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HEADER TRANSFERASE 19-NOV-01 1KEZ
TITLE CRYSTAL STRUCTURE OF THE MACROCYCLE-FORMING THIOESTERASE
TITLE 2 DOMAIN OF ERYTHROMYCIN POLYKETIDE SYNTHASE (DEBS TE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHRONOLIDE SYNTHASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: TERMINAL THIOESTERASE DOMAIN, MODULE 6 (RESIDUES
COMPND 5 2893-3172);
COMPND 6 SYNONYM: 6-DEOXYERYTHRONOLIDE B SYNTHASE III;
COMPND 7 EC: 2.3.1.94;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21C
KEYWDS POLYKETIDE SYNTHASE, 6-DEOXYERYTHRONOLIDE SYNTHASE, MODULAR
KEYWDS 2 POLYKETIDE SYNTHASE, THIOESTERASE, 6-DEB, TE, DEBS, ALPHA,
KEYWDS 3 BETA-HYDROLASE, MACROCYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-C.TSAI,L.J.W.MIERCKE,J.KRUCINSKI,R.GOKHALE,J.C.-H.CHEN,
AUTHOR 2 P.G.FOSTER,D.E.CANE,C.KHOSLA,R.M.STROUD
REVDAT 1 09-JAN-02 1KEZ 0
JRNL AUTH S.-C.TSAI,L.J.W.MIERCKE,J.KRUCINSKI,R.GOKHALE,
JRNL AUTH 2 J.C.-H.CHEN,P.G.FOSTER,D.E.CANE,C.KHOSLA,R.M.STROUD
JRNL TITL CRYSTAL STRUCTURE OF THE MACROCYCLE-FORMING
JRNL TITL 2 THIOESTERASE DOMAIN OF THE ERYTHROMYCIN POLYKETIDE
JRNL TITL 3 SYNTHASE: VERSATILITY FROM A UNIQUE SUBSTRATE
JRNL TITL 4 CHANNEL
JRNL REF PROC.NAT.ACAD.SCI.USA V. 98 14808 2001
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : CNS LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 45998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2542
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2542
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6033
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 393
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.85000
REMARK 3 B22 (A**2) : -4.85000
REMARK 3 B33 (A**2) : 9.71000
REMARK 3 B12 (A**2) : 1.50000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.67
REMARK 3 ESD FROM SIGMAA (A) : 0.71
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.63
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.034
REMARK 3 BOND ANGLES (DEGREES) : 3.00
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.33
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KEZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-2001.
REMARK 100 THE RCSB ID CODE IS RCSB014882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-DEC-1999; 01-MAY-1998
REMARK 200 TEMPERATURE (KELVIN) : 103.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y; Y
REMARK 200 RADIATION SOURCE : ALS ; SSRL ; SSRL ; SSRL
REMARK 200 BEAMLINE : 5.0.2; 7-1; 9-1; 9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 1.08; 0.98; 0.96-1.2
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR; CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50859
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03100
REMARK 200 FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.61700
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: XTALVIEW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1 M MGCL2, HEPES 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.50000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 139.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 139.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 69.50000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 GLU A 13
REMARK 465 ALA A 14
REMARK 465 ASN A 282
REMARK 465 SER A 283
REMARK 465 SER A 284
REMARK 465 SER A 285
REMARK 465 VAL A 286
REMARK 465 ASP A 287
REMARK 465 LYS A 288
REMARK 465 LEU A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 ALA A 292
REMARK 465 LEU A 293
REMARK 465 GLU A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 LEU B 5
REMARK 465 ASP B 6
REMARK 465 SER B 7
REMARK 465 GLY B 8
REMARK 465 THR B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 ARG B 12
REMARK 465 GLU B 13
REMARK 465 ALA B 14
REMARK 465 ASN B 282
REMARK 465 SER B 283
REMARK 465 SER B 284
