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HEADER HYDROLASE 11-JAN-23 8C65
TITLE CRYSTAL STRUCTURE OF CUTINASE ADCUT FROM ACIDOVORAX DELAFIELDII (PBS
TITLE 2 DEPOLYMERASE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PBS(A) DEPOLYMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACIDOVORAX DELAFIELDII;
SOURCE 3 ORGANISM_TAXID: 47920;
SOURCE 4 GENE: PBSA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CUTINASE, PET, PBS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,M.CLARK
REVDAT 1 24-JAN-24 8C65 0
JRNL AUTH M.CLARK,M.ZAHN
JRNL TITL PREDICTIONS OF THE SUBSTRATE SPECIFICITIES OF THE
JRNL TITL 2 PLASTIC-DEGRADING ENZYMES ISPETASE AND ADCUT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 51.1
REMARK 3 NUMBER OF REFLECTIONS : 39402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.814
REMARK 3 FREE R VALUE TEST SET COUNT : 1897
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 405
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 7.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 13
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3976
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 405
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : 0.04700
REMARK 3 B33 (A**2) : -0.22200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.157
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.252
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4114 ; 0.009 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 3516 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5618 ; 1.518 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8254 ; 0.549 ; 1.549
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 543 ; 7.082 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 34 ; 8.239 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 614 ;12.922 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 608 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4868 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 844 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 919 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 51 ; 0.165 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2103 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 334 ; 0.238 ; 0.200
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): 2122 ; 0.796 ; 0.780
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2122 ; 0.792 ; 0.779
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2654 ; 1.360 ; 1.161
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2655 ; 1.364 ; 1.163
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1992 ; 1.109 ; 0.902
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1991 ; 1.105 ; 0.900
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2954 ; 1.743 ; 1.314
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2955 ; 1.742 ; 1.315
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 42 A 304 NULL
REMARK 3 1 A 42 A 304 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 42 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1854 0.3380 8.6597
REMARK 3 T TENSOR
REMARK 3 T11: 0.0084 T22: 0.0034
REMARK 3 T33: 0.0157 T12: 0.0026
REMARK 3 T13: -0.0010 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.4080 L22: 0.6894
REMARK 3 L33: 0.7747 L12: -0.0197
REMARK 3 L13: -0.0048 L23: -0.0198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0184 S13: -0.0130
REMARK 3 S21: 0.0102 S22: 0.0083 S23: 0.0058
REMARK 3 S31: 0.0109 S32: 0.0016 S33: -0.0026
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9081 27.4105 20.7016
REMARK 3 T TENSOR
REMARK 3 T11: 0.0079 T22: 0.0033
REMARK 3 T33: 0.0095 T12: 0.0030
REMARK 3 T13: -0.0028 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.6484 L22: 0.7044
REMARK 3 L33: 0.6933 L12: 0.0903
REMARK 3 L13: -0.2414 L23: -0.1123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: 0.0083 S13: 0.0065
REMARK 3 S21: 0.0094 S22: -0.0037 S23: 0.0172
REMARK 3 S31: -0.0123 S32: 0.0009 S33: 0.0004
