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HEADER HYDROLASE 01-SEP-17 5YAL
TITLE FERULIC ACID ESTERASE FROM STREPTOMYCES CINNAMONEUS AT 1.5 A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 42-383;
COMPND 5 EC: 3.1.1.73;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CINNAMONEUS;
SOURCE 3 ORGANISM_TAXID: 53446;
SOURCE 4 GENE: ESTA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERULIC ACID ESTERASE, CATALYTIC TRIAD, SERINE PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TAMURA,M.URAJI,E.MIZOHATA,K.OGAWA,T.INOUE,T.HATANAKA
REVDAT 1 06-DEC-17 5YAL 0
JRNL AUTH M.URAJI,H.TAMURA,E.MIZOHATA,J.ARIMA,K.WAN,K.OGAWA,T.INOUE,
JRNL AUTH 2 T.HATANAKA
JRNL TITL LOOP OF STREPTOMYCES FERULOYL ESTERASE PLAYS AN IMPORTANT
JRNL TITL 2 ROLE IN ITS ACTIVITY OF RELEASING FERULIC ACID FROM BIOMASS
JRNL REF APPL. ENVIRON. MICROBIOL. 2017
JRNL REFN ESSN 1098-5336
JRNL PMID 29150515
JRNL DOI 10.1128/AEM.02300-17
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 50503
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2658
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) : 3676
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 193
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2610
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.269
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2708 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2608 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3694 ; 1.180 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5989 ; 0.897 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 347 ; 5.777 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 116 ;32.885 ;21.638
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 418 ;10.772 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;11.158 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 404 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3082 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 618 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1374 ; 0.601 ; 1.692
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1372 ; 0.602 ; 1.691
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1716 ; 1.094 ; 2.534
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1717 ; 1.094 ; 2.534
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1334 ; 0.619 ; 1.787
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1334 ; 0.619 ; 1.787
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1976 ; 1.065 ; 2.646
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3149 ; 3.598 ;13.964
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3052 ; 3.146 ;13.620
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 : NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5YAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300004950.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6500
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53162
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 42.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
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) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.60400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
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: 5YAE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE TRIHYDRATE,
REMARK 280 SODIUM CACODYLATE TRIHYDRATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 26.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.58500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.58500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.42500
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: 530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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 191 -121.82 55.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YAE RELATED DB: PDB
REMARK 900 5YAE IS USED AS A SEARCH MODEL FOR THE MOLECULAR REPLACEMENT
DBREF1 5YAL A 1 342 UNP A0A0M4UW33_STRCJ
