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HEADER HYDROLASE 30-MAY-25 9RD2
TITLE CRYSTAL STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE VARIANT (LCC_ICCG)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEAF-BRANCH COMPOST CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LC-CUTINASE,LCC,PET-DIGESTING ENZYME,POLY(ETHYLENE
COMPND 5 TEREPHTHALATE) HYDROLASE,PET 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: UNIDENTIFIED PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, PET-DEGRADING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KOSINAS,K.MAKRYNIOTIS,C.TRANTZAS,E.NIKOLAIVITS,M.DIMAROGONA,
AUTHOR 2 E.TOPAKAS
REVDAT 1 10-JUN-26 9RD2 0
JRNL AUTH C.KOSINAS,K.MAKRYNIOTIS,E.NIKOLAIVITS,M.DIMAROGONA,E.TOPAKAS
JRNL TITL CRYSTAL STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE VARIANT
JRNL TITL 2 (LCC_ICCG)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0419
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 35866
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) : 0.171
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.916
REMARK 3 FREE R VALUE TEST SET COUNT : 1763
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) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2480
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3360
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1939
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 113
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03600
REMARK 3 B22 (A**2) : -0.03600
REMARK 3 B33 (A**2) : 0.07300
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): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.745
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2051 ; 0.010 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1877 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2810 ; 1.797 ; 1.786
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4308 ; 0.640 ; 1.722
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 268 ; 6.964 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 16 ;11.245 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 288 ;11.646 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2519 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 503 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 407 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 26 ; 0.256 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1058 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 104 ; 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): 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): 1051 ; 2.682 ; 2.843
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1051 ; 2.680 ; 2.843
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1320 ; 3.411 ; 5.090
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1321 ; 3.416 ; 5.093
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1000 ; 3.775 ; 3.225
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1001 ; 3.774 ; 3.228
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1488 ; 5.304 ; 5.733
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1489 ; 5.302 ; 5.735
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 9RD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1292147526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-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 : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.7290
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35907
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 47.626
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 25.90
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 47.58
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 17.60
REMARK 200 R MERGE FOR SHELL (I) : 0.06100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM NITRATE, 20% (W/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 36.86900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.04050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.04050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.43450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.04050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.04050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.30350
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.04050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.04050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 18.43450
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.04050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.04050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.30350
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 36.86900
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 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 35
REMARK 465 GLN A 293
REMARK 465 LEU A 294
REMARK 465 GLU A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
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 HG1 THR A 198 H VAL A 200 1.27
REMARK 500 HG1 THR A 287 H ASN A 289 1.27
REMARK 500 HG1 THR A 82 H LEU A 84 1.34
REMARK 500 H ARG A 65 O HOH A 501 1.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE1 TYR A 95 HH TYR A 95 7555 1.21
REMARK 500 CE1 TYR A 95 OH TYR A 95 7555 1.98
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 THR A 96 -4.45 74.95
REMARK 500 SER A 165 -125.33 67.79
REMARK 500 THR A 188 58.85 35.39
REMARK 500 HIS A 218 -85.29 -126.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 131 0.10 SIDE CHAIN
REMARK 500 ARG A 151 0.09 SIDE CHAIN
REMARK 500 ARG A 271 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9RD2 A 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 9RD2 MET A 35 UNP G9BY57 INITIATING METHIONINE
SEQADV 9RD2 GLY A 127 UNP G9BY57 TYR 127 ENGINEERED MUTATION
SEQADV 9RD2 CYS A 238 UNP G9BY57 ASP 238 ENGINEERED MUTATION
SEQADV 9RD2 ILE A 243 UNP G9BY57 PHE 243 ENGINEERED MUTATION
SEQADV 9RD2 CYS A 283 UNP G9BY57 SER 283 ENGINEERED MUTATION
SEQADV 9RD2 LEU A 294 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 GLU A 295 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 HIS A 296 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 HIS A 297 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 HIS A 298 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 HIS A 299 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 HIS A 300 UNP G9BY57 EXPRESSION TAG
SEQADV 9RD2 HIS A 301 UNP G9BY57 EXPRESSION TAG
SEQRES 1 A 267 MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG
SEQRES 2 A 267 SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR
SEQRES 3 A 267 TYR THR VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 A 267 GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE
SEQRES 5 A 267 GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA
SEQRES 6 A 267 SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS
SEQRES 7 A 267 GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE
SEQRES 8 A 267 ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA
SEQRES 9 A 267 LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG
SEQRES 10 A 267 ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 A 267 SER MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN
SEQRES 12 A 267 ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP
SEQRES 13 A 267 HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU
SEQRES 14 A 267 ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER
SEQRES 15 A 267 GLN HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR
SEQRES 16 A 267 THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS
SEQRES 17 A 267 ILE ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR
SEQRES 18 A 267 THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR
SEQRES 19 A 267 ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA
SEQRES 20 A 267 LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
HET IMD A 401 10
HET NO3 A 402 4
HET NO3 A 403 4
HET PEG A 404 17
HET EDO A 405 10
HETNAM IMD IMIDAZOLE
HETNAM NO3 NITRATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 IMD C3 H5 N2 1+
FORMUL 3 NO3 2(N O3 1-)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 EDO C2 H6 O2
FORMUL 7 HOH *113(H2 O)
HELIX 1 AA1 SER A 48 ALA A 52 5 5
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 ALA A 152 1 6
HELIX 7 AA7 SER 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
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 GLY A 87 O VAL A 115
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 2.11
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.05
CRYST1 88.081 88.081 73.738 90.00 90.00 90.00 P 41 21 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 0.011353 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011353 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013562 0.00000
TER 3904 CYS A 292
MASTER 339 0 5 11 9 0 0 6 2076 1 49 21
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