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HEADER HYDROLASE 30-DEC-20 7DS7
TITLE THE CRYSTAL STRUCTURE OF LEAF-BRANCH COMPOST CUTINASE FROM BIORTUS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEAF-BRANCH COMPOST CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LCC,PET-DIGESTING ENZYME,POLY(ETHYLENE TEREPHTHALATE)
COMPND 5 HYDROLASE,PETASE;
COMPND 6 EC: 3.1.1.74,3.1.1.101;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNKNOWN PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CATALYTIC ACTIVITY, HYDROLASE ACTIVITY, ACTING ON ESTER BONDS,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.WANG,Z.LV,W.CHENG,D.LIN,F.CHU,X.XU,J.TAN
REVDAT 1 13-JAN-21 7DS7 0
JRNL AUTH F.WANG,Z.LV,W.CHENG,D.LIN,F.CHU,X.XU,J.TAN
JRNL TITL THE CRYSTAL STRUCTURE OF LEAF-BRANCH COMPOST CUTINASE FROM
JRNL TITL 2 BIORTUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 13144
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.158
REMARK 3 FREE R VALUE TEST SET COUNT : 678
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1948
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.48500
REMARK 3 B12 (A**2) : -0.07500
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): 0.286
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.206
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.606
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2040 ; 0.002 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1812 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2796 ; 1.200 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4196 ; 1.125 ; 1.564
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 263 ; 6.508 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;26.642 ;20.700
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 285 ;10.403 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;12.029 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 272 ; 0.043 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2358 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 450 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 380 ; 0.183 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 35 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 984 ; 0.150 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 135 ; 0.123 ; 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): 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): 1043 ; 0.202 ; 1.052
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1042 ; 0.201 ; 1.051
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1306 ; 0.373 ; 1.575
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1307 ; 0.373 ; 1.576
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 997 ; 0.161 ; 1.105
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 994 ; 0.149 ; 1.098
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1489 ; 0.293 ; 1.648
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1490 ; 0.293 ; 1.651
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 : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7DS7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300019848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13146
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 47.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26200
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: PHASER
REMARK 200 STARTING MODEL: 6THT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6M IMIDAZOLE, 0.1M TRI-SODIUM
REMARK 280 CITRATE PH7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 17.56850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.56850
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.56850
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: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 MET A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 HIS A 21
REMARK 465 HIS A 22
REMARK 465 HIS A 23
REMARK 465 HIS A 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 GLU A 27
REMARK 465 ASN A 28
REMARK 465 LEU A 29
REMARK 465 TYR A 30
REMARK 465 PHE A 31
REMARK 465 GLN A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 GLY A 35
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 145 21.49 -142.03
REMARK 500 ALA A 165 -118.38 64.34
REMARK 500 THR A 188 59.16 30.88
REMARK 500 ALA A 209 34.83 -99.64
REMARK 500 HIS A 218 -86.75 -123.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7DS7 A 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 7DS7 MET A 17 UNP G9BY57 INITIATING METHIONINE