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8C65 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-23.
REMARK 100 THE DEPOSITION ID IS D_1292127880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39403
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.491
REMARK 200 RESOLUTION RANGE LOW (A) : 54.626
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.1
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.19500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.26200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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 (%): 40.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.2 M AMMONIUM CITRATE
REMARK 280 DIBASIC, 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 48.21500
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 LEU A 305
REMARK 465 GLU A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 LEU B 305
REMARK 465 GLU B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
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 514 O HOH A 571 1.82
REMARK 500 ND2 ASN A 294 O HOH A 401 2.02
REMARK 500 OG SER A 152 O HOH A 402 2.06
REMARK 500 O HOH B 583 O HOH B 584 2.09
REMARK 500 O HOH A 444 O HOH A 462 2.10
REMARK 500 O HOH A 583 O HOH A 601 2.14
REMARK 500 O HOH B 529 O HOH B 572 2.14
REMARK 500 ND2 ASN B 247 O HOH B 401 2.15
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 ASN A 87 39.85 -147.08
REMARK 500 SER A 174 -120.91 57.70
REMARK 500 HIS A 228 -90.87 -124.22
REMARK 500 SER A 237 -15.20 -150.60
REMARK 500 ASN A 291 66.59 39.52
REMARK 500 THR B 43 -44.60 63.98
REMARK 500 ASN B 87 35.48 -144.97
REMARK 500 SER B 174 -121.74 60.39
REMARK 500 ALA B 223 67.88 -119.54
REMARK 500 HIS B 228 -91.67 -123.86
REMARK 500 SER B 237 -16.53 -149.11
REMARK 500 ASN B 291 69.26 39.75
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 137 0.09 SIDE CHAIN
REMARK 500 ARG B 78 0.10 SIDE CHAIN
REMARK 500 ARG B 137 0.09 SIDE CHAIN
REMARK 500 ARG B 153 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8C65 A 42 304 UNP Q8RR62 Q8RR62_ACIDE 42 304
DBREF 8C65 B 42 304 UNP Q8RR62 Q8RR62_ACIDE 42 304
SEQADV 8C65 LEU A 305 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 GLU A 306 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS A 307 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS A 308 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS A 309 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS A 310 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS A 311 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS A 312 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 LEU B 305 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 GLU B 306 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS B 307 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS B 308 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS B 309 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS B 310 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS B 311 UNP Q8RR62 EXPRESSION TAG
SEQADV 8C65 HIS B 312 UNP Q8RR62 EXPRESSION TAG
SEQRES 1 A 271 GLN THR ASN PRO TYR GLU ARG GLY PRO ALA PRO THR THR
SEQRES 2 A 271 SER SER LEU GLU ALA SER ARG GLY PRO PHE SER TYR GLN
SEQRES 3 A 271 SER PHE THR VAL SER ARG PRO SER GLY TYR ARG ALA GLY
SEQRES 4 A 271 THR VAL TYR TYR PRO THR ASN ALA GLY GLY PRO VAL GLY
SEQRES 5 A 271 ALA ILE ALA ILE VAL PRO GLY PHE THR ALA ARG GLN SER
SEQRES 6 A 271 SER ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 7 A 271 PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP
SEQRES 8 A 271 GLN PRO ASP SER ARG SER ARG GLN GLN MET ALA ALA LEU
SEQRES 9 A 271 SER GLN VAL ALA THR LEU SER ARG THR SER SER SER PRO
SEQRES 10 A 271 ILE TYR ASN LYS VAL ASP THR SER ARG LEU GLY VAL MET
SEQRES 11 A 271 GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA
SEQRES 12 A 271 ARG ASN ASN PRO SER ILE LYS ALA ALA ALA PRO GLN ALA
SEQRES 13 A 271 PRO TRP SER ALA SER LYS ASN PHE SER SER LEU THR VAL
SEQRES 14 A 271 PRO THR LEU ILE ILE ALA CYS GLU ASN ASP THR ILE ALA
SEQRES 15 A 271 PRO VAL ASN GLN HIS ALA ASP THR PHE TYR ASP SER MET
