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HEADER HYDROLASE 26-FEB-24 8YFZ
TITLE CRYSTAL STRUCTURE OF THE EST1 H274E MUTANT AT PH 4.2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROLOBUS SHIBATAE;
SOURCE 3 ORGANISM_TAXID: 2286;
SOURCE 4 GENE: SSHESTI, J5U21_01394, J5U22_01308;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTC99A
KEYWDS ALPHA/BETA-HYDRORASE FOLD, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.UNNO,Y.OSHIMA,T.NISHINO,T.NAKAYAMA,M.KUSUNOKI
REVDAT 1 10-JUL-24 8YFZ 0
JRNL AUTH K.OHARA,Y.OSHIMA,H.UNNO,S.NAGANO,M.KUSUNOKI,S.TAKAHASHI,
JRNL AUTH 2 T.WAKI,S.YAMASHITA,T.NAKAYAMA
JRNL TITL LOWERING PH OPTIMUM OF ACTIVITY OF SSHESTI, A SLIGHTLY
JRNL TITL 2 ALKALIPHILIC ARCHAEAL ESTERASE OF THE HORMONE-SENSITIVE
JRNL TITL 3 LIPASE FAMILY.
JRNL REF J.BIOSCI.BIOENG. 2024
JRNL REFN ISSN 1389-1723
JRNL PMID 38918133
JRNL DOI 10.1016/J.JBIOSC.2024.05.010
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 43785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2337
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3084
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2339
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.114
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2436 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2272 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3308 ; 1.355 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5281 ; 0.788 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 301 ; 5.578 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;35.357 ;23.524
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 396 ;12.630 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.239 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 375 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2690 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 506 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 516 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2262 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1252 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1307 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 141 ; 0.136 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 15 ; 0.135 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.243 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.215 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1929 ; 1.007 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 611 ; 0.175 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2434 ; 1.190 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1093 ; 2.054 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 872 ; 2.849 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8YFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1300045494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 90.0
REMARK 200 PH : 4.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46125
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 18.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.29200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3000, 200MM NACL, 100MM
REMARK 280 PHOSPHATE-CITRATE, PH 4.2, VAPOR DIFFUSION, TEMPERATURE 293K, PH
REMARK 280 4.20
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.26100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.83600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.42000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.26100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.83600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.42000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.26100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 35.83600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.42000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.26100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 35.83600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.42000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 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 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 GLY A 14
