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HEADER HYDROLASE 17-DEC-21 7QJS
TITLE CRYSTAL STRUCTURE OF A CUTINASE ENZYME FROM THERMOBIFIDA FUSCA YX
TITLE 2 (705)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA YX;
SOURCE 3 ORGANISM_TAXID: 269800;
SOURCE 4 GENE: CUT2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,T.J.SHAKESPEARE,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 28-DEC-22 7QJS 0
JRNL AUTH E.ERICKSON,J.E.GADO,L.AVILAN,F.BRATTI,R.K.BRIZENDINE,
JRNL AUTH 2 P.A.COX,R.GILL,R.GRAHAM,D.J.KIM,G.KONIG,W.E.MICHENER,
JRNL AUTH 3 S.POUDEL,K.J.RAMIREZ,T.J.SHAKESPEARE,M.ZAHN,E.S.BOYD,
JRNL AUTH 4 C.M.PAYNE,J.L.DUBOIS,A.R.PICKFORD,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL SOURCING THERMOTOLERANT POLY(ETHYLENE TEREPHTHALATE)
JRNL TITL 2 HYDROLASE SCAFFOLDS FROM NATURAL DIVERSITY
JRNL REF NAT COMMUN V. 13 7850 2022
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-022-35237-X
REMARK 2
REMARK 2 RESOLUTION. 1.43 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 64.4
REMARK 3 NUMBER OF REFLECTIONS : 57020
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) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.953
REMARK 3 FREE R VALUE TEST SET COUNT : 2826
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) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 113
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 1.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 7
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3982
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 372
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00800
REMARK 3 B22 (A**2) : -0.28100
REMARK 3 B33 (A**2) : 0.27100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.104
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.503
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4125 ; 0.014 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3820 ; 0.001 ; 0.014
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5619 ; 1.857 ; 1.651
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8790 ; 1.539 ; 1.575
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 522 ; 7.319 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;29.253 ;20.455
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 616 ;11.169 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;18.672 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 546 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4712 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 988 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 893 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 82 ; 0.210 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2095 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 334 ; 0.210 ; 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): 2076 ; 1.173 ; 1.395
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2075 ; 1.166 ; 1.393
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2590 ; 1.827 ; 2.080
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2591 ; 1.828 ; 2.081
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2049 ; 1.551 ; 1.590
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2050 ; 1.551 ; 1.591
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3025 ; 2.417 ; 2.303
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3026 ; 2.417 ; 2.305
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 B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 263 NULL
REMARK 3 2 B 1 B 263 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 263
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1345 8.5054 20.6596
REMARK 3 T TENSOR
REMARK 3 T11: 0.0027 T22: 0.0065
REMARK 3 T33: 0.0031 T12: -0.0030
REMARK 3 T13: 0.0018 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.1648 L22: 0.2360
REMARK 3 L33: 0.2861 L12: 0.0678
REMARK 3 L13: -0.0011 L23: 0.0822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: -0.0138 S13: -0.0178
REMARK 3 S21: -0.0063 S22: 0.0019 S23: -0.0198
REMARK 3 S31: 0.0083 S32: -0.0146 S33: 0.0050
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 263
REMARK 3 RESIDUE RANGE : B 302 B 302
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5697 42.6545 -0.8351
REMARK 3 T TENSOR
REMARK 3 T11: 0.0040 T22: 0.0077
REMARK 3 T33: 0.0040 T12: -0.0047
REMARK 3 T13: -0.0007 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.0978 L22: 0.4112
REMARK 3 L33: 0.3858 L12: 0.1546
REMARK 3 L13: -0.0385 L23: -0.1643
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: -0.0108 S13: 0.0051
