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HEADER BIOSYNTHETIC PROTEIN 25-JUL-18 6E6U
TITLE VARIANT C89S OF DIECKMANN CYCLASE, NCMC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIECKMANN CYCLASE, NCMC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROTHRIX SYRINGAE;
SOURCE 3 ORGANISM_TAXID: 103733;
SOURCE 4 ATCC: 51364;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DIECKMANN CYCLASE, OFF-LOADING, DIECKMANN CONDENSATION, BIOSYNTHETIC
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.P.COGAN,S.K.NAIR
REVDAT 3 21-OCT-20 6E6U 1 JRNL REMARK
REVDAT 2 12-FEB-20 6E6U 1 JRNL
REVDAT 1 31-JUL-19 6E6U 0
JRNL AUTH D.P.COGAN,J.LY,S.K.NAIR
JRNL TITL STRUCTURAL BASIS FOR ENZYMATIC OFF-LOADING OF HYBRID
JRNL TITL 2 POLYKETIDES BY DIECKMANN CONDENSATION.
JRNL REF ACS CHEM.BIOL. 2020
JRNL REFN ESSN 1554-8937
JRNL PMID 33017142
JRNL DOI 10.1021/ACSCHEMBIO.0C00579
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 67900
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3570
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4997
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 296
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 519
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : -0.82000
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): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.629
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4022 ; 0.021 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3784 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5491 ; 2.084 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8663 ; 1.158 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 528 ; 5.916 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 170 ;34.390 ;22.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 569 ;12.879 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;20.231 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 633 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4620 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 882 ; 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): 2124 ; 2.322 ; 2.118
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2123 ; 2.320 ; 2.117
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2648 ; 3.240 ; 3.167
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2649 ; 3.241 ; 3.167
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1898 ; 3.477 ; 2.474
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1890 ; 3.461 ; 2.472
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2831 ; 5.092 ; 3.564
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4651 ; 8.421 ;27.885
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4448 ; 7.465 ;26.660
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 6E6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71503
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 80.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.14100
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: PHASER
REMARK 200 STARTING MODEL: 6E6Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM SULFATE, 2.5% PEG 400,
REMARK 280 0.1 M HEPES PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 39.16150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.58075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.74225
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 15
REMARK 465 ALA A 16
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 PRO B 4
REMARK 465 PRO B 15
REMARK 465 ALA B 16
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP B 185 CG OD1 OD2
