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HEADER HYDROLASE 25-NOV-25 9XV5
TITLE CATALYTIC DOMAIN OF N1484
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: C3 CLUSTER PET HYDROLASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA UREILYTICA;
SOURCE 3 ORGANISM_TAXID: 709868;
SOURCE 4 GENE: DDE19_30945;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: SHUFFLE T7
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HWANG,H.SEO,K.-J.KIM
REVDAT 1 03-JUN-26 9XV5 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) : 43.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 45975
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2473
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) : 1.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3423
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 174
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.97000
REMARK 3 B22 (A**2) : -0.83000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.055
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.057
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.039
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2093 ; 0.012 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 1927 ; 0.002 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2873 ; 1.830 ; 1.648
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4434 ; 0.622 ; 1.556
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 281 ; 7.249 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 16 ; 8.451 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 296 ;13.803 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 327 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2555 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 501 ; 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): 1094 ; 1.277 ; 0.979
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1093 ; 1.278 ; 0.976
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1385 ; 1.844 ; 1.756
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1386 ; 1.845 ; 1.758
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 999 ; 1.987 ; 1.187
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1000 ; 1.987 ; 1.187
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1489 ; 2.919 ; 2.077
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2506 ; 8.908 ;23.070
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2392 ; 8.351 ;17.440
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 9XV5 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_1300066414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-25
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 : 48448
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 43.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2000
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) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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 (%): 44.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) PEG 8000, 0.1M IMIDAZOLE (PH
REMARK 280 8.0), 0.2M SODIUM CHLORIDE, 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 42.10600
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: 250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9620 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 0
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLU 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 465 HIS A 266
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 ASN A 37 44.52 -86.68
REMARK 500 THR A 62 -9.59 83.16
REMARK 500 SER A 130 -129.28 65.03
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 680 DISTANCE = 5.93 ANGSTROMS
DBREF1 9XV5 A 1 259 UNP A0A3N9XER1_9ACTN
DBREF2 9XV5 A A0A3N9XER1 54 312
SEQADV 9XV5 MET A 0 UNP A0A3N9XER INITIATING METHIONINE
SEQADV 9XV5 GLU A 260 UNP A0A3N9XER EXPRESSION TAG
SEQADV 9XV5 HIS A 261 UNP A0A3N9XER EXPRESSION TAG
SEQADV 9XV5 HIS A 262 UNP A0A3N9XER EXPRESSION TAG
SEQADV 9XV5 HIS A 263 UNP A0A3N9XER EXPRESSION TAG
SEQADV 9XV5 HIS A 264 UNP A0A3N9XER EXPRESSION TAG
SEQADV 9XV5 HIS A 265 UNP A0A3N9XER EXPRESSION TAG
SEQADV 9XV5 HIS A 266 UNP A0A3N9XER EXPRESSION TAG
SEQRES 1 A 267 MET ALA ASP ASN PRO TYR GLN ARG GLY PRO ASP PRO THR
SEQRES 2 A 267 ARG THR SER VAL THR ALA VAL ASN GLY PRO PHE ALA ASN
SEQRES 3 A 267 THR SER VAL SER VAL PRO THR GLY TYR GLY PHE ASN GLY
SEQRES 4 A 267 GLY ARG ILE TYR TYR PRO THR ASP THR SER GLN GLY THR
SEQRES 5 A 267 PHE GLY ALA ILE ALA ILE SER PRO GLY TYR THR ALA LEU
SEQRES 6 A 267 PHE SER ALA GLU LEU ALA TRP MET GLY PRO TRP LEU ALA
SEQRES 7 A 267 SER HIS GLY PHE VAL VAL ILE GLY ILE GLU THR ASN SER
SEQRES 8 A 267 ARG ASN ASP PHE ASP THR ALA ARG GLY THR GLN LEU LEU
SEQRES 9 A 267 ALA ALA LEU ASP TYR LEU THR GLN GLN SER PRO VAL ARG
SEQRES 10 A 267 ASP ARG VAL ASP PRO ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 A 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ILE ARG
SEQRES 12 A 267 ARG SER SER LEU LYS ALA VAL VAL GLY ILE ALA PRO TYR
SEQRES 13 A 267 SER PRO SER SER ASN LEU ALA ASN ASP ARG VAL PRO THR
SEQRES 14 A 267 MET ILE PHE ALA GLY GLN ALA ASP THR VAL VAL THR PRO
SEQRES 15 A 267 SER TYR ALA THR GLY LEU TYR ASN SER LEU PRO THR THR
SEQRES 16 A 267 THR GLU SER VAL TYR LEU GLU VAL ALA GLY ALA ASP HIS
SEQRES 17 A 267 GLY PHE MET VAL GLY ARG SER ASN PRO VAL MET VAL ARG
SEQRES 18 A 267 THR MET LEU PRO PHE VAL LYS MET PHE ILE ASP ASN ASP
SEQRES 19 A 267 ALA ARG TYR SER GLN PHE LEU CYS PRO LEU LEU ASP SER
SEQRES 20 A 267 SER GLY VAL VAL THR TYR ARG SER THR CYS PRO LEU LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
HET GOL A 301 6
HET EDO A 302 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 C2 H6 O2
FORMUL 4 HOH *280(H2 O)
HELIX 1 AA1 THR A 14 ALA A 18 5 5
HELIX 2 AA2 LEU A 64 LEU A 69 1 6
HELIX 3 AA3 TRP A 71 HIS A 79 1 9
HELIX 4 AA4 PHE A 94 GLN 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 SER A 190 1 11
HELIX 8 AA8 ASN A 215 ASN A 232 1 18
HELIX 9 AA9 ASP A 233 LEU A 240 5 8
SHEET 1 AA1 9 ASN A 25 VAL A 30 0
SHEET 2 AA1 9 GLY A 39 PRO A 44 -1 O ILE A 41 N VAL A 28
SHEET 3 AA1 9 VAL A 82 ILE A 86 -1 O VAL A 83 N TYR A 42
SHEET 4 AA1 9 PHE A 52 SER A 58 1 N ILE A 55 O VAL A 82
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 ILE A 152 1 O ILE A 152 N GLY A 128
SHEET 7 AA1 9 THR A 168 GLY A 173 1 O MET A 169 N GLY A 151
SHEET 8 AA1 9 SER A 197 VAL A 202 1 O VAL A 202 N ALA A 172
SHEET 9 AA1 9 VAL A 249 SER A 254 -1 O ARG A 253 N TYR A 199
SSBOND 1 CYS A 241 CYS A 256 1555 1555 2.11
CISPEP 1 CYS A 241 PRO A 242 0 -7.89
CISPEP 2 CYS A 256 PRO A 257 0 -0.04
CRYST1 34.239 84.212 43.853 90.00 92.78 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 0.029206 0.000000 0.001419 0.00000
SCALE2 0.000000 0.011875 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022830 0.00000
TER 2005 LEU A 259
MASTER 282 0 2 9 9 0 0 6 2212 1 12 21
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