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HEADER HYDROLASE 28-JUL-22 7YM9
TITLE CRYSTAL STRUCTURE OF A PET HYDROLASE FROM CRYPTOSPORANGIUM AURANTIACUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOSPORANGIUM AURANTIACUM;
SOURCE 3 ORGANISM_TAXID: 134849;
SOURCE 4 GENE: SAMN05443668_101498;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLY(ETHYLENE TEREPHTHALATE) HYDROLASE, ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HONG,D.KI,K.-J.KIM
REVDAT 1 12-JUL-23 7YM9 0
JRNL AUTH H.HONG,D.KI,K.-J.KIM
JRNL TITL EMERGENCE OF A NEWLY IDENTIFIED PETASE FROM CRYPTOSPORANGIUM
JRNL TITL 2 AURANTIACUM: FROM CHARACTERIZATION TO ENGINEERING FOR
JRNL TITL 3 EFFICIENT PET DECOMPOSITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 126891
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 6373
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) : 1.34
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9152
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 505
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 0.28000
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): 0.047
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.028
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.661
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
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): 4097 ; 0.016 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3720 ; 0.001 ; 0.014
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5625 ; 2.008 ; 1.647
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8555 ; 1.581 ; 1.572
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 6.885 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 202 ;29.392 ;20.990
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 563 ;10.744 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.153 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 545 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4795 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1017 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7YM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1300031243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-20
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133383
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
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: 5LUL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG3350, 0.1 M SODIUM
REMARK 280 MALONATE PH4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 41.15450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.22450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.15450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.22450
REMARK 290 SMTRY3 4 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 40
REMARK 465 ALA A 41
REMARK 465 ALA A 42
REMARK 465 LEU A 300
REMARK 465 GLU A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 MET B 40
REMARK 465 ALA B 41
REMARK 465 ALA B 42
REMARK 465 LEU B 300
REMARK 465 GLU B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
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 169 -131.61 60.99
REMARK 500 HIS A 223 -89.70 -132.25
REMARK 500 ASN B 44 117.75 -167.22
REMARK 500 ILE B 102 29.58 48.94
REMARK 500 SER B 169 -130.05 61.35
REMARK 500 HIS B 223 -90.17 -121.27
