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HEADER HYDROLASE 06-MAR-26 29CU
TITLE CRYSTAL STRUCTURE OF A CUTINASE FROM SACCHAROPOLYSPORA DENDRANTHEMAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA DENDRANTHEMAE;
SOURCE 3 ORGANISM_TAXID: 1181886;
SOURCE 4 GENE: FHU35_111186;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS POLY(ETHYLENE TEREPHTHALATE) HYDROLASE, CUTINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.WAIN,A.R.PICKFORD,S.P.WOOD
REVDAT 1 18-MAR-26 29CU 0
JRNL AUTH B.WAIN,A.R.PICKFORD,K.TORNESAKIS,P.COX,E.RUDGE,F.FIGUEIREDO,
JRNL AUTH 2 S.WOOD
JRNL TITL EXAMINING PETASE ACTIVITY ACROSS A PHYLOGENETIC GENUS:
JRNL TITL 2 INVESTIGATING THERMOSTABILITY AND THE EFFECT OF A SINGLE
JRNL TITL 3 SURFACE-CHARGE-ALTERING SUBSTITUTION ON PET FILM DEGRADATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
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) : 1.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.7
REMARK 3 NUMBER OF REFLECTIONS : 63583
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) : 0.121
REMARK 3 R VALUE (WORKING SET) : 0.120
REMARK 3 FREE R VALUE : 0.144
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3358
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.13
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 714
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 12.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 33
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1912
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.12000
REMARK 3 B22 (A**2) : -1.27000
REMARK 3 B33 (A**2) : 0.15000
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): 0.034
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.958
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2096 ; 0.013 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1879 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2886 ; 1.834 ; 1.814
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4389 ; 0.639 ; 1.736
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 6.341 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 10 ; 7.958 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 302 ;11.221 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 318 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2514 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 432 ; 0.002 ; 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): 1081 ; 3.043 ; 0.795
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1081 ; 3.020 ; 0.795
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1369 ; 4.384 ; 1.432
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1370 ; 4.389 ; 1.436
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1015 ; 4.887 ; 0.992
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1016 ; 4.885 ; 0.992
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1518 ; 6.742 ; 1.745
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2377 ;12.902 ;11.360
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2301 ;11.298 ; 9.770
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3975 ; 4.288 ; 3.000
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 : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 29CU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-26.
REMARK 100 THE DEPOSITION ID IS D_1292149264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-24
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
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 : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67263
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.130
REMARK 200 RESOLUTION RANGE LOW (A) : 50.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.1
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 11.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY SITTING DROP
REMARK 280 VAPOR DIFFUSION AT 4 DEGREES C. DROPS WERE SET UP BY MIXING 1 UL
REMARK 280 OF PROTEIN SOLUTION (10 MG/ML IN Y SODIUM PHOSPHATE BUFFER, PH
REMARK 280 7.5) WITH 1 UL OF RESERVOIR SOLUTION (0.2 M SODIUM FLUORIDE, 20%
REMARK 280 (W/V) PEG 3350, UNBUFFERED). THE DROPS WERE INCUBATED FOR 9
REMARK 280 MONTHS. THE SETUP WAS PERFORMED USING A TTP LABTECH MOSQUITO
REMARK 280 LIQUID HANDLING ROBOT., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277.15K
