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HEADER HYDROLASE 26-MAR-24 8YTV
TITLE THE M19 VARIANT OF MIPA-PETASE FROM MICROMONOSPORA PATTALOONGENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RECOMBINANT MIPA-P-M19 VARIANT;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA PATTALOONGENSIS;
SOURCE 3 ORGANISM_TAXID: 405436;
SOURCE 4 GENE: SAMN05444365_106119;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA GAMI-B
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HONG,H.SEO,J.PARK,K.-J.KIM
REVDAT 1 15-JAN-25 8YTV 0
JRNL AUTH H.SEO,H.HONG,J.PARK,S.H.LEE,D.KI,A.RYU,H.Y.SAGONG,K.J.KIM
JRNL TITL LANDSCAPE PROFILING OF PET DEPOLYMERASES USING A NATURAL
JRNL TITL 2 SEQUENCE CLUSTER FRAMEWORK.
JRNL REF SCIENCE V. 387 P5637 2025
JRNL REFN ESSN 1095-9203
JRNL PMID 39745946
JRNL DOI 10.1126/SCIENCE.ADP5637
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0411
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 35259
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1928
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) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2533
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3440
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3736
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.28000
REMARK 3 B22 (A**2) : -2.99000
REMARK 3 B33 (A**2) : 4.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.647
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3924 ; 0.006 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 3536 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5369 ; 1.290 ; 1.638
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8120 ; 0.427 ; 1.561
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 516 ; 7.311 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 31 ; 9.107 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 543 ;13.241 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 579 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4799 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 981 ; 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): 2052 ; 2.378 ; 3.167
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2052 ; 2.378 ; 3.167
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2572 ; 3.405 ; 5.685
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2573 ; 3.404 ; 5.685
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1872 ; 3.344 ; 3.477
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1871 ; 3.338 ; 3.475
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2798 ; 4.902 ; 6.259
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4440 ; 6.671 ;32.720
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4423 ; 6.664 ;32.430
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
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 8YTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300046369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JAN-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DCM SI (111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35259
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 42.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PET3350, CITRIC ACID, BIS-TRIS