REMARK 465 PHE A 15
REMARK 465 VAL A 16
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 SER A 151 -116.63 59.62
REMARK 500 TYR A 177 62.15 30.97
REMARK 500 PHE A 197 -62.90 75.72
REMARK 500 SER A 223 75.08 -116.96
REMARK 500 TYR A 243 66.55 -107.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WZJ RELATED DB: PDB
REMARK 900 EST1 AT PH7.0
REMARK 900 RELATED ID: 1WZP RELATED DB: PDB
REMARK 900 EST1 H274A MUTANT AT PH 4.2
REMARK 900 RELATED ID: 1WZQ RELATED DB: PDB
REMARK 900 EST1 H274E MUTANT AT PH 7.0
REMARK 900 RELATED ID: 1WZR RELATED DB: PDB
REMARK 900 EST1 H274E MUTANT AT PH 4.0
REMARK 900 RELATED ID: 1WZT RELATED DB: PDB
REMARK 900 EST1 H274D MUTANT AT PH 4.2
DBREF 8YFZ A 1 305 UNP Q5NU42 Q5NU42_9CREN 1 305
SEQADV 8YFZ GLU A 274 UNP Q5NU42 HIS 274 ENGINEERED MUTATION
SEQRES 1 A 305 MET PRO LEU ASP PRO ARG ILE LYS LYS LEU LEU GLU SER
SEQRES 2 A 305 GLY PHE VAL VAL PRO ILE GLY LYS ALA SER VAL ASP GLU
SEQRES 3 A 305 VAL ARG LYS ILE PHE ARG GLN LEU ALA SER ALA ALA PRO
SEQRES 4 A 305 LYS ALA GLU VAL ARG LYS VAL GLU ASP ILE LYS ILE PRO
SEQRES 5 A 305 GLY SER GLU THR SER ILE ASN ALA ARG VAL TYR PHE PRO
SEQRES 6 A 305 LYS ALA LYS GLY PRO TYR GLY VAL LEU VAL TYR LEU HIS
SEQRES 7 A 305 GLY GLY GLY PHE VAL ILE GLY ASP VAL GLU SER TYR ASP
SEQRES 8 A 305 PRO LEU CYS ARG ALA ILE THR ASN ALA CYS ASN CYS VAL
SEQRES 9 A 305 VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU TYR LYS
SEQRES 10 A 305 PHE PRO SER ALA VAL ILE ASP SER PHE ASP ALA THR ASN
SEQRES 11 A 305 TRP ILE TYR ASN ASN LEU ASP LYS PHE ASP GLY GLU MET
SEQRES 12 A 305 GLY ILE ALA ILE ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 13 A 305 ALA ALA VAL VAL ALA LEU LEU SER LYS GLY LYS LEU ASP
SEQRES 14 A 305 LEU LYS TYR GLN ILE LEU ILE TYR PRO ALA VAL GLY PHE
SEQRES 15 A 305 ASP SER VAL SER ARG SER MET ILE GLU TYR SER ASP GLY
SEQRES 16 A 305 PHE PHE LEU THR ARG GLU HIS ILE GLU TRP PHE GLY SER
SEQRES 17 A 305 GLN TYR LEU ARG SER PRO ALA ASP LEU LEU ASP PHE ARG
SEQRES 18 A 305 PHE SER PRO ILE ILE ALA GLN ASP LEU SER GLY LEU PRO
SEQRES 19 A 305 PRO ALA LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG
SEQRES 20 A 305 ASP GLN GLY GLU ALA TYR ALA ASN ARG LEU LEU GLN ALA
SEQRES 21 A 305 GLY VAL PRO VAL THR SER VAL ARG PHE ASN ASN VAL ILE
SEQRES 22 A 305 GLU GLY PHE LEU SER PHE PHE PRO LEU ILE ASP GLN GLY
SEQRES 23 A 305 LYS ASP ALA ILE GLY LEU ILE GLY SER VAL LEU ARG ARG
SEQRES 24 A 305 THR PHE TYR ASP LYS SER
HET BOG A 401 20
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 2 BOG C14 H28 O6
FORMUL 3 HOH *211(H2 O)
HELIX 1 AA1 ASP A 4 SER A 13 1 10
HELIX 2 AA2 SER A 23 ALA A 37 1 15
HELIX 3 AA3 TYR A 90 ASN A 102 1 13
HELIX 4 AA4 PRO A 119 ASN A 135 1 17
HELIX 5 AA5 LEU A 136 ASP A 140 5 5
HELIX 6 AA6 SER A 151 LYS A 165 1 15
HELIX 7 AA7 SER A 186 TYR A 192 1 7
HELIX 8 AA8 THR A 199 LEU A 211 1 13
HELIX 9 AA9 SER A 213 ASP A 219 5 7
HELIX 10 AB1 SER A 223 ALA A 227 5 5
HELIX 11 AB2 LEU A 246 ALA A 260 1 15
HELIX 12 AB3 GLY A 275 PHE A 280 5 6
HELIX 13 AB4 ILE A 283 ASP A 303 1 21
SHEET 1 AA1 8 LYS A 45 PRO A 52 0
SHEET 2 AA1 8 SER A 57 PHE A 64 -1 O VAL A 62 N GLU A 47
SHEET 3 AA1 8 VAL A 104 VAL A 108 -1 O VAL A 105 N TYR A 63
SHEET 4 AA1 8 VAL A 73 LEU A 77 1 N LEU A 74 O VAL A 104
SHEET 5 AA1 8 ILE A 145 ASP A 150 1 O ALA A 146 N VAL A 75
SHEET 6 AA1 8 LEU A 170 ILE A 176 1 O LYS A 171 N ILE A 145
SHEET 7 AA1 8 ALA A 236 TYR A 243 1 O LEU A 237 N LEU A 175
SHEET 8 AA1 8 VAL A 264 ILE A 273 1 O PHE A 269 N THR A 240
CISPEP 1 GLY A 69 PRO A 70 0 2.64
CISPEP 2 ALA A 113 PRO A 114 0 -0.36
CISPEP 3 PHE A 118 PRO A 119 0 0.79
CRYST1 58.522 71.672 136.840 90.00 90.00 90.00 I 2 2 2 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 0.017088 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007308 0.00000
TER 2361 SER A 305
MASTER 304 0 1 13 8 0 0 6 2570 1 20 24
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