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 19.25100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.06400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.85350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.06400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.25100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.85350
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 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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 260
REMARK 465 GLU A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
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 GLY A 62 CA
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 99 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
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 SER A 131 -120.94 64.89
REMARK 500 SER A 131 -119.71 64.89
REMARK 500 THR A 154 59.66 34.98
REMARK 500 HIS A 185 -82.52 -124.95
REMARK 500 ALA A 198 130.76 -178.45
REMARK 500 THR A 256 37.84 -96.37
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 676 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 677 DISTANCE = 6.37 ANGSTROMS
DBREF1 29CU A 1 259 UNP A0A561VAE2_9PSEU
DBREF2 29CU A A0A561VAE2 37 295
SEQADV 29CU LEU A 260 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU GLU A 261 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU HIS A 262 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU HIS A 263 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU HIS A 264 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU HIS A 265 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU HIS A 266 UNP A0A561VAE EXPRESSION TAG
SEQADV 29CU HIS A 267 UNP A0A561VAE EXPRESSION TAG
SEQRES 1 A 267 ALA GLU THR ALA ASP VAL HIS GLY PRO ASP PRO THR GLU
SEQRES 2 A 267 GLU SER ILE THR ALA PRO ARG GLY PRO PHE GLU VAL ALA
SEQRES 3 A 267 GLU GLU SER VAL PRO ARG SER SER VAL SER GLY PHE GLY
SEQRES 4 A 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR THR ASP GLY
SEQRES 5 A 267 LEU PHE SER ALA LEU ALA ILE SER PRO GLY PHE THR GLY
SEQRES 6 A 267 PRO GLU GLY SER ILE ALA TRP LEU GLY PRO ARG LEU ALA
SEQRES 7 A 267 SER GLN GLY PHE VAL VAL PHE THR ILE GLU THR ILE THR
SEQRES 8 A 267 LEU THR ASP PRO PRO ASP SER ARG ALA ALA GLN LEU GLN
SEQRES 9 A 267 ALA SER LEU ASP TYR LEU THR ASP ASP SER SER VAL GLN
SEQRES 10 A 267 ASP ARG VAL ASP PRO ASP ARG LEU GLY VAL MET GLY HIS
SEQRES 11 A 267 SER MET GLY GLY GLY GLY SER LEU LYS ALA ALA LEU ASP
SEQRES 12 A 267 ASN PRO ALA LEU LYS ALA VAL VAL PRO LEU THR PRO TRP
SEQRES 13 A 267 HIS THR THR LYS ASP PHE SER GLY VAL THR ALA PRO THR
SEQRES 14 A 267 LEU ILE ILE GLY ALA GLN ASN ASP THR ILE ALA PRO VAL
SEQRES 15 A 267 SER GLU HIS ALA GLU PRO PHE TYR GLU SER LEU PRO ASP
SEQRES 16 A 267 ASP PRO ALA LYS ALA TYR VAL GLU LEU ALA GLY GLU GLY
SEQRES 17 A 267 HIS LEU ALA PRO ILE LEU GLY ASN THR THR LEU ALA LYS
SEQRES 18 A 267 TYR SER ILE ALA TRP ILE LYS ARG PHE LEU ASP GLU ASP
SEQRES 19 A 267 THR ARG TYR ASP GLN PHE LEU CYS PRO PRO PRO GLN ASP
SEQRES 20 A 267 PRO ALA LEU SER ASP TYR ARG SER THR CYS PRO HIS LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
HET GOL A 301 12
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *277(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 PRO A 31 VAL A 35 5 5
HELIX 3 AA3 SER A 69 ALA A 71 5 3
HELIX 4 AA4 TRP A 72 SER A 79 1 8
HELIX 5 AA5 PRO A 95 ASP A 113 1 19
HELIX 6 AA6 SER A 131 ASN A 144 1 14
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 LEU A 210 GLY A 215 1 6
HELIX 9 AA9 ASN A 216 LEU A 231 1 16
HELIX 10 AB1 ASP A 234 LEU A 241 5 8
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O GLY A 41 N VAL A 30
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N LEU A 57 O PHE A 85
SHEET 5 AA1 6 VAL A 120 HIS A 130 1 O ASP A 121 N PHE A 54
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O LEU A 204 N GLY A 173
SHEET 3 AA2 3 LEU A 250 SER A 255 -1 O ARG A 254 N TYR A 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.05
CISPEP 1 ASP A 196 PRO A 197 0 11.49
CISPEP 2 CYS A 242 PRO A 243 0 -4.62
CISPEP 3 CYS A 257 PRO A 258 0 0.09
CRYST1 38.502 61.707 88.128 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 0.025973 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016206 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011347 0.00000
TER 2010 HIS A 259
MASTER 326 0 1 10 9 0 0 6 2195 1 14 21
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