SEQADV 7DS7 GLY A 18 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 SER A 19 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 SER A 20 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 HIS A 21 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 HIS A 22 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 HIS A 23 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 HIS A 24 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 HIS A 25 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 HIS A 26 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 GLU A 27 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 ASN A 28 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 LEU A 29 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 TYR A 30 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 PHE A 31 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 GLN A 32 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 GLY A 33 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 GLY A 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 GLY A 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7DS7 GLY A 127 UNP G9BY57 TYR 127 ENGINEERED MUTATION
SEQADV 7DS7 ALA A 165 UNP G9BY57 SER 165 ENGINEERED MUTATION
SEQADV 7DS7 CYS A 238 UNP G9BY57 ASP 238 ENGINEERED MUTATION
SEQADV 7DS7 ILE A 243 UNP G9BY57 PHE 243 ENGINEERED MUTATION
SEQADV 7DS7 CYS A 283 UNP G9BY57 SER 283 ENGINEERED MUTATION
SEQRES 1 A 277 MET GLY SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 A 277 TYR PHE GLN GLY GLY GLY SER ASN PRO TYR GLN ARG GLY
SEQRES 3 A 277 PRO ASN PRO THR ARG SER ALA LEU THR ALA ASP GLY PRO
SEQRES 4 A 277 PHE SER VAL ALA THR TYR THR VAL SER ARG LEU SER VAL
SEQRES 5 A 277 SER GLY PHE GLY GLY GLY VAL ILE TYR TYR PRO THR GLY
SEQRES 6 A 277 THR SER LEU THR PHE GLY GLY ILE ALA MET SER PRO GLY
SEQRES 7 A 277 TYR THR ALA ASP ALA SER SER LEU ALA TRP LEU GLY ARG
SEQRES 8 A 277 ARG LEU ALA SER HIS GLY PHE VAL VAL LEU VAL ILE ASN
SEQRES 9 A 277 THR ASN SER ARG PHE ASP GLY PRO ASP SER ARG ALA SER
SEQRES 10 A 277 GLN LEU SER ALA ALA LEU ASN TYR LEU ARG THR SER SER
SEQRES 11 A 277 PRO SER ALA VAL ARG ALA ARG LEU ASP ALA ASN ARG LEU
SEQRES 12 A 277 ALA VAL ALA GLY HIS ALA MET GLY GLY GLY GLY THR LEU
SEQRES 13 A 277 ARG ILE ALA GLU GLN ASN PRO SER LEU LYS ALA ALA VAL
SEQRES 14 A 277 PRO LEU THR PRO TRP HIS THR ASP LYS THR PHE ASN THR
SEQRES 15 A 277 SER VAL PRO VAL LEU ILE VAL GLY ALA GLU ALA ASP THR
SEQRES 16 A 277 VAL ALA PRO VAL SER GLN HIS ALA ILE PRO PHE TYR GLN
SEQRES 17 A 277 ASN LEU PRO SER THR THR PRO LYS VAL TYR VAL GLU LEU
SEQRES 18 A 277 CYS ASN ALA SER HIS ILE ALA PRO ASN SER ASN ASN ALA
SEQRES 19 A 277 ALA ILE SER VAL TYR THR ILE SER TRP MET LYS LEU TRP
SEQRES 20 A 277 VAL ASP ASN ASP THR ARG TYR ARG GLN PHE LEU CYS ASN
SEQRES 21 A 277 VAL ASN ASP PRO ALA LEU CYS ASP PHE ARG THR ASN ASN
SEQRES 22 A 277 ARG HIS CYS GLN
HET IMD A 301 5
HET GOL A 302 6
HET CIT A 303 13
HETNAM IMD IMIDAZOLE
HETNAM GOL GLYCEROL
HETNAM CIT CITRIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IMD C3 H5 N2 1+
FORMUL 3 GOL C3 H8 O3
FORMUL 4 CIT C6 H8 O7
FORMUL 5 HOH *114(H2 O)
HELIX 1 AA1 ARG A 47 ALA A 52 5 6
HELIX 2 AA2 SER A 64 VAL A 68 5 5
HELIX 3 AA3 ASP A 98 SER A 101 5 4
HELIX 4 AA4 LEU A 102 HIS A 112 1 11
HELIX 5 AA5 GLY A 127 SER A 145 1 19
HELIX 6 AA6 PRO A 147 ARG A 153 1 7
HELIX 7 AA7 ALA A 165 ASN A 178 1 14
HELIX 8 AA8 HIS A 218 LEU A 226 1 9
HELIX 9 AA9 ILE A 243 SER A 247 5 5
HELIX 10 AB1 ASN A 249 ASP A 265 1 17
HELIX 11 AB2 ASP A 267 LEU A 274 5 8
HELIX 12 AB3 ASN A 289 GLN A 293 5 5
SHEET 1 AA1 6 SER A 57 VAL A 63 0
SHEET 2 AA1 6 GLY A 74 THR A 80 -1 O GLY A 74 N VAL A 63
SHEET 3 AA1 6 VAL A 115 ILE A 119 -1 O VAL A 116 N TYR A 77
SHEET 4 AA1 6 PHE A 86 SER A 92 1 N MET A 91 O LEU A 117
SHEET 5 AA1 6 LEU A 154 HIS A 164 1 O ASP A 155 N PHE A 86
SHEET 6 AA1 6 ALA A 184 LEU A 187 1 O LEU A 187 N GLY A 163
SHEET 1 AA2 3 VAL A 202 ALA A 207 0
SHEET 2 AA2 3 LYS A 232 LEU A 237 1 O VAL A 235 N GLY A 206
SHEET 3 AA2 3 LEU A 282 THR A 287 -1 O ARG A 286 N TYR A 234
SSBOND 1 CYS A 238 CYS A 283 1555 1555 2.04
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.03
CRYST1 109.412 109.412 35.137 90.00 90.00 120.00 P 63 6
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 0.009140 0.005277 0.000000 0.00000
SCALE2 0.000000 0.010554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028460 0.00000
TER 1964 GLN A 293
MASTER 295 0 3 12 9 0 0 6 2086 1 28 22
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