REMARK 3 S21: 0.0069 S22: 0.0059 S23: 0.0328
REMARK 3 S31: -0.0323 S32: 0.0222 S33: -0.0131
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 7QJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1292118617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9119
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57020
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.429
REMARK 200 RESOLUTION RANGE LOW (A) : 75.106
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 1.17000
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: 5ZOA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M CESIUM CHLORIDE, 0.1 M MES PH
REMARK 280 6.5, 30% (V/V) JEFFAMINE M-600, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 75.10600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 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 0
REMARK 465 ASP A 246
REMARK 465 GLY A 247
REMARK 465 LEU A 248
REMARK 465 PHE A 249
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 MET B 0
REMARK 465 ASP B 246
REMARK 465 GLY B 247
REMARK 465 LEU B 248
REMARK 465 PHE B 249
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
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 HD1 HIS B 156 H ASN B 158 1.18
REMARK 500 HD1 HIS A 156 H ASN A 158 1.18
REMARK 500 H PHE A 261 O HOH A 401 1.31
REMARK 500 HH11 ARG A 138 O HOH A 405 1.41
REMARK 500 HH TYR B 106 O HOH B 406 1.56
REMARK 500 HH11 ARG A 31 O ALA A 34 1.56
REMARK 500 HH11 ARG B 31 O ALA B 34 1.56
REMARK 500 O HOH A 404 O HOH B 487 1.96
REMARK 500 O HOH B 410 O HOH B 469 2.01
REMARK 500 N PHE A 261 O HOH A 401 2.03
REMARK 500 NH1 ARG B 31 O ALA B 34 2.07
REMARK 500 NH1 ARG A 31 O ALA A 34 2.09
REMARK 500 OE2 GLU A 263 NH2 ARG B 256 2.11
REMARK 500 OD1 ASP B 204 O HOH B 401 2.11
REMARK 500 OE1 GLU A 253 O HOH A 402 2.12
REMARK 500 O ILE A 150 O HOH A 403 2.18
REMARK 500 O HOH A 477 O HOH A 529 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 555 O HOH B 403 1556 2.04
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 ARG A 228 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 PRO B 260 N - CA - C ANGL. DEV. = -15.9 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 130 -120.05 64.70
REMARK 500 THR A 153 59.15 33.51
REMARK 500 HIS A 184 -91.82 -128.56
REMARK 500 THR A 258 31.25 -99.93
REMARK 500 SER B 130 -120.07 63.71
REMARK 500 THR B 153 61.57 30.93
REMARK 500 HIS B 184 -88.41 -128.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 302
DBREF 7QJS A 0 261 UNP E9LVH9 E9LVH9_9ACTN 1 262
DBREF 7QJS B 0 261 UNP E9LVH9 E9LVH9_9ACTN 1 262
SEQADV 7QJS LEU A 262 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS GLU A 263 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS A 264 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS A 265 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS A 266 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS A 267 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS A 268 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS A 269 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS LEU B 262 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS GLU B 263 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS B 264 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS B 265 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS B 266 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS B 267 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS B 268 UNP E9LVH9 EXPRESSION TAG
SEQADV 7QJS HIS B 269 UNP E9LVH9 EXPRESSION TAG
SEQRES 1 A 270 MET ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP
SEQRES 2 A 270 ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER
SEQRES 3 A 270 GLU GLU ARG ALA SER ARG PHE GLY ALA ASP GLY PHE GLY
SEQRES 4 A 270 GLY GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR
SEQRES 5 A 270 GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLN
SEQRES 6 A 270 ALA SER VAL ALA TRP LEU GLY GLU ARG ILE ALA SER HIS
SEQRES 7 A 270 GLY PHE VAL VAL ILE THR ILE ASP THR ASN THR THR LEU
SEQRES 8 A 270 ASP GLN PRO ASP SER ARG ALA ARG GLN LEU ASN ALA ALA
SEQRES 9 A 270 LEU ASP TYR MET ILE ASN ASP ALA SER SER ALA VAL ARG
SEQRES 10 A 270 SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS
SEQRES 11 A 270 SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER GLN
SEQRES 12 A 270 ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP
SEQRES 13 A 270 HIS LEU ASN LYS ASN TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 A 270 LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 270 LEU THR HIS ALA ARG PRO PHE TYR ASN SER LEU PRO THR