REMARK 280 PROPANE, PH 6.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 25.67950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 38
REMARK 465 ALA A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 ALA A 42
REMARK 465 SER A 43
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 465 HIS A 302
REMARK 465 MET B 38
REMARK 465 ALA B 39
REMARK 465 PRO B 40
REMARK 465 PRO B 41
REMARK 465 ALA B 42
REMARK 465 SER B 43
REMARK 465 ALA B 44
REMARK 465 THR B 45
REMARK 465 GLN B 46
REMARK 465 ARG B 47
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
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 O HOH B 436 O HOH B 439 1.88
REMARK 500 SG CYS B 203 O HOH B 429 2.15
REMARK 500 O HOH B 431 O HOH B 443 2.16
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 168 -120.20 66.48
REMARK 500 HIS A 222 -75.46 -114.95
REMARK 500 SER B 168 -118.43 68.25
REMARK 500 HIS B 222 -80.97 -133.71
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 110 0.10 SIDE CHAIN
REMARK 500 ARG A 134 0.11 SIDE CHAIN
REMARK 500 ARG B 134 0.10 SIDE CHAIN
REMARK 500 ARG B 265 0.11 SIDE CHAIN
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 B 461 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B 462 DISTANCE = 7.88 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8YTU RELATED DB: PDB
DBREF1 8YTV A 39 294 UNP A0A1H3QT72_9ACTN
DBREF2 8YTV A A0A1H3QT72 39 294
DBREF1 8YTV B 39 294 UNP A0A1H3QT72_9ACTN
DBREF2 8YTV B A0A1H3QT72 39 294
SEQADV 8YTV MET A 38 UNP A0A1H3QT7 INITIATING METHIONINE
SEQADV 8YTV GLN A 46 UNP A0A1H3QT7 GLU 46 VARIANT
SEQADV 8YTV CYS A 49 UNP A0A1H3QT7 LEU 49 VARIANT
SEQADV 8YTV CYS A 61 UNP A0A1H3QT7 SER 61 VARIANT
SEQADV 8YTV GLN A 67 UNP A0A1H3QT7 ALA 67 VARIANT
SEQADV 8YTV ALA A 90 UNP A0A1H3QT7 PRO 90 VARIANT
SEQADV 8YTV THR A 147 UNP A0A1H3QT7 SER 147 VARIANT
SEQADV 8YTV CYS A 179 UNP A0A1H3QT7 ASP 179 VARIANT
SEQADV 8YTV LYS A 197 UNP A0A1H3QT7 THR 197 VARIANT
SEQADV 8YTV CYS A 198 UNP A0A1H3QT7 SER 198 VARIANT
SEQADV 8YTV CYS A 201 UNP A0A1H3QT7 ARG 201 VARIANT
SEQADV 8YTV CYS A 203 UNP A0A1H3QT7 THR 203 VARIANT
SEQADV 8YTV THR A 215 UNP A0A1H3QT7 GLY 215 VARIANT
SEQADV 8YTV GLN A 221 UNP A0A1H3QT7 SER 221 VARIANT
SEQADV 8YTV GLN A 228 UNP A0A1H3QT7 THR 228 VARIANT
SEQADV 8YTV CYS A 229 UNP A0A1H3QT7 GLY 229 VARIANT
SEQADV 8YTV CYS A 231 UNP A0A1H3QT7 ALA 231 VARIANT
SEQADV 8YTV CYS A 241 UNP A0A1H3QT7 ALA 241 VARIANT
SEQADV 8YTV ASP A 251 UNP A0A1H3QT7 ALA 251 VARIANT
SEQADV 8YTV CYS A 286 UNP A0A1H3QT7 SER 286 VARIANT
SEQADV 8YTV LEU A 295 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV GLU A 296 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS A 297 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS A 298 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS A 299 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS A 300 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS A 301 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS A 302 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV MET B 38 UNP A0A1H3QT7 INITIATING METHIONINE
SEQADV 8YTV GLN B 46 UNP A0A1H3QT7 GLU 46 VARIANT
SEQADV 8YTV CYS B 49 UNP A0A1H3QT7 LEU 49 VARIANT
SEQADV 8YTV CYS B 61 UNP A0A1H3QT7 SER 61 VARIANT
SEQADV 8YTV GLN B 67 UNP A0A1H3QT7 ALA 67 VARIANT
SEQADV 8YTV ALA B 90 UNP A0A1H3QT7 PRO 90 VARIANT
SEQADV 8YTV THR B 147 UNP A0A1H3QT7 SER 147 VARIANT
