER MET SER
SEQRES 2 A 258 ARG ILE THR ILE GLU ARG ASP GLY LEU THR LEU VAL GLY
SEQRES 3 A 258 ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR ASP MET ALA
SEQRES 4 A 258 ILE LEU MET HIS GLY PHE THR ALA ASN ARG ASN THR PRO
SEQRES 5 A 258 LEU LEU ARG GLN ILE ALA ASP ASN LEU ARG ASP GLU ASN
SEQRES 6 A 258 VAL ALA SER VAL ARG PHE ASP PHE ASN GLY HIS GLY GLU
SEQRES 7 A 258 SER ASP GLY ALA PHE GLU ASP MET THR VAL CYS ASN GLU
SEQRES 8 A 258 ILE ALA ASP ALA GLN LYS ILE LEU GLU TYR VAL ARG THR
SEQRES 9 A 258 ASP PRO HIS VAL ARG ASN ILE PHE LEU VAL GLY HIS ALA
SEQRES 10 A 258 GLN GLY GLY VAL VAL ALA SER MET LEU ALA GLY LEU TYR
SEQRES 11 A 258 PRO ASP ILE VAL LYS LYS VAL VAL LEU LEU ALA PRO ALA
SEQRES 12 A 258 ALA GLN LEU LYS ASP ASP ALA LEU ASN GLY ASP THR GLN
SEQRES 13 A 258 GLY ALA THR TYR ASN PRO GLU HIS ILE PRO ALA ALA ILE
SEQRES 14 A 258 PRO PHE HIS GLY LYS LYS LEU GLY GLY PHE TYR LEU ARG
SEQRES 15 A 258 THR ALA GLN VAL LEU PRO ILE TYR GLU ILE ALA LYS HIS
SEQRES 16 A 258 TYR THR ASN PRO VAL SER ILE ILE VAL GLY SER ASN ASP
SEQRES 17 A 258 GLN VAL VAL ALA PRO LYS TYR SER LYS LYS TYR ASP GLU
SEQRES 18 A 258 VAL TYR GLU ASN SER GLU LEU HIS MET VAL PRO ASP ALA
SEQRES 19 A 258 ASP HIS SER PHE THR GLY GLN TYR LYS ASP SER ALA VAL
SEQRES 20 A 258 ASP LEU THR ALA GLU PHE LEU LYS PRO LEU PHE
SEQRES 1 B 258 GLY THR THR GLU ASN LEU TYR PHE GLN GLY SER MET SER
SEQRES 2 B 258 ARG ILE THR ILE GLU ARG ASP GLY LEU THR LEU VAL GLY
SEQRES 3 B 258 ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR ASP MET ALA
SEQRES 4 B 258 ILE LEU MET HIS GLY PHE THR ALA ASN ARG ASN THR PRO
SEQRES 5 B 258 LEU LEU ARG GLN ILE ALA ASP ASN LEU ARG ASP GLU ASN
SEQRES 6 B 258 VAL ALA SER VAL ARG PHE ASP PHE ASN GLY HIS GLY GLU
SEQRES 7 B 258 SER ASP GLY ALA PHE GLU ASP MET THR VAL CYS ASN GLU
SEQRES 8 B 258 ILE ALA ASP ALA GLN LYS ILE LEU GLU TYR VAL ARG THR
SEQRES 9 B 258 ASP PRO HIS VAL ARG ASN ILE PHE LEU VAL GLY HIS ALA
SEQRES 10 B 258 GLN GLY GLY VAL VAL ALA SER MET LEU ALA GLY LEU TYR
SEQRES 11 B 258 PRO ASP ILE VAL LYS LYS VAL VAL LEU LEU ALA PRO ALA
SEQRES 12 B 258 ALA GLN LEU LYS ASP ASP ALA LEU ASN GLY ASP THR GLN
SEQRES 13 B 258 GLY ALA THR TYR ASN PRO GLU HIS ILE PRO ALA ALA ILE
SEQRES 14 B 258 PRO PHE HIS GLY LYS LYS LEU GLY GLY PHE TYR LEU ARG
SEQRES 15 B 258 THR ALA GLN VAL LEU PRO ILE TYR GLU ILE ALA LYS HIS
SEQRES 16 B 258 TYR THR ASN PRO VAL SER ILE ILE VAL GLY SER ASN ASP
SEQRES 17 B 258 GLN VAL VAL ALA PRO LYS TYR SER LYS LYS TYR ASP GLU
