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HEADER HYDROLASE 25-NOV-25 9XV6
TITLE CATALYTIC DOMAIN OF N1363
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C3 CLUSTER PET HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALLORHIZOCOLA RHIZOSPHAERAE;
SOURCE 3 ORGANISM_TAXID: 1872709;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SHUFFLE T7
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HWANG,H.SEO,K.-J.KIM
REVDAT 1 03-JUN-26 9XV6 0
JRNL AUTH H.SEO,H.HWANG,J.PARK,D.KI,W.CHOI,Y.YOON,D.KIM,K.J.KIM
JRNL TITL EFFECT OF SURFACE ELECTROSTATIC POTENTIAL ON PH-ACTIVITY
JRNL TITL 2 PROFILE IN PET DEPOLYMERASES.
JRNL REF J HAZARD MATER V. 511 42179 2026
JRNL REFN ESSN 1873-3336
JRNL PMID 42033830
JRNL DOI 10.1016/J.JHAZMAT.2026.142179
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 45795
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.143
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2187
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1928
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.34000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.039
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.039
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.024
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.570
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2099 ; 0.011 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 1918 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2877 ; 1.786 ; 1.648
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4415 ; 0.617 ; 1.560
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 281 ; 6.470 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 14 ;10.144 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 300 ;13.692 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2558 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 506 ; 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): 1091 ; 1.199 ; 0.823
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1091 ; 1.163 ; 0.823
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1383 ; 1.968 ; 1.474
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1384 ; 1.968 ; 1.476
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1008 ; 2.082 ; 1.019
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1009 ; 2.081 ; 1.020
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1495 ; 3.135 ; 1.773
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2489 ; 6.207 ;11.680
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2407 ; 5.704 ; 9.650
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 9XV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-25.
REMARK 100 THE DEPOSITION ID IS D_1300066415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-SEP-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 : 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 : NULL
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 : 45798
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 34.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.17100
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 (%): 40.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (V/V) PEG 3350, 0.07M CITRIC ACID,
REMARK 280 0.03M BIS-TRIS PROPANE (PH 3.4), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
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 20.45050
REMARK 290 SMTRY3 2 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 TOTAL BURIED SURFACE AREA: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 0
REMARK 465 GLU A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
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 ASP A 2 -136.94 -90.61
REMARK 500 SER A 130 -124.79 62.17
REMARK 500 ASN A 213 122.29 -39.49
REMARK 500 THR A 254 30.06 -92.94
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9XV6 A 0 265 PDB 9XV6 9XV6 0 265
SEQRES 1 A 266 MET ALA ASP ASN PRO TYR GLN ARG GLY PRO ASP PRO THR
SEQRES 2 A 266 ARG ASP SER VAL ALA ALA SER ARG GLY THR PHE ALA THR
SEQRES 3 A 266 ALA SER THR THR VAL GLY SER GLY ASN GLY PHE GLY ALA
SEQRES 4 A 266 GLY PHE ILE TYR TYR PRO THR ASP THR SER GLN GLY THR
SEQRES 5 A 266 PHE GLY ALA VAL ALA ILE VAL PRO GLY TYR THR ALA THR
SEQRES 6 A 266 TRP ALA ALA GLU GLY ALA TRP MET GLY HIS TRP LEU ALA
SEQRES 7 A 266 SER PHE GLY PHE VAL VAL ILE GLY ILE ASP THR ILE ASN
SEQRES 8 A 266 ARG ASN ASP TRP ASP THR ALA ARG GLY THR GLN LEU LEU
SEQRES 9 A 266 ALA ALA LEU ASP TYR LEU THR GLN ARG SER THR VAL ARG
SEQRES 10 A 266 ASP ARG VAL ASP ALA SER ARG LEU ALA VAL MET GLY HIS
SEQRES 11 A 266 SER MET GLY GLY GLY GLY ALA MET TYR ALA ALA LEU GLN
SEQRES 12 A 266 ARG PRO SER LEU LYS ALA ALA VAL GLY LEU ALA PRO PHE
SEQRES 13 A 266 SER PRO SER GLN ASN LEU ASN GLY MET ARG VAL PRO THR
SEQRES 14 A 266 MET LEU LEU ALA GLY GLN HIS ASP THR THR THR THR PRO
SEQRES 15 A 266 ALA SER ILE THR SER LEU TYR ASN GLY ILE PRO ALA ALA
SEQRES 16 A 266 THR GLU LYS ALA TYR LEU GLU LEU SER GLY ALA GLY HIS
SEQRES 17 A 266 GLY PHE PRO THR SER ASN ASN SER VAL MET MET ARG LYS
SEQRES 18 A 266 VAL ILE PRO TRP LEU LYS ILE PHE VAL ASP SER ASP VAL
SEQRES 19 A 266 ARG TYR THR GLN PHE LEU CYS PRO LEU MET ASP ASN THR
SEQRES 20 A 266 GLY ILE ARG SER TYR GLN SER THR CYS PRO LEU LEU GLU
SEQRES 21 A 266 HIS HIS HIS HIS HIS HIS
HET GOL A 301 6
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 HOH *255(H2 O)
HELIX 1 AA1 ASP A 14 ALA A 18 5 5
HELIX 2 AA2 THR A 64 GLY A 69 1 6
HELIX 3 AA3 TRP A 71 SER A 78 1 8
HELIX 4 AA4 TRP A 94 ARG A 112 1 19
HELIX 5 AA5 VAL A 115 ASP A 117 5 3
HELIX 6 AA6 SER A 130 ARG A 143 1 14
HELIX 7 AA7 THR A 180 GLY A 190 1 11
HELIX 8 AA8 GLY A 208 SER A 212 5 5
HELIX 9 AA9 ASN A 214 ASP A 230 1 17
HELIX 10 AB1 ASP A 232 LEU A 239 5 8
SHEET 1 AA1 9 THR A 25 VAL A 30 0
SHEET 2 AA1 9 ALA A 38 PRO A 44 -1 O ILE A 41 N THR A 28
SHEET 3 AA1 9 VAL A 82 ASP A 87 -1 O GLY A 85 N PHE A 40
SHEET 4 AA1 9 PHE A 52 VAL A 58 1 N VAL A 55 O ILE A 84
SHEET 5 AA1 9 VAL A 119 HIS A 129 1 O ASP A 120 N PHE A 52
SHEET 6 AA1 9 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 7 AA1 9 THR A 168 GLY A 173 1 O LEU A 171 N GLY A 151
SHEET 8 AA1 9 LYS A 197 LEU A 202 1 O LEU A 202 N ALA A 172
SHEET 9 AA1 9 ILE A 248 SER A 253 -1 O ARG A 249 N GLU A 201
SSBOND 1 CYS A 240 CYS A 255 1555 1555 2.15
CISPEP 1 CYS A 240 PRO A 241 0 -9.57
CISPEP 2 CYS A 255 PRO A 256 0 1.76
CRYST1 44.083 40.901 68.399 90.00 105.43 90.00 P 1 21 1 2
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 0.022684 0.000000 0.006261 0.00000
SCALE2 0.000000 0.024449 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015167 0.00000
TER 2022 LEU A 258
MASTER 268 0 4 10 9 0 0 6 2201 1 20 21
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