SEQADV 8YTV CYS B 179 UNP A0A1H3QT7 ASP 179 VARIANT
SEQADV 8YTV LYS B 197 UNP A0A1H3QT7 THR 197 VARIANT
SEQADV 8YTV CYS B 198 UNP A0A1H3QT7 SER 198 VARIANT
SEQADV 8YTV CYS B 201 UNP A0A1H3QT7 ARG 201 VARIANT
SEQADV 8YTV CYS B 203 UNP A0A1H3QT7 THR 203 VARIANT
SEQADV 8YTV THR B 215 UNP A0A1H3QT7 GLY 215 VARIANT
SEQADV 8YTV GLN B 221 UNP A0A1H3QT7 SER 221 VARIANT
SEQADV 8YTV GLN B 228 UNP A0A1H3QT7 THR 228 VARIANT
SEQADV 8YTV CYS B 229 UNP A0A1H3QT7 GLY 229 VARIANT
SEQADV 8YTV CYS B 231 UNP A0A1H3QT7 ALA 231 VARIANT
SEQADV 8YTV CYS B 241 UNP A0A1H3QT7 ALA 241 VARIANT
SEQADV 8YTV ASP B 251 UNP A0A1H3QT7 ALA 251 VARIANT
SEQADV 8YTV CYS B 286 UNP A0A1H3QT7 SER 286 VARIANT
SEQADV 8YTV LEU B 295 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV GLU B 296 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS B 297 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS B 298 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS B 299 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS B 300 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS B 301 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTV HIS B 302 UNP A0A1H3QT7 EXPRESSION TAG
SEQRES 1 A 265 MET ALA PRO PRO ALA SER ALA THR GLN ARG GLY CYS ALA
SEQRES 2 A 265 PRO THR ALA ALA ASN ILE THR GLY ASP GLY CYS TYR GLY
SEQRES 3 A 265 VAL VAL SER GLN THR ILE THR GLY ALA SER GLY PHE GLY
SEQRES 4 A 265 GLY GLY VAL VAL TYR TYR PRO ASN ALA THR GLU ARG PHE
SEQRES 5 A 265 ALA VAL VAL ALA ILE SER PRO GLY TYR THR GLU ARG TRP
SEQRES 6 A 265 SER SER PHE ALA TRP LEU GLY ARG ARG LEU ALA SER TRP
SEQRES 7 A 265 GLY PHE VAL VAL VAL GLY ILE GLU THR ASN SER LEU PHE
SEQRES 8 A 265 ASP GLN PRO ASN SER ARG GLY THR GLN LEU LEU ARG ALA
SEQRES 9 A 265 LEU ASP TRP ALA SER THR SER ALA PRO ALA ALA VAL ARG
SEQRES 10 A 265 ASP ARG VAL ASP ALA THR ARG GLN GLY VAL SER GLY HIS
SEQRES 11 A 265 SER MET GLY GLY GLY GLY THR LEU SER ALA MET CYS GLN
SEQRES 12 A 265 ARG PRO SER VAL ARG ALA GLY VAL PRO LEU ALA PRO TRP
SEQRES 13 A 265 HIS THR THR LYS CYS TRP PRO CYS VAL CYS ASN PRO VAL
SEQRES 14 A 265 MET ILE LEU GLY GLY GLN ASN ASP THR ILE ALA PRO VAL
SEQRES 15 A 265 SER GLN HIS ALA ILE PRO MET TYR GLN CYS VAL CYS SER
SEQRES 16 A 265 GLY GLU LYS ALA TYR VAL GLU LEU CYS GLY ALA GLY HIS
SEQRES 17 A 265 ASN PHE PRO ASN SER ASP ASN PRO ILE VAL SER ARG ALA
SEQRES 18 A 265 ALA VAL SER TRP PHE LYS ARG PHE LEU ASP ASP ASP THR
SEQRES 19 A 265 ARG PHE ALA PRO PHE ALA CYS ASP PHE GLY GLY ALA SER
SEQRES 20 A 265 ILE CYS GLN PHE ARG SER THR CYS PRO VAL LEU GLU HIS
SEQRES 21 A 265 HIS HIS HIS HIS HIS
SEQRES 1 B 265 MET ALA PRO PRO ALA SER ALA THR GLN ARG GLY CYS ALA
SEQRES 2 B 265 PRO THR ALA ALA ASN ILE THR GLY ASP GLY CYS TYR GLY
SEQRES 3 B 265 VAL VAL SER GLN THR ILE THR GLY ALA SER GLY PHE GLY
SEQRES 4 B 265 GLY GLY VAL VAL TYR TYR PRO ASN ALA THR GLU ARG PHE
SEQRES 5 B 265 ALA VAL VAL ALA ILE SER PRO GLY TYR THR GLU ARG TRP
SEQRES 6 B 265 SER SER PHE ALA TRP LEU GLY ARG ARG LEU ALA SER TRP
SEQRES 7 B 265 GLY PHE VAL VAL VAL GLY ILE GLU THR ASN SER LEU PHE
SEQRES 8 B 265 ASP GLN PRO ASN SER ARG GLY THR GLN LEU LEU ARG ALA
SEQRES 9 B 265 LEU ASP TRP ALA SER THR SER ALA PRO ALA ALA VAL ARG
SEQRES 10 B 265 ASP ARG VAL ASP ALA THR ARG GLN GLY VAL SER GLY HIS
