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HEADER HYDROLASE 29-JUN-25 9VMR
TITLE CRYSTAL STRUCTURE OF PHTHALATE HYDROLASE ESTJ6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PHTHALIC ACID ESTERS, BIOREMEDIATION, BIFUNCTIONAL HYDROLASE,
KEYWDS 2 PLASTICIZER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.WANG,Y.B.CHEN,R.K.HU
REVDAT 1 08-JUL-26 9VMR 0
JRNL AUTH Y.H.WANG,Y.B.CHEN,R.K.HU
JRNL TITL STRUCTURAL OF BIFUNCTIONAL PHTHALATE HYDROLASE ESTJ6 AT 1.8
JRNL TITL 2 ANGSTROMS RESOLUTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 35923
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1876
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2581
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.26000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : -0.82000
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): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.084
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.900
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2223 ; 0.011 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2165 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3023 ; 1.828 ; 1.807
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5003 ; 0.646 ; 1.744
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 293 ; 5.745 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 11 ; 7.015 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 359 ;14.309 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 341 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2612 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 450 ; 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): 1175 ; 2.149 ; 2.263
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1175 ; 2.149 ; 2.262
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1467 ; 2.702 ; 4.058
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1468 ; 2.708 ; 4.060
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1048 ; 4.011 ; 2.677
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1049 ; 4.009 ; 2.677
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1557 ; 5.897 ; 4.678
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2649 ; 7.198 ;23.870
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2521 ; 6.796 ;21.920
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 9VMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 30-JUN-25.
REMARK 100 THE DEPOSITION ID IS D_1300061012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-22
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 : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37718
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.4500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 11.80
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 MOL/L (NH4)2SO4, 0.1 MOL/L HEPES
REMARK 280 (PH 6.6), AND 0.5% (W/V) PEG 8000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.98450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.98450
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.14850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.43050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.14850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.43050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.98450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.14850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.43050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.98450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.14850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.43050
REMARK 290 SMTRY3 8 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 690 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 694 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 722 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 726 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 ALA A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
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 A 537 O HOH A 691 2.02