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7YM9 A 41 299 UNP A0A1M7II12_9ACTN
DBREF2 7YM9 A A0A1M7II12 41 299
DBREF1 7YM9 B 41 299 UNP A0A1M7II12_9ACTN
DBREF2 7YM9 B A0A1M7II12 41 299
SEQADV 7YM9 MET A 40 UNP A0A1M7II1 INITIATING METHIONINE
SEQADV 7YM9 LEU A 300 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 GLU A 301 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS A 302 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS A 303 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS A 304 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS A 305 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS A 306 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS A 307 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 MET B 40 UNP A0A1M7II1 INITIATING METHIONINE
SEQADV 7YM9 LEU B 300 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 GLU B 301 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS B 302 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS B 303 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS B 304 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS B 305 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS B 306 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 7YM9 HIS B 307 UNP A0A1M7II1 EXPRESSION TAG
SEQRES 1 A 268 MET ALA ALA ASP ASN PRO TYR GLN ARG GLY PRO ASP PRO
SEQRES 2 A 268 THR ASN ALA SER ILE GLU ALA ALA THR GLY PRO PHE ALA
SEQRES 3 A 268 VAL GLY THR GLN PRO ILE VAL GLY ALA SER GLY PHE GLY
SEQRES 4 A 268 GLY GLY GLN ILE TYR TYR PRO THR ASP THR SER GLN THR
SEQRES 5 A 268 TYR GLY ALA VAL VAL ILE VAL PRO GLY PHE ILE SER VAL
SEQRES 6 A 268 TRP ALA GLN LEU ASN TRP LEU GLY PRO ARG LEU ALA SER
SEQRES 7 A 268 GLN GLY PHE VAL VAL ILE GLY ILE GLU THR SER VAL ILE
SEQRES 8 A 268 THR ASP LEU PRO ASP PRO ARG GLY ASP GLN ALA LEU ALA
SEQRES 9 A 268 ALA LEU ASP TRP ALA THR THR ARG SER PRO VAL ALA SER
SEQRES 10 A 268 ARG ILE ASP ARG THR ARG LEU ALA ALA ALA GLY TRP SER
SEQRES 11 A 268 MET GLY GLY GLY GLY LEU ARG ARG ALA ALA LEU GLN ARG
SEQRES 12 A 268 PRO SER LEU LYS ALA ILE VAL GLY MET ALA PRO TRP ASN
SEQRES 13 A 268 GLY GLU ARG ASN TRP SER ALA VAL THR VAL PRO THR LEU
SEQRES 14 A 268 PHE PHE GLY GLY SER SER ASP ALA VAL ALA SER PRO ASN
SEQRES 15 A 268 ASP HIS ALA LYS PRO PHE TYR ASN SER ILE THR ARG ALA
SEQRES 16 A 268 GLU LYS ASP TYR ILE GLU LEU ARG ASN ALA ASP HIS PHE
SEQRES 17 A 268 PHE PRO THR SER ALA ASN THR THR MET ALA LYS TYR PHE
SEQRES 18 A 268 ILE SER TRP LEU LYS ARG TRP VAL ASP ASN ASP THR ARG
SEQRES 19 A 268 TYR THR GLN PHE LEU CYS PRO GLY PRO SER THR GLY LEU
SEQRES 20 A 268 PHE ALA PRO VAL SER ALA SER MET ASN THR CYS PRO PHE
SEQRES 21 A 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 268 MET ALA ALA ASP ASN PRO TYR GLN ARG GLY PRO ASP PRO
SEQRES 2 B 268 THR ASN ALA SER ILE GLU ALA ALA THR GLY PRO PHE ALA
SEQRES 3 B 268 VAL GLY THR GLN PRO ILE VAL GLY ALA SER GLY PHE GLY
SEQRES 4 B 268 GLY GLY GLN ILE TYR TYR PRO THR ASP THR SER GLN THR
SEQRES 5 B 268 TYR GLY ALA VAL VAL ILE VAL PRO GLY PHE ILE SER VAL
SEQRES 6 B 268 TRP ALA GLN LEU ASN TRP LEU GLY PRO ARG LEU ALA SER
SEQRES 7 B 268 GLN GLY PHE VAL VAL ILE GLY ILE GLU THR SER VAL ILE
SEQRES 8 B 268 THR ASP LEU PRO ASP PRO ARG GLY ASP GLN ALA LEU ALA
SEQRES 9 B 268 ALA LEU ASP TRP ALA THR THR ARG SER PRO VAL ALA SER