REMARK 465 SER B 285
REMARK 465 VAL B 286
REMARK 465 ASP B 287
REMARK 465 LYS B 288
REMARK 465 LEU B 289
REMARK 465 ALA B 290
REMARK 465 ALA B 291
REMARK 465 ALA B 292
REMARK 465 LEU B 293
REMARK 465 GLU B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 GLN C 4
REMARK 465 LEU C 5
REMARK 465 ASP C 6
REMARK 465 SER C 7
REMARK 465 GLY C 8
REMARK 465 THR C 9
REMARK 465 PRO C 10
REMARK 465 ALA C 11
REMARK 465 ARG C 12
REMARK 465 GLU C 13
REMARK 465 ALA C 14
REMARK 465 ASN C 282
REMARK 465 SER C 283
REMARK 465 SER C 284
REMARK 465 SER C 285
REMARK 465 VAL C 286
REMARK 465 ASP C 287
REMARK 465 LYS C 288
REMARK 465 LEU C 289
REMARK 465 ALA C 290
REMARK 465 ALA C 291
REMARK 465 ALA C 292
REMARK 465 LEU C 293
REMARK 465 GLU C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 147 CE MET A 147 SD -0.043
REMARK 500 MET B 116 CE MET B 116 SD 0.049
REMARK 500 MET B 234 CE MET B 234 SD 0.046
REMARK 500 MET C 262 CE MET C 262 SD -0.061
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 109 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 193 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 PHE B 44 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 ALA B 78 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 GLU B 108 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 MET B 116 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 MET B 179 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP B 200 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 THR B 252 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 ALA B 254 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 PHE B 260 N - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 ALA C 254 N - CA - C ANGL. DEV. = 8.4 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 142 -106.55 58.39
REMARK 500 LYS A 243 156.92 60.52
REMARK 500 LYS B 243 128.21 62.97
REMARK 500 MET B 262 -95.55 33.14
REMARK 500 SER C 142 -106.49 51.30
REMARK 500 LYS C 243 126.32 62.65
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 3 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH 5 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH 11 DISTANCE = 18.09 ANGSTROMS
REMARK 525 HOH 12 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH 18 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH 22 DISTANCE = 8.91 ANGSTROMS
REMARK 525 HOH 23 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH 24 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH 29 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH 32 DISTANCE = 10.31 ANGSTROMS
REMARK 525 HOH 34 DISTANCE = 8.90 ANGSTROMS
REMARK 525 HOH 35 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH 44 DISTANCE = 10.50 ANGSTROMS
REMARK 525 HOH 46 DISTANCE = 11.50 ANGSTROMS
REMARK 525 HOH 47 DISTANCE = 12.51 ANGSTROMS
REMARK 525 HOH 51 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH 59 DISTANCE = 8.72 ANGSTROMS
REMARK 525 HOH 66 DISTANCE = 12.75 ANGSTROMS
REMARK 525 HOH 67 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH 77 DISTANCE = 11.43 ANGSTROMS
REMARK 525 HOH 82 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH 83 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH 85 DISTANCE = 10.14 ANGSTROMS
REMARK 525 HOH 86 DISTANCE = 13.06 ANGSTROMS
REMARK 525 HOH 90 DISTANCE = 12.40 ANGSTROMS
REMARK 525 HOH 94 DISTANCE = 9.88 ANGSTROMS
REMARK 525 HOH 101 DISTANCE = 8.54 ANGSTROMS
REMARK 525 HOH 112 DISTANCE = 11.07 ANGSTROMS
REMARK 525 HOH 115 DISTANCE = 10.93 ANGSTROMS
REMARK 525 HOH 116 DISTANCE = 7.94 ANGSTROMS
REMARK 525 HOH 120 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH 125 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH 129 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH 136 DISTANCE = 9.73 ANGSTROMS