SEQRES 18 B 258 VAL TYR GLU ASN SER GLU LEU HIS MET VAL PRO ASP ALA
SEQRES 19 B 258 ASP HIS SER PHE THR GLY GLN TYR LYS ASP SER ALA VAL
SEQRES 20 B 258 ASP LEU THR ALA GLU PHE LEU LYS PRO LEU PHE
SEQRES 1 C 258 GLY THR THR GLU ASN LEU TYR PHE GLN GLY SER MET SER
SEQRES 2 C 258 ARG ILE THR ILE GLU ARG ASP GLY LEU THR LEU VAL GLY
SEQRES 3 C 258 ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR ASP MET ALA
SEQRES 4 C 258 ILE LEU MET HIS GLY PHE THR ALA ASN ARG ASN THR PRO
SEQRES 5 C 258 LEU LEU ARG GLN ILE ALA ASP ASN LEU ARG ASP GLU ASN
SEQRES 6 C 258 VAL ALA SER VAL ARG PHE ASP PHE ASN GLY HIS GLY GLU
SEQRES 7 C 258 SER ASP GLY ALA PHE GLU ASP MET THR VAL CYS ASN GLU
SEQRES 8 C 258 ILE ALA ASP ALA GLN LYS ILE LEU GLU TYR VAL ARG THR
SEQRES 9 C 258 ASP PRO HIS VAL ARG ASN ILE PHE LEU VAL GLY HIS ALA
SEQRES 10 C 258 GLN GLY GLY VAL VAL ALA SER MET LEU ALA GLY LEU TYR
SEQRES 11 C 258 PRO ASP ILE VAL LYS LYS VAL VAL LEU LEU ALA PRO ALA
SEQRES 12 C 258 ALA GLN LEU LYS ASP ASP ALA LEU ASN GLY ASP THR GLN
SEQRES 13 C 258 GLY ALA THR TYR ASN PRO GLU HIS ILE PRO ALA ALA ILE
SEQRES 14 C 258 PRO PHE HIS GLY LYS LYS LEU GLY GLY PHE TYR LEU ARG
SEQRES 15 C 258 THR ALA GLN VAL LEU PRO ILE TYR GLU ILE ALA LYS HIS
SEQRES 16 C 258 TYR THR ASN PRO VAL SER ILE ILE VAL GLY SER ASN ASP
SEQRES 17 C 258 GLN VAL VAL ALA PRO LYS TYR SER LYS LYS TYR ASP GLU
SEQRES 18 C 258 VAL TYR GLU ASN SER GLU LEU HIS MET VAL PRO ASP ALA
SEQRES 19 C 258 ASP HIS SER PHE THR GLY GLN TYR LYS ASP SER ALA VAL
SEQRES 20 C 258 ASP LEU THR ALA GLU PHE LEU LYS PRO LEU PHE
SEQRES 1 D 258 GLY THR THR GLU ASN LEU TYR PHE GLN GLY SER MET SER
SEQRES 2 D 258 ARG ILE THR ILE GLU ARG ASP GLY LEU THR LEU VAL GLY
SEQRES 3 D 258 ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR ASP MET ALA
SEQRES 4 D 258 ILE LEU MET HIS GLY PHE THR ALA ASN ARG ASN THR PRO
SEQRES 5 D 258 LEU LEU ARG GLN ILE ALA ASP ASN LEU ARG ASP GLU ASN
SEQRES 6 D 258 VAL ALA SER VAL ARG PHE ASP PHE ASN GLY HIS GLY GLU
SEQRES 7 D 258 SER ASP GLY ALA PHE GLU ASP MET THR VAL CYS ASN GLU
SEQRES 8 D 258 ILE ALA ASP ALA GLN LYS ILE LEU GLU TYR VAL ARG THR
SEQRES 9 D 258 ASP PRO HIS VAL ARG ASN ILE PHE LEU VAL GLY HIS ALA
SEQRES 10 D 258 GLN GLY GLY VAL VAL ALA SER MET LEU ALA GLY LEU TYR
SEQRES 11 D 258 PRO ASP ILE VAL LYS LYS VAL VAL LEU LEU ALA PRO ALA
SEQRES 12 D 258 ALA GLN LEU LYS ASP ASP ALA LEU ASN GLY ASP THR GLN
SEQRES 13 D 258 GLY ALA THR TYR ASN PRO GLU HIS ILE PRO ALA ALA ILE
SEQRES 14 D 258 PRO PHE HIS GLY LYS LYS LEU GLY GLY PHE TYR LEU ARG