REMARK 500 O HOH A 539 O HOH A 647 2.13
REMARK 500 O HOH A 571 O HOH A 645 2.14
REMARK 500 O HOH A 473 O HOH A 681 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 25 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 LEU A 229 CB - CG - CD1 ANGL. DEV. = 10.4 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 146 -120.08 61.49
REMARK 500 VAL A 195 -39.19 -138.08
REMARK 500 ALA A 239 58.95 -92.58
REMARK 500 GLU A 267 -2.76 67.20
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 731 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 732 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A 733 DISTANCE = 6.39 ANGSTROMS
DBREF1 9VMR A 1 298 UNP A0A4P8L7K3_9ZZZZ
DBREF2 9VMR A A0A4P8L7K3 1 298
SEQADV 9VMR HIS A 299 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMR HIS A 300 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMR HIS A 301 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMR HIS A 302 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMR HIS A 303 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMR HIS A 304 UNP A0A4P8L7K EXPRESSION TAG
SEQRES 1 A 304 MET ALA SER PRO GLN LEU GLN MET ALA LEU ASP ALA PHE
SEQRES 2 A 304 LYS THR MET GLY GLU LYS MET ALA GLN ALA GLY ASN ASP
SEQRES 3 A 304 VAL LYS ALA LEU ARG ALA VAL MET GLU GLU MET SER GLY
SEQRES 4 A 304 PHE PRO SER ALA GLY GLU THR LYS CYS THR PRO VAL ASN
SEQRES 5 A 304 ALA GLY GLY VAL PRO ALA GLU TRP ILE SER GLY PRO GLY
SEQRES 6 A 304 ALA ALA ASP ASP ARG VAL ILE LEU TYR VAL HIS GLY GLY
SEQRES 7 A 304 GLY TYR VAL MET GLY SER ILE ALA THR HIS ARG GLU THR
SEQRES 8 A 304 VAL ALA ARG LEU SER LYS ALA SER GLY ALA ARG GLY LEU
SEQRES 9 A 304 ALA LEU ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO
SEQRES 10 A 304 ALA ALA VAL ASP ASP ALA THR ALA ALA TYR ARG TRP LEU
SEQRES 11 A 304 LEU SER GLN ASN ILE LYS PRO ALA HIS ILE VAL ILE ALA
SEQRES 12 A 304 GLY ASP SER ALA GLY GLY GLY LEU THR LEU ALA THR LEU
SEQRES 13 A 304 ILE ALA LEU ARG ASP ALA LYS VAL PRO LEU PRO ALA ALA
SEQRES 14 A 304 GLY VAL CYS ILE SER PRO TRP THR ASP MET GLU GLY ALA
SEQRES 15 A 304 GLY GLU SER MET THR THR ARG ALA LYS ALA ASP PRO VAL
SEQRES 16 A 304 VAL GLN LYS GLN GLY LEU LEU GLY MET ALA GLN LEU TYR
SEQRES 17 A 304 LEU GLY GLY LYS ASP PRO LYS SER PRO LEU ALA ALA PRO
SEQRES 18 A 304 LEU HIS ALA ASN LEU ALA GLY LEU PRO PRO LEU LEU ILE
SEQRES 19 A 304 GLN VAL GLY ASP ALA GLU THR LEU LEU ASP ASP SER ILE
SEQRES 20 A 304 ARG VAL ALA GLU LYS ALA LYS LYS ALA GLY VAL LYS VAL
SEQRES 21 A 304 ASP LEU GLU VAL TRP PRO GLU MET PRO HIS VAL TRP HIS
SEQRES 22 A 304 LEU PHE ALA PRO PHE LEU PRO GLU GLY GLN GLN ALA ILE
SEQRES 23 A 304 ASP LYS ILE GLY LYS TYR VAL ARG GLN ILE THR ALA HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
FORMUL 2 HOH *333(H2 O)
HELIX 1 AA1 PRO A 4 GLY A 24 1 21
HELIX 2 AA2 ASP A 26 MET A 37 1 12
HELIX 3 AA3 PHE A 40 THR A 46 5 7
HELIX 4 AA4 SER A 84 GLY A 100 1 17
HELIX 5 AA5 PRO A 117 GLN A 133 1 17
HELIX 6 AA6 LYS A 136 ALA A 138 5 3
HELIX 7 AA7 SER A 146 ALA A 162 1 17
HELIX 8 AA8 GLU A 184 ARG A 189 1 6
HELIX 9 AA9 GLN A 197 GLY A 210 1 14
HELIX 10 AB1 ALA A 220 ALA A 224 5 5
HELIX 11 AB2 LEU A 242 ALA A 256 1 15
HELIX 12 AB3 VAL A 271 ALA A 276 5 6
HELIX 13 AB4 LEU A 279 THR A 297 1 19
SHEET 1 AA1 8 LYS A 47 ALA A 53 0
SHEET 2 AA1 8 VAL A 56 SER A 62 -1 O VAL A 56 N ALA A 53
SHEET 3 AA1 8 ALA A 101 LEU A 106 -1 O GLY A 103 N ILE A 61
SHEET 4 AA1 8 ALA A 67 VAL A 75 1 N ILE A 72 O LEU A 104
SHEET 5 AA1 8 ILE A 140 ASP A 145 1 O ALA A 143 N LEU A 73
SHEET 6 AA1 8 ALA A 169 ILE A 173 1 O ILE A 173 N GLY A 144
SHEET 7 AA1 8 LEU A 232 GLY A 237 1 O LEU A 233 N CYS A 172
SHEET 8 AA1 8 VAL A 260 TRP A 265 1 O ASP A 261 N LEU A 232
CISPEP 1 ALA A 111 PRO A 112 0 -1.02
CISPEP 2 PHE A 116 PRO A 117 0 3.56
CRYST1 64.297 120.861 97.969 90.00 90.00 90.00 C 2 2 21 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 0.015553 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010207 0.00000
TER 2175 THR A 297
MASTER 348 0 0 13 8 0 0 6 2507 1 0 24
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