REMARK 525 HOH 137 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH 138 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH 141 DISTANCE = 8.66 ANGSTROMS
REMARK 525 HOH 146 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH 150 DISTANCE = 14.28 ANGSTROMS
REMARK 525 HOH 151 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH 153 DISTANCE = 9.34 ANGSTROMS
REMARK 525 HOH 157 DISTANCE = 12.20 ANGSTROMS
REMARK 525 HOH 159 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH 167 DISTANCE = 13.13 ANGSTROMS
REMARK 525 HOH 172 DISTANCE = 12.17 ANGSTROMS
REMARK 525 HOH 174 DISTANCE = 13.52 ANGSTROMS
REMARK 525 HOH 181 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH 184 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH 187 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH 191 DISTANCE = 10.78 ANGSTROMS
REMARK 525 HOH 193 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH 198 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH 200 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH 203 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH 204 DISTANCE = 11.74 ANGSTROMS
REMARK 525 HOH 205 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH 207 DISTANCE = 9.11 ANGSTROMS
REMARK 525 HOH 208 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH 209 DISTANCE = 13.02 ANGSTROMS
REMARK 525 HOH 214 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH 215 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH 218 DISTANCE = 11.61 ANGSTROMS
REMARK 525 HOH 225 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH 226 DISTANCE = 9.82 ANGSTROMS
REMARK 525 HOH 230 DISTANCE = 10.05 ANGSTROMS
REMARK 525 HOH 239 DISTANCE = 14.25 ANGSTROMS
REMARK 525 HOH 241 DISTANCE = 11.39 ANGSTROMS
REMARK 525 HOH 245 DISTANCE = 14.13 ANGSTROMS
REMARK 525 HOH 247 DISTANCE = 10.77 ANGSTROMS
REMARK 525 HOH 256 DISTANCE = 9.10 ANGSTROMS
REMARK 525 HOH 262 DISTANCE = 9.60 ANGSTROMS
REMARK 525 HOH 265 DISTANCE = 11.56 ANGSTROMS
REMARK 525 HOH 267 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH 268 DISTANCE = 9.17 ANGSTROMS
REMARK 525 HOH 269 DISTANCE = 8.28 ANGSTROMS
REMARK 525 HOH 270 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH 278 DISTANCE = 15.13 ANGSTROMS
REMARK 525 HOH 280 DISTANCE = 10.88 ANGSTROMS
REMARK 525 HOH 284 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 286 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH 295 DISTANCE = 9.45 ANGSTROMS
REMARK 525 HOH 296 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH 299 DISTANCE = 20.14 ANGSTROMS
REMARK 525 HOH 300 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH 302 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH 303 DISTANCE = 11.44 ANGSTROMS
REMARK 525 HOH 309 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH 310 DISTANCE = 14.90 ANGSTROMS
REMARK 525 HOH 311 DISTANCE = 9.74 ANGSTROMS
REMARK 525 HOH 317 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH 329 DISTANCE = 12.70 ANGSTROMS
REMARK 525 HOH 331 DISTANCE = 12.81 ANGSTROMS
REMARK 525 HOH 337 DISTANCE = 10.97 ANGSTROMS
REMARK 525 HOH 339 DISTANCE = 8.54 ANGSTROMS
REMARK 525 HOH 341 DISTANCE = 19.82 ANGSTROMS
REMARK 525 HOH 344 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH 347 DISTANCE = 16.99 ANGSTROMS
REMARK 525 HOH 354 DISTANCE = 15.67 ANGSTROMS
REMARK 525 HOH 363 DISTANCE = 10.34 ANGSTROMS
REMARK 525 HOH 364 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH 367 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH 368 DISTANCE = 13.78 ANGSTROMS
REMARK 525 HOH 373 DISTANCE = 15.45 ANGSTROMS
REMARK 525 HOH 376 DISTANCE = 10.05 ANGSTROMS
REMARK 525 HOH 377 DISTANCE = 13.20 ANGSTROMS
REMARK 525 HOH 379 DISTANCE = 10.54 ANGSTROMS
REMARK 525 HOH 383 DISTANCE = 17.34 ANGSTROMS
REMARK 525 HOH 393 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH 395 DISTANCE = 11.10 ANGSTROMS
REMARK 525 HOH 398 DISTANCE = 5.00 ANGSTROMS
REMARK 525 HOH