SEQRES 16 A 271 SER ARG ASN PRO ARG GLU PHE LEU GLU ILE ASN ASN GLY
SEQRES 17 A 271 SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA
SEQRES 18 A 271 LEU LEU GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE
SEQRES 19 A 271 MET ASP ASN ASP ARG ARG TYR THR SER PHE ALA CYS SER
SEQRES 20 A 271 ASN PRO ASN SER TYR ASN VAL SER ASP PHE ARG VAL ALA
SEQRES 21 A 271 ALA CYS ASN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 271 GLN THR ASN PRO TYR GLU ARG GLY PRO ALA PRO THR THR
SEQRES 2 B 271 SER SER LEU GLU ALA SER ARG GLY PRO PHE SER TYR GLN
SEQRES 3 B 271 SER PHE THR VAL SER ARG PRO SER GLY TYR ARG ALA GLY
SEQRES 4 B 271 THR VAL TYR TYR PRO THR ASN ALA GLY GLY PRO VAL GLY
SEQRES 5 B 271 ALA ILE ALA ILE VAL PRO GLY PHE THR ALA ARG GLN SER
SEQRES 6 B 271 SER ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 7 B 271 PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP
SEQRES 8 B 271 GLN PRO ASP SER ARG SER ARG GLN GLN MET ALA ALA LEU
SEQRES 9 B 271 SER GLN VAL ALA THR LEU SER ARG THR SER SER SER PRO
SEQRES 10 B 271 ILE TYR ASN LYS VAL ASP THR SER ARG LEU GLY VAL MET
SEQRES 11 B 271 GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA
SEQRES 12 B 271 ARG ASN ASN PRO SER ILE LYS ALA ALA ALA PRO GLN ALA
SEQRES 13 B 271 PRO TRP SER ALA SER LYS ASN PHE SER SER LEU THR VAL
SEQRES 14 B 271 PRO THR LEU ILE ILE ALA CYS GLU ASN ASP THR ILE ALA
SEQRES 15 B 271 PRO VAL ASN GLN HIS ALA ASP THR PHE TYR ASP SER MET
SEQRES 16 B 271 SER ARG ASN PRO ARG GLU PHE LEU GLU ILE ASN ASN GLY
SEQRES 17 B 271 SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA
SEQRES 18 B 271 LEU LEU GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE
SEQRES 19 B 271 MET ASP ASN ASP ARG ARG TYR THR SER PHE ALA CYS SER
SEQRES 20 B 271 ASN PRO ASN SER TYR ASN VAL SER ASP PHE ARG VAL ALA
SEQRES 21 B 271 ALA CYS ASN LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *405(H2 O)
HELIX 1 AA1 THR A 53 ALA A 59 1 7
HELIX 2 AA2 ARG A 104 ASN A 109 5 6
HELIX 3 AA3 TRP A 110 SER A 117 1 8
HELIX 4 AA4 GLN A 133 ARG A 153 1 21
HELIX 5 AA5 SER A 174 ASN A 187 1 14
HELIX 6 AA6 HIS A 228 MET A 236 1 9
HELIX 7 AA7 ASN A 260 ASP A 277 1 18
HELIX 8 AA8 ASP A 279 ARG A 281 5 3
HELIX 9 AA9 TYR A 282 SER A 288 1 7
HELIX 10 AB1 THR B 53 ALA B 59 1 7
HELIX 11 AB2 ARG B 104 ASN B 109 5 6
HELIX 12 AB3 TRP B 110 SER B 117 1 8
HELIX 13 AB4 GLN B 133 ARG B 153 1 21
HELIX 14 AB5 SER B 174 ASN B 187 1 14
HELIX 15 AB6 HIS B 228 MET B 236 1 9
HELIX 16 AB7 ASN B 260 ASP B 277 1 18
HELIX 17 AB8 ASP B 279 ARG B 281 5 3
HELIX 18 AB9 TYR B 282 SER B 288 1 7
SHEET 1 AA1 6 TYR A 66 THR A 70 0
SHEET 2 AA1 6 ALA A 79 PRO A 85 -1 O VAL A 82 N PHE A 69
SHEET 3 AA1 6 VAL A 121 ASP A 126 -1 O VAL A 122 N TYR A 83
SHEET 4 AA1 6 VAL A 92 VAL A 98 1 N ILE A 97 O ILE A 123
SHEET 5 AA1 6 VAL A 163 TRP A 173 1 O ASP A 164 N VAL A 92
SHEET 6 AA1 6 ALA A 192 GLN A 196 1 O GLN A 196 N GLY A 172
SHEET 1 AA2 3 THR A 212 CYS A 217 0
SHEET 2 AA2 3 ARG A 241 ILE A 246 1 O GLU A 242 N ILE A 214
SHEET 3 AA2 3 VAL A 295 ALA A 301 -1 O ARG A 299 N PHE A 243
SHEET 1 AA3 6 TYR B 66 THR B 70 0
SHEET 2 AA3 6 ALA B 79 PRO B 85 -1 O VAL B 82 N PHE B 69
SHEET 3 AA3 6 VAL B 121 ASP B 126 -1 O VAL B 122 N TYR B 83
SHEET 4 AA3 6 VAL B 92 VAL B 98 1 N ILE B 97 O ILE B 123
SHEET 5 AA3 6 VAL B 163 TRP B 173 1 O ASP B 164 N VAL B 92
SHEET 6 AA3 6 ALA B 192 GLN B 196 1 O GLN B 196 N GLY B 172
SHEET 1 AA4 3 THR B 212 CYS B 217 0
SHEET 2 AA4 3 ARG B 241 ILE B 246 1 O LEU B 244 N ALA B 216
SHEET 3 AA4 3 VAL B 295 ALA B 301 -1 O ARG B 299 N PHE B 243
SSBOND 1 CYS A 217 CYS A 253 1555 1555 2.12
SSBOND 2 CYS A 287 CYS A 303 1555 1555 2.12
SSBOND 3 CYS B 217 CYS B 253 1555 1555 2.12
SSBOND 4 CYS B 287 CYS B 303 1555 1555 2.06
CRYST1 45.798 96.430 58.525 90.00 111.03 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 0.021835 0.000000 0.008396 0.00000
SCALE2 0.000000 0.010370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018306 0.00000
TER 2004 ASN A 304
TER 4008 ASN B 304
MASTER 364 0 0 18 18 0 0 6 4381 2 8 42
END |