REMARK 470 GLU B 189 CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 73 CD GLU A 73 OE1 -0.067
REMARK 500 ARG B 70 CZ ARG B 70 NH1 0.090
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 LEU A 19 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ASP A 24 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 178 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 259 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 259 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LEU B 19 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ASP B 24 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP B 24 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 81 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 81 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 108 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 108 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 GLU B 247 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG B 259 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 259 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 269 NE - CZ - NH1 ANGL. DEV. = 3.2 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 89 -131.54 57.72
REMARK 500 ALA B 27 81.72 -152.86
REMARK 500 ALA B 33 151.19 -48.18
REMARK 500 SER B 89 -131.15 54.95
REMARK 500 ALA B 183 13.49 -155.76
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 B 674 DISTANCE = 5.94 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
DBREF1 6E6U A 1 272 UNP A0A1X9WEN9_9PSEU
DBREF2 6E6U A A0A1X9WEN9 1 272
DBREF1 6E6U B 1 272 UNP A0A1X9WEN9_9PSEU
DBREF2 6E6U B A0A1X9WEN9 1 272
SEQADV 6E6U SER A -2 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6U ASN A -1 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6U ALA A 0 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6U SER A 89 UNP A0A1X9WEN CYS 89 ENGINEERED MUTATION
SEQADV 6E6U SER B -2 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6U ASN B -1 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6U ALA B 0 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6U SER B 89 UNP A0A1X9WEN CYS 89 ENGINEERED MUTATION
SEQRES 1 A 275 SER ASN ALA MET THR ALA PRO ARG ALA TRP ARG PRO ILE
SEQRES 2 A 275 ALA GLY GLY PRO PRO ALA GLY PRO LEU VAL LEU ALA VAL
SEQRES 3 A 275 ASP PHE ALA ALA THR GLY ARG PRO GLU ALA ALA PHE ALA
SEQRES 4 A 275 ASP LEU VAL ALA ARG LEU ASP PRO GLY THR GLU VAL TRP
SEQRES 5 A 275 GLU SER LEU GLN PRO PRO LEU GLY THR GLU THR GLY MET
SEQRES 6 A 275 VAL ALA GLU ASP TYR VAL THR ARG TRP GLU GLU GLU VAL
SEQRES 7 A 275 ARG ALA SER GLY ARG ARG ILE GLY ALA VAL LEU GLY PHE
SEQRES 8 A 275 SER ALA GLY SER ALA PHE ALA GLY GLU LEU ALA VAL ARG
SEQRES 9 A 275 LEU ALA ARG SER GLN PRO ARG SER PRO ARG LEU VAL VAL
SEQRES 10 A 275 PHE ASP PRO GLU SER PRO THR THR SER THR LEU TYR TYR
SEQRES 11 A 275 GLN PHE ARG LYS VAL VAL GLU SER LEU ALA GLY VAL LEU
SEQRES 12 A 275 GLY GLU GLN ALA ALA ARG GLU ALA LEU ALA GLU GLY THR
SEQRES 13 A 275 ALA ALA ALA ASP ARG ILE GLY ASP VAL GLU GLY LEU GLY
SEQRES 14 A 275 ALA GLU LEU VAL ARG VAL PHE THR ALA ALA GLY ARG ALA
SEQRES 15 A 275 ALA CYS ALA ALA ALA ASP LEU ASP ASP GLU PHE ALA ASP
SEQRES 16 A 275 GLU LEU THR ALA THR TYR ARG SER PHE VAL SER TYR LEU
SEQRES 17 A 275 VAL ALA ALA ALA ALA VAL ASP HIS VAL LYS CYS TRP SER
SEQRES 18 A 275 GLY ALA VAL ALA VAL SER SER ALA THR PRO THR SER GLY
SEQRES 19 A 275 LEU ASN PRO LEU ASP PRO ALA ALA ARG ALA ALA LEU VAL
SEQRES 20 A 275 GLU ARG GLU LEU THR PHE ASP VAL HIS HIS ALA ASP LEU
SEQRES 21 A 275 LEU ARG ASP PRO GLY VAL ALA ARG ALA VAL ALA ARG LEU
SEQRES 22 A 275 LEU ALA