SEQRES 15 D 258 THR ALA GLN VAL LEU PRO ILE TYR GLU ILE ALA LYS HIS
SEQRES 16 D 258 TYR THR ASN PRO VAL SER ILE ILE VAL GLY SER ASN ASP
SEQRES 17 D 258 GLN VAL VAL ALA PRO LYS TYR SER LYS LYS TYR ASP GLU
SEQRES 18 D 258 VAL TYR GLU ASN SER GLU LEU HIS MET VAL PRO ASP ALA
SEQRES 19 D 258 ASP HIS SER PHE THR GLY GLN TYR LYS ASP SER ALA VAL
SEQRES 20 D 258 ASP LEU THR ALA GLU PHE LEU LYS PRO LEU PHE
HET ZYC A 301 16
HET ZYC B 301 16
HET ZYC C 301 16
HET ZYC D 301 16
HETNAM ZYC ETHYL (2E)-3-(4-HYDROXY-3-METHOXYPHENYL)PROP-2-ENOATE
HETSYN ZYC ETHYL FERULATE
FORMUL 5 ZYC 4(C12 H14 O4)
FORMUL 9 HOH *440(H2 O)
HELIX 1 AA1 THR A 40 GLU A 53 1 14
HELIX 2 AA2 ALA A 71 MET A 75 5 5
HELIX 3 AA3 THR A 76 THR A 93 1 18
HELIX 4 AA4 ALA A 106 TYR A 119 1 14
HELIX 5 AA5 ALA A 133 GLY A 142 1 10
HELIX 6 AA6 GLY A 167 VAL A 175 1 9
HELIX 7 AA7 PRO A 177 LYS A 183 1 7
HELIX 8 AA8 PRO A 202 TYR A 212 1 11
HELIX 9 AA9 THR A 228 GLN A 230 5 3
HELIX 10 AB1 TYR A 231 LYS A 244 1 14
HELIX 11 AB2 THR B 40 GLU B 53 1 14
HELIX 12 AB3 ALA B 71 MET B 75 5 5
HELIX 13 AB4 THR B 76 THR B 93 1 18
HELIX 14 AB5 ALA B 106 TYR B 119 1 14
HELIX 15 AB6 ALA B 133 GLY B 142 1 10
HELIX 16 AB7 GLY B 167 VAL B 175 1 9
HELIX 17 AB8 PRO B 177 LYS B 183 1 7
HELIX 18 AB9 PRO B 202 TYR B 212 1 11
HELIX 19 AC1 GLY B 229 LYS B 244 1 16
HELIX 20 AC2 THR C 40 GLU C 53 1 14
HELIX 21 AC3 ALA C 71 MET C 75 5 5
HELIX 22 AC4 THR C 76 THR C 93 1 18
HELIX 23 AC5 ALA C 106 TYR C 119 1 14
HELIX 24 AC6 ALA C 133 GLY C 142 1 10
HELIX 25 AC7 GLY C 167 VAL C 175 1 9
HELIX 26 AC8 PRO C 177 LYS C 183 1 7
HELIX 27 AC9 PRO C 202 TYR C 212 1 11
HELIX 28 AD1 GLY C 229 LYS C 244 1 16
HELIX 29 AD2 THR D 40 GLU D 53 1 14
HELIX 30 AD3 ALA D 71 MET D 75 5 5
HELIX 31 AD4 THR D 76 ASP D 94 1 19
HELIX 32 AD5 ALA D 106 TYR D 119 1 14
HELIX 33 AD6 ALA D 133 GLY D 142 1 10
HELIX 34 AD7 GLY D 167 GLN D 174 1 8
HELIX 35 AD8 PRO D 177 LYS D 183 1 7
HELIX 36 AD9 PRO D 202 TYR D 212 1 11
HELIX 37 AE1 GLY D 229 LYS D 244 1 16
SHEET 1 AA1 8 SER A 0 ARG A 8 0
SHEET 2 AA1 8 LEU A 11 GLU A 19 -1 O GLY A 15 N ILE A 4
SHEET 3 AA1 8 VAL A 55 PHE A 60 -1 O SER A 57 N GLU A 18
SHEET 4 AA1 8 TYR A 25 MET A 31 1 N LEU A 30 O VAL A 58
SHEET 5 AA1 8 VAL A 97 HIS A 105 1 O VAL A 103 N ILE A 29
SHEET 6 AA1 8 VAL A 123 LEU A 129 1 O LYS A 124 N ILE A 100
SHEET 7 AA1 8 VAL A 189 GLY A 194 1 O ILE A 192 N LEU A 128
SHEET 8 AA1 8 SER A 215 VAL A 220 1 O HIS A 218 N ILE A 191
SHEET 1 AA2 2 ASP A 143 THR A 144 0