SEQRES 16 A 270 SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR
SEQRES 17 A 270 HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS
SEQRES 18 A 270 TYR SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP
SEQRES 19 A 270 THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP
SEQRES 20 A 270 GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 270 PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 MET ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP
SEQRES 2 B 270 ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER
SEQRES 3 B 270 GLU GLU ARG ALA SER ARG PHE GLY ALA ASP GLY PHE GLY
SEQRES 4 B 270 GLY GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR
SEQRES 5 B 270 GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLN
SEQRES 6 B 270 ALA SER VAL ALA TRP LEU GLY GLU ARG ILE ALA SER HIS
SEQRES 7 B 270 GLY PHE VAL VAL ILE THR ILE ASP THR ASN THR THR LEU
SEQRES 8 B 270 ASP GLN PRO ASP SER ARG ALA ARG GLN LEU ASN ALA ALA
SEQRES 9 B 270 LEU ASP TYR MET ILE ASN ASP ALA SER SER ALA VAL ARG
SEQRES 10 B 270 SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS
SEQRES 11 B 270 SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER GLN
SEQRES 12 B 270 ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP
SEQRES 13 B 270 HIS LEU ASN LYS ASN TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 B 270 LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL
SEQRES 15 B 270 LEU THR HIS ALA ARG PRO PHE TYR ASN SER LEU PRO THR
SEQRES 16 B 270 SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR
SEQRES 17 B 270 HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS
SEQRES 18 B 270 TYR SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP
SEQRES 19 B 270 THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP
SEQRES 20 B 270 GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS
SEQRES 21 B 270 PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL A 301 14
HET PG4 A 302 23
HET GOL B 301 14
HET PEG B 302 17
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 PG4 C8 H18 O5
FORMUL 6 PEG C4 H10 O3
FORMUL 7 HOH *372(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 THR A 63 SER A 66 5 4
HELIX 3 AA3 VAL A 67 SER A 76 1 10
HELIX 4 AA4 GLN A 92 ASP A 110 1 19
HELIX 5 AA5 SER A 112 SER A 117 1 6
HELIX 6 AA6 SER A 130 ARG A 143 1 14
HELIX 7 AA7 HIS A 184 LEU A 192 1 9
HELIX 8 AA8 PHE A 209 ILE A 213 5 5
HELIX 9 AA9 ASN A 215 ASP A 231 1 17
HELIX 10 AB1 ASP A 233 ARG A 235 5 3
HELIX 11 AB2 TYR A 236 CYS A 241 1 6
HELIX 12 AB3 THR B 11 ALA B 17 1 7
HELIX 13 AB4 THR B 63 SER B 66 5 4
HELIX 14 AB5 VAL B 67 SER B 76 1 10
HELIX 15 AB6 GLN B 92 ASP B 110 1 19
HELIX 16 AB7 SER B 112 SER B 117 1 6
HELIX 17 AB8 SER B 130 ARG B 143 1 14
HELIX 18 AB9 HIS B 184 LEU B 192 1 9
HELIX 19 AC1 PHE B 209 ILE B 213 5 5
HELIX 20 AC2 ASN B 215 ASP B 231 1 17
HELIX 21 AC3 ASP B 233 ARG B 235 5 3
HELIX 22 AC4 TYR B 236 CYS B 241 1 6
SHEET 1 AA1 6 VAL A 24 ALA A 29 0
SHEET 2 AA1 6 GLY A 40 PRO A 45 -1 O ILE A 42 N GLU A 27
SHEET 3 AA1 6 PHE A 79 ILE A 84 -1 O VAL A 81 N TYR A 43
SHEET 4 AA1 6 TYR A 51 SER A 57 1 N VAL A 54 O VAL A 80
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O ASP A 120 N TYR A 51
SHEET 6 AA1 6 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 ALA A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O LEU A 203 N GLY A 172
SHEET 3 AA2 3 VAL A 252 SER A 257 -1 O GLU A 254 N GLU A 202
SHEET 1 AA3 6 VAL B 24 ALA B 29 0
SHEET 2 AA3 6 GLY B 40 PRO B 45 -1 O ILE B 42 N GLU B 27
SHEET 3 AA3 6 PHE B 79 ILE B 84 -1 O VAL B 81 N TYR B 43
SHEET 4 AA3 6 TYR B 51 SER B 57 1 N VAL B 54 O VAL B 80
SHEET 5 AA3 6 ILE B 119 HIS B 129 1 O ASP B 120 N TYR B 51
SHEET 6 AA3 6 ALA B 148 LEU B 152 1 O LEU B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 ALA B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O LEU B 203 N GLY B 172
SHEET 3 AA4 3 VAL B 252 SER B 257 -1 O GLU B 254 N GLU B 202
SSBOND 1 CYS A 241 CYS A 259 1555 1555 2.07
SSBOND 2 CYS B 241 CYS B 259 1555 1555 2.05
CISPEP 1 CYS A 241 PRO A 242 0 -1.96
CISPEP 2 CYS A 259 PRO A 260 0 -5.44
CISPEP 3 CYS B 241 PRO B 242 0 -7.85
CISPEP 4 CYS B 259 PRO B 260 0 -6.59
CRYST1 36.164 150.212 43.396 90.00 92.51 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 0.027652 0.000000 0.001212 0.00000
SCALE2 0.000000 0.006657 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023066 0.00000
TER 3958 GLU A 263
TER 7902 GLU B 263
MASTER 405 0 4 22 18 0 0 6 4383 2 72 42
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