SEQRES 1 B 275 SER ASN ALA MET THR ALA PRO ARG ALA TRP ARG PRO ILE
SEQRES 2 B 275 ALA GLY GLY PRO PRO ALA GLY PRO LEU VAL LEU ALA VAL
SEQRES 3 B 275 ASP PHE ALA ALA THR GLY ARG PRO GLU ALA ALA PHE ALA
SEQRES 4 B 275 ASP LEU VAL ALA ARG LEU ASP PRO GLY THR GLU VAL TRP
SEQRES 5 B 275 GLU SER LEU GLN PRO PRO LEU GLY THR GLU THR GLY MET
SEQRES 6 B 275 VAL ALA GLU ASP TYR VAL THR ARG TRP GLU GLU GLU VAL
SEQRES 7 B 275 ARG ALA SER GLY ARG ARG ILE GLY ALA VAL LEU GLY PHE
SEQRES 8 B 275 SER ALA GLY SER ALA PHE ALA GLY GLU LEU ALA VAL ARG
SEQRES 9 B 275 LEU ALA ARG SER GLN PRO ARG SER PRO ARG LEU VAL VAL
SEQRES 10 B 275 PHE ASP PRO GLU SER PRO THR THR SER THR LEU TYR TYR
SEQRES 11 B 275 GLN PHE ARG LYS VAL VAL GLU SER LEU ALA GLY VAL LEU
SEQRES 12 B 275 GLY GLU GLN ALA ALA ARG GLU ALA LEU ALA GLU GLY THR
SEQRES 13 B 275 ALA ALA ALA ASP ARG ILE GLY ASP VAL GLU GLY LEU GLY
SEQRES 14 B 275 ALA GLU LEU VAL ARG VAL PHE THR ALA ALA GLY ARG ALA
SEQRES 15 B 275 ALA CYS ALA ALA ALA ASP LEU ASP ASP GLU PHE ALA ASP
SEQRES 16 B 275 GLU LEU THR ALA THR TYR ARG SER PHE VAL SER TYR LEU
SEQRES 17 B 275 VAL ALA ALA ALA ALA VAL ASP HIS VAL LYS CYS TRP SER
SEQRES 18 B 275 GLY ALA VAL ALA VAL SER SER ALA THR PRO THR SER GLY
SEQRES 19 B 275 LEU ASN PRO LEU ASP PRO ALA ALA ARG ALA ALA LEU VAL
SEQRES 20 B 275 GLU ARG GLU LEU THR PHE ASP VAL HIS HIS ALA ASP LEU
SEQRES 21 B 275 LEU ARG ASP PRO GLY VAL ALA ARG ALA VAL ALA ARG LEU
SEQRES 22 B 275 LEU ALA
HET SO4 A 301 5
HET SO4 B 301 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *519(H2 O)
HELIX 1 AA1 ALA A 34 ALA A 40 1 7
HELIX 2 AA2 VAL A 63 GLY A 79 1 17
HELIX 3 AA3 ALA A 90 GLN A 106 1 17
HELIX 4 AA4 THR A 121 LEU A 136 1 16
HELIX 5 AA5 LEU A 136 GLY A 141 1 6
HELIX 6 AA6 GLY A 141 ILE A 159 1 19
HELIX 7 AA7 ASP A 161 ALA A 183 1 23
HELIX 8 AA8 ASP A 187 VAL A 211 1 25
HELIX 9 AA9 ASP A 212 SER A 218 1 7
HELIX 10 AB1 ASP A 236 VAL A 244 1 9
HELIX 11 AB2 HIS A 253 ARG A 259 5 7
HELIX 12 AB3 ASP A 260 ALA A 272 1 13
HELIX 13 AB4 ALA B 34 ARG B 41 1 8
HELIX 14 AB5 VAL B 63 GLY B 79 1 17
HELIX 15 AB6 ALA B 90 GLN B 106 1 17
HELIX 16 AB7 THR B 121 LEU B 136 1 16
HELIX 17 AB8 LEU B 136 GLY B 141 1 6
HELIX 18 AB9 GLY B 141 ILE B 159 1 19
HELIX 19 AC1 ASP B 161 ASP B 185 1 25
HELIX 20 AC2 ASP B 187 VAL B 211 1 25
HELIX 21 AC3 ASP B 212 TRP B 217 1 6
HELIX 22 AC4 ASP B 236 VAL B 244 1 9
HELIX 23 AC5 HIS B 253 ARG B 259 5 7
HELIX 24 AC6 ASP B 260 ALA B 272 1 13
SHEET 1 AA1 7 TRP A 7 ALA A 11 0
SHEET 2 AA1 7 GLU A 47 SER A 51 -1 O GLU A 50 N ARG A 8
SHEET 3 AA1 7 LEU A 19 VAL A 23 1 N VAL A 20 O TRP A 49
SHEET 4 AA1 7 ILE A 82 PHE A 88 1 O LEU A 86 N LEU A 21
SHEET 5 AA1 7 ARG A 111 PHE A 115 1 O PHE A 115 N GLY A 87
SHEET 6 AA1 7 VAL A 221 SER A 224 1 O VAL A 223 N VAL A 114
SHEET 7 AA1 7 ARG A 246 THR A 249 1 O ARG A 246 N ALA A 222
SHEET 1 AA2 7 TRP B 7 ALA B 11 0
SHEET 2 AA2 7 VAL B 48 SER B 51 -1 O VAL B 48 N ILE B 10
SHEET 3 AA2 7 LEU B 19 VAL B 23 1 N ALA B 22 O SER B 51
SHEET 4 AA2 7 ILE B 82 PHE B 88 1 O LEU B 86 N LEU B 21
SHEET 5 AA2 7 ARG B 111 PHE B 115 1 O PHE B 115 N GLY B 87
SHEET 6 AA2 7 VAL B 221 SER B 224 1 O VAL B 223 N VAL B 114
SHEET 7 AA2 7 ARG B 246 THR B 249 1 O ARG B 246 N ALA B 222
SITE 1 AC1 6 ARG A 81 ARG A 108 PHE A 250 HOH A 485
SITE 2 AC1 6 HOH A 493 HOH A 547
SITE 1 AC2 3 PHE B 250 HOH B 483 HOH B 556
CRYST1 80.361 80.361 78.323 90.00 90.00 90.00 P 41 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 0.012444 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012768 0.00000
TER 1973 ALA A 272
TER 3938 ALA B 272
MASTER 385 0 2 24 14 0 3 6 4465 2 10 44
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