SHEET 2 AA2 2 ALA A 147 THR A 148 -1 O ALA A 147 N THR A 144
SHEET 1 AA3 2 ALA A 157 PHE A 160 0
SHEET 2 AA3 2 LYS A 163 GLY A 166 -1 O LYS A 163 N PHE A 160
SHEET 1 AA4 8 SER B 0 ARG B 8 0
SHEET 2 AA4 8 LEU B 11 GLU B 19 -1 O LEU B 13 N ILE B 6
SHEET 3 AA4 8 ALA B 56 PHE B 60 -1 O SER B 57 N GLU B 18
SHEET 4 AA4 8 TYR B 25 MET B 31 1 N LEU B 30 O VAL B 58
SHEET 5 AA4 8 VAL B 97 HIS B 105 1 O VAL B 103 N ILE B 29
SHEET 6 AA4 8 VAL B 123 LEU B 129 1 O LYS B 124 N ILE B 100
SHEET 7 AA4 8 VAL B 189 GLY B 194 1 O ILE B 192 N LEU B 128
SHEET 8 AA4 8 SER B 215 VAL B 220 1 O VAL B 220 N VAL B 193
SHEET 1 AA5 2 ASP B 143 THR B 144 0
SHEET 2 AA5 2 ALA B 147 THR B 148 -1 O ALA B 147 N THR B 144
SHEET 1 AA6 2 ALA B 157 PHE B 160 0
SHEET 2 AA6 2 LYS B 163 GLY B 166 -1 O LYS B 163 N PHE B 160
SHEET 1 AA7 8 SER C 0 ARG C 8 0
SHEET 2 AA7 8 LEU C 11 GLU C 19 -1 O LEU C 13 N ILE C 6
SHEET 3 AA7 8 ALA C 56 PHE C 60 -1 O SER C 57 N GLU C 18
SHEET 4 AA7 8 TYR C 25 MET C 31 1 N LEU C 30 O VAL C 58
SHEET 5 AA7 8 VAL C 97 HIS C 105 1 O VAL C 103 N ILE C 29
SHEET 6 AA7 8 VAL C 123 LEU C 129 1 O LYS C 124 N ILE C 100
SHEET 7 AA7 8 VAL C 189 GLY C 194 1 O ILE C 192 N LEU C 128
SHEET 8 AA7 8 SER C 215 VAL C 220 1 O HIS C 218 N ILE C 191
SHEET 1 AA8 2 ASP C 143 THR C 144 0
SHEET 2 AA8 2 ALA C 147 THR C 148 -1 O ALA C 147 N THR C 144
SHEET 1 AA9 2 ALA C 157 PHE C 160 0
SHEET 2 AA9 2 LYS C 163 GLY C 166 -1 O LYS C 163 N PHE C 160
SHEET 1 AB1 8 ARG D 3 ARG D 8 0
SHEET 2 AB1 8 LEU D 11 GLU D 18 -1 O LEU D 13 N ILE D 6
SHEET 3 AB1 8 ALA D 56 PHE D 60 -1 O SER D 57 N GLU D 18
SHEET 4 AB1 8 TYR D 25 MET D 31 1 N LEU D 30 O VAL D 58
SHEET 5 AB1 8 VAL D 97 HIS D 105 1 O VAL D 103 N ILE D 29
SHEET 6 AB1 8 VAL D 123 LEU D 129 1 O LEU D 129 N GLY D 104
SHEET 7 AB1 8 VAL D 189 ILE D 192 1 O ILE D 192 N LEU D 128
SHEET 8 AB1 8 SER D 215 HIS D 218 1 O HIS D 218 N ILE D 191
SHEET 1 AB2 2 ASP D 143 THR D 144 0
SHEET 2 AB2 2 ALA D 147 THR D 148 -1 O ALA D 147 N THR D 144
SHEET 1 AB3 2 ALA D 157 PHE D 160 0
SHEET 2 AB3 2 LYS D 163 GLY D 166 -1 O LYS D 163 N PHE D 160
CRYST1 130.376 153.391 91.252 90.00 127.40 90.00 C 1 2 1 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 0.007670 0.000000 0.005863 0.00000
SCALE2 0.000000 0.006519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013794 0.00000
TER 1989 PRO A 245
TER 3984 PRO B 245
TER 5973 PRO C 245
TER 7872 PRO D 245
MASTER 349 0 4 37 48 0 0 6 8372 4 64 80
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