DBREF2 5YAL A A0A0M4UW33 42 383
SEQADV 5YAL ALA A 8 UNP A0A0M4UW3 PRO 49 ENGINEERED MUTATION
SEQRES 1 A 342 ALA THR ALA GLY GLN GLU VAL ALA ALA PRO ALA THR ARG
SEQRES 2 A 342 ILE PRO LEU GLY THR LYS THR LEU HIS LEU VAL ASP ALA
SEQRES 3 A 342 SER ARG GLN ASP PRO TRP LYS PRO SER ALA GLY ASN ARG
SEQRES 4 A 342 GLU LEU MET VAL THR LEU TRP TYR PRO SER LEU PRO SER
SEQRES 5 A 342 ARG GLU PRO ALA ALA PRO TYR VAL SER LYS PRO LEU SER
SEQRES 6 A 342 ARG ALA VAL LEU GLY ASN ASP VAL LEU ALA GLY VAL ARG
SEQRES 7 A 342 THR HIS ALA VAL ALA GLY ALA ARG PRO ALA PRO VAL PRO
SEQRES 8 A 342 ARG PRO LEU VAL VAL LEU SER PRO GLY PHE GLY MET SER
SEQRES 9 A 342 ARG ILE THR LEU THR ALA LEU GLY GLU ASP LEU ALA SER
SEQRES 10 A 342 ARG GLY TYR ALA VAL ALA ALA VAL ASP HIS THR TYR GLU
SEQRES 11 A 342 ALA PRO VAL GLU PHE PRO GLY GLY ARG ILE GLU LYS CYS
SEQRES 12 A 342 THR LEU CYS ASP ASP SER ARG MET ASP PRO GLY ALA VAL
SEQRES 13 A 342 VAL ARG ASN ARG ALA LYS ASP LEU ARG PHE VAL LEU ASP
SEQRES 14 A 342 ARG LEU THR GLY PRO GLY SER GLU LEU ARG VAL ASP ALA
SEQRES 15 A 342 ARG ARG ILE GLY VAL ALA GLY HIS SER ILE GLY GLY ALA
SEQRES 16 A 342 SER ALA VAL GLU VAL MET ARG GLU ASP ARG ARG VAL ASP
SEQRES 17 A 342 ALA ALA ILE ASN LEU ASP GLY ASN PHE PHE THR GLU PRO
SEQRES 18 A 342 PRO ALA GLU GLY LEU ASN LYS PRO VAL LEU LEU LEU GLY
SEQRES 19 A 342 ALA ARG ARG SER GLY LEU PRO GLU PRO GLN GLU ASN TRP
SEQRES 20 A 342 GLU ARG ALA TRP LYS GLN LEU THR GLY TRP LYS ARG TRP
SEQRES 21 A 342 LEU ASP VAL PRO ALA GLY GLY HIS MET THR PHE THR ASP
SEQRES 22 A 342 VAL PRO TRP ILE VAL ASP ARG PHE GLY MET PRO GLY GLN
SEQRES 23 A 342 ILE PRO PRO GLU GLN VAL GLU GLY GLN LEU GLY THR VAL
SEQRES 24 A 342 SER ALA ALA ARG ALA THR ALA VAL THR ARG ASN TYR VAL
SEQRES 25 A 342 ALA ALA PHE PHE ASP ARG HIS LEU ARG GLY ARG PRO SER
SEQRES 26 A 342 PRO LEU LEU ASP ARG PRO SER SER ALA HIS PRO GLU VAL
SEQRES 27 A 342 THR PHE MET LYS
HET NA A 401 1
HET ACT A 402 4
HET GOL A 403 6
HETNAM NA SODIUM ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NA NA 1+
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *223(H2 O)
HELIX 1 AA1 LYS A 33 ALA A 36 5 4
HELIX 2 AA2 SER A 61 GLY A 70 1 10
HELIX 3 AA3 ASP A 72 VAL A 77 5 6
HELIX 4 AA4 SER A 104 THR A 107 5 4
HELIX 5 AA5 LEU A 108 ARG A 118 1 11
HELIX 6 AA6 PRO A 136 GLY A 138 5 3
HELIX 7 AA7 CYS A 143 ASP A 148 1 6
HELIX 8 AA8 ASP A 152 GLY A 173 1 22
HELIX 9 AA9 SER A 191 ASP A 204 1 14
HELIX 10 AB1 ARG A 237 GLY A 239 5 3
HELIX 11 AB2 LEU A 240 GLN A 253 1 14
HELIX 12 AB3 GLY A 267 THR A 272 5 6
HELIX 13 AB4 ASP A 273 GLY A 282 1 10
HELIX 14 AB5 PRO A 288 GLU A 290 5 3
HELIX 15 AB6 GLN A 291 LEU A 296 1 6
HELIX 16 AB7 SER A 300 ARG A 321 1 22
HELIX 17 AB8 SER A 325 ASP A 329 5 5
SHEET 1 AA110 VAL A 82 ALA A 83 0
SHEET 2 AA110 LEU A 16 GLN A 29 1 N LEU A 16 O VAL A 82
SHEET 3 AA110 ASN A 38 PRO A 48 -1 O ARG A 39 N ASP A 25
SHEET 4 AA110 ALA A 121 HIS A 127 -1 O ASP A 126 N MET A 42
SHEET 5 AA110 ARG A 92 SER A 98 1 N LEU A 97 O ALA A 123
SHEET 6 AA110 VAL A 180 HIS A 190 1 O GLY A 186 N LEU A 94
SHEET 7 AA110 ALA A 209 LEU A 213 1 O LEU A 213 N GLY A 189
SHEET 8 AA110 VAL A 230 ALA A 235 1 O LEU A 231 N ASN A 212
SHEET 9 AA110 LYS A 258 VAL A 263 1 O LEU A 261 N LEU A 232
SHEET 10 AA110 THR A 339 PHE A 340 -1 O THR A 339 N ASP A 262
SHEET 1 AA2 2 VAL A 133 GLU A 134 0
SHEET 2 AA2 2 ILE A 140 GLU A 141 -1 O GLU A 141 N VAL A 133
SSBOND 1 CYS A 143 CYS A 146 1555 1555 2.04
LINK NA NA A 401 O HOH A 513 1555 1555 2.60
SITE 1 AC1 3 PHE A 101 SER A 191 HOH A 513
SITE 1 AC2 6 ASN A 38 PHE A 217 THR A 219 ASN A 246
SITE 2 AC2 6 ARG A 249 HOH A 605
SITE 1 AC3 10 GLU A 54 ALA A 56 HIS A 80 THR A 298
SITE 2 AC3 10 SER A 300 ARG A 303 HOH A 505 HOH A 516
SITE 3 AC3 10 HOH A 519 HOH A 522
CRYST1 52.900 70.850 87.170 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 0.018904 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011472 0.00000
TER 2630 LYS A 342
MASTER 274 0 3 17 12 0 6 6 2844 1 14 27
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