SEQRES 11 B 265 SER MET GLY GLY GLY GLY THR LEU SER ALA MET CYS GLN
SEQRES 12 B 265 ARG PRO SER VAL ARG ALA GLY VAL PRO LEU ALA PRO TRP
SEQRES 13 B 265 HIS THR THR LYS CYS TRP PRO CYS VAL CYS ASN PRO VAL
SEQRES 14 B 265 MET ILE LEU GLY GLY GLN ASN ASP THR ILE ALA PRO VAL
SEQRES 15 B 265 SER GLN HIS ALA ILE PRO MET TYR GLN CYS VAL CYS SER
SEQRES 16 B 265 GLY GLU LYS ALA TYR VAL GLU LEU CYS GLY ALA GLY HIS
SEQRES 17 B 265 ASN PHE PRO ASN SER ASP ASN PRO ILE VAL SER ARG ALA
SEQRES 18 B 265 ALA VAL SER TRP PHE LYS ARG PHE LEU ASP ASP ASP THR
SEQRES 19 B 265 ARG PHE ALA PRO PHE ALA CYS ASP PHE GLY GLY ALA SER
SEQRES 20 B 265 ILE CYS GLN PHE ARG SER THR CYS PRO VAL LEU GLU HIS
SEQRES 21 B 265 HIS HIS HIS HIS HIS
FORMUL 3 HOH *183(H2 O)
HELIX 1 AA1 ARG A 101 SER A 104 5 4
HELIX 2 AA2 PHE A 105 TRP A 115 1 11
HELIX 3 AA3 GLN A 130 SER A 148 1 19
HELIX 4 AA4 PRO A 150 ASP A 155 1 6
HELIX 5 AA5 SER A 168 ARG A 181 1 14
HELIX 6 AA6 HIS A 222 VAL A 230 1 9
HELIX 7 AA7 ASN A 246 SER A 250 5 5
HELIX 8 AA8 ASN A 252 ASP A 268 1 17
HELIX 9 AA9 ASP A 270 ARG A 272 5 3
HELIX 10 AB1 PHE A 273 CYS A 278 1 6
HELIX 11 AB2 ALA B 54 GLY B 58 5 5
HELIX 12 AB3 ARG B 101 SER B 104 5 4
HELIX 13 AB4 PHE B 105 SER B 114 1 10
HELIX 14 AB5 GLN B 130 SER B 148 1 19
HELIX 15 AB6 PRO B 150 ASP B 155 1 6
HELIX 16 AB7 SER B 168 ARG B 181 1 14
HELIX 17 AB8 HIS B 222 CYS B 229 1 8
HELIX 18 AB9 ASN B 252 ASP B 268 1 17
HELIX 19 AC1 ASP B 270 ARG B 272 5 3
HELIX 20 AC2 PHE B 273 ASP B 279 1 7
SHEET 1 AA1 6 VAL A 64 THR A 68 0
SHEET 2 AA1 6 GLY A 78 PRO A 83 -1 O TYR A 82 N VAL A 65
SHEET 3 AA1 6 VAL A 118 ILE A 122 -1 O VAL A 119 N TYR A 81
SHEET 4 AA1 6 PHE A 89 SER A 95 1 N VAL A 92 O VAL A 120
SHEET 5 AA1 6 VAL A 157 HIS A 167 1 O ASP A 158 N PHE A 89
SHEET 6 AA1 6 ALA A 186 LEU A 190 1 O LEU A 190 N GLY A 166
SHEET 1 AA2 3 VAL A 206 GLY A 211 0
SHEET 2 AA2 3 LYS A 235 LEU A 240 1 O LEU A 240 N GLY A 210
SHEET 3 AA2 3 ILE A 285 SER A 290 -1 O GLN A 287 N GLU A 239
SHEET 1 AA3 6 VAL B 64 THR B 68 0
SHEET 2 AA3 6 GLY B 77 PRO B 83 -1 O VAL B 80 N GLN B 67
SHEET 3 AA3 6 VAL B 118 GLU B 123 -1 O GLY B 121 N VAL B 79
SHEET 4 AA3 6 PHE B 89 SER B 95 1 N ILE B 94 O VAL B 120
SHEET 5 AA3 6 VAL B 157 HIS B 167 1 O ASP B 158 N PHE B 89
SHEET 6 AA3 6 ALA B 186 LEU B 190 1 O LEU B 190 N GLY B 166
SHEET 1 AA4 3 VAL B 206 GLY B 211 0
SHEET 2 AA4 3 LYS B 235 LEU B 240 1 O ALA B 236 N ILE B 208
SHEET 3 AA4 3 ILE B 285 SER B 290 -1 O ARG B 289 N TYR B 237
SSBOND 1 CYS A 49 CYS A 61 1555 1555 2.13
SSBOND 2 CYS A 179 CYS A 201 1555 1555 2.07
SSBOND 3 CYS A 198 CYS A 229 1555 1555 2.10
SSBOND 4 CYS A 203 CYS A 231 1555 1555 2.12
SSBOND 5 CYS A 241 CYS A 286 1555 1555 2.51
SSBOND 6 CYS A 278 CYS A 292 1555 1555 2.10
SSBOND 7 CYS B 179 CYS B 201 1555 1555 2.08
SSBOND 8 CYS B 198 CYS B 229 1555 1555 2.07
SSBOND 9 CYS B 203 CYS B 231 1555 1555 2.08
SSBOND 10 CYS B 241 CYS B 286 1555 1555 2.61
SSBOND 11 CYS B 278 CYS B 292 1555 1555 2.08
CRYST1 42.619 51.359 107.654 90.00 94.33 90.00 P 1 21 1 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 0.023464 0.000000 0.001777 0.00000
SCALE2 0.000000 0.019471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009316 0.00000
TER 1922 GLU A 296
TER 3803 GLU B 296
MASTER 337 0 0 20 18 0 0 6 3919 2 23 42
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