SEQRES 10 B 268 ARG ILE ASP ARG THR ARG LEU ALA ALA ALA GLY TRP SER
SEQRES 11 B 268 MET GLY GLY GLY GLY LEU ARG ARG ALA ALA LEU GLN ARG
SEQRES 12 B 268 PRO SER LEU LYS ALA ILE VAL GLY MET ALA PRO TRP ASN
SEQRES 13 B 268 GLY GLU ARG ASN TRP SER ALA VAL THR VAL PRO THR LEU
SEQRES 14 B 268 PHE PHE GLY GLY SER SER ASP ALA VAL ALA SER PRO ASN
SEQRES 15 B 268 ASP HIS ALA LYS PRO PHE TYR ASN SER ILE THR ARG ALA
SEQRES 16 B 268 GLU LYS ASP TYR ILE GLU LEU ARG ASN ALA ASP HIS PHE
SEQRES 17 B 268 PHE PRO THR SER ALA ASN THR THR MET ALA LYS TYR PHE
SEQRES 18 B 268 ILE SER TRP LEU LYS ARG TRP VAL ASP ASN ASP THR ARG
SEQRES 19 B 268 TYR THR GLN PHE LEU CYS PRO GLY PRO SER THR GLY LEU
SEQRES 20 B 268 PHE ALA PRO VAL SER ALA SER MET ASN THR CYS PRO PHE
SEQRES 21 B 268 LEU GLU HIS HIS HIS HIS HIS HIS
HET MLI A 401 7
HET MLI B 401 7
HETNAM MLI MALONATE ION
FORMUL 3 MLI 2(C3 H2 O4 2-)
FORMUL 5 HOH *470(H2 O)
HELIX 1 AA1 THR A 53 ALA A 59 1 7
HELIX 2 AA2 VAL A 104 ASN A 109 5 6
HELIX 3 AA3 TRP A 110 SER A 117 1 8
HELIX 4 AA4 LEU A 133 ARG A 151 1 19
HELIX 5 AA5 VAL A 154 SER A 156 5 3
HELIX 6 AA6 SER A 169 GLY A 174 1 6
HELIX 7 AA7 GLY A 174 ARG A 182 1 9
HELIX 8 AA8 HIS A 223 ILE A 231 1 9
HELIX 9 AA9 PHE A 247 SER A 251 5 5
HELIX 10 AB1 ASN A 253 ASP A 269 1 17
HELIX 11 AB2 ASP A 271 ARG A 273 5 3
HELIX 12 AB3 TYR A 274 CYS A 279 1 6
HELIX 13 AB4 THR B 53 ALA B 59 1 7
HELIX 14 AB5 VAL B 104 ASN B 109 5 6
HELIX 15 AB6 TRP B 110 SER B 117 1 8
HELIX 16 AB7 LEU B 133 ARG B 151 1 19
HELIX 17 AB8 VAL B 154 SER B 156 5 3
HELIX 18 AB9 SER B 169 GLY B 174 1 6
HELIX 19 AC1 GLY B 174 ARG B 182 1 9
HELIX 20 AC2 HIS B 223 ILE B 231 1 9
HELIX 21 AC3 PHE B 247 SER B 251 5 5
HELIX 22 AC4 ASN B 253 ASP B 269 1 17
HELIX 23 AC5 ASP B 271 ARG B 273 5 3
HELIX 24 AC6 TYR B 274 CYS B 279 1 6
SHEET 1 AA1 9 VAL A 66 PRO A 70 0
SHEET 2 AA1 9 GLY A 80 PRO A 85 -1 O TYR A 84 N GLY A 67
SHEET 3 AA1 9 VAL A 121 ILE A 125 -1 O VAL A 122 N TYR A 83
SHEET 4 AA1 9 TYR A 92 VAL A 98 1 N VAL A 95 O ILE A 123
SHEET 5 AA1 9 ILE A 158 TRP A 168 1 O ASP A 159 N TYR A 92
SHEET 6 AA1 9 ALA A 187 MET A 191 1 O MET A 191 N GLY A 167
SHEET 7 AA1 9 THR A 207 GLY A 212 1 O LEU A 208 N GLY A 190
SHEET 8 AA1 9 LYS A 236 LEU A 241 1 O LEU A 241 N GLY A 211
SHEET 9 AA1 9 VAL A 290 ASN A 295 -1 O MET A 294 N TYR A 238
SHEET 1 AA2 9 VAL B 66 PRO B 70 0
SHEET 2 AA2 9 GLY B 80 PRO B 85 -1 O TYR B 84 N GLY B 67
SHEET 3 AA2 9 VAL B 121 ILE B 125 -1 O VAL B 122 N TYR B 83
SHEET 4 AA2 9 TYR B 92 VAL B 98 1 N ILE B 97 O ILE B 123
SHEET 5 AA2 9 ILE B 158 TRP B 168 1 O ALA B 166 N VAL B 96
SHEET 6 AA2 9 ALA B 187 MET B 191 1 O MET B 191 N GLY B 167
SHEET 7 AA2 9 THR B 207 GLY B 212 1 O PHE B 210 N GLY B 190
SHEET 8 AA2 9 LYS B 236 LEU B 241 1 O LEU B 241 N GLY B 211
SHEET 9 AA2 9 VAL B 290 ASN B 295 -1 O MET B 294 N TYR B 238
SSBOND 1 CYS A 279 CYS A 297 1555 1555 2.08
SSBOND 2 CYS B 279 CYS B 297 1555 1555 2.06
CISPEP 1 CYS A 279 PRO A 280 0 7.24
CISPEP 2 CYS A 297 PRO A 298 0 -0.36
CISPEP 3 CYS B 279 PRO B 280 0 7.82
CISPEP 4 CYS B 297 PRO B 298 0 4.40
CRYST1 82.309 82.449 87.391 90.00 90.00 90.00 P 21 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 0.012149 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011443 0.00000
TER 1978 PHE A 299
TER 3957 PHE B 299
MASTER 293 0 2 24 18 0 0 6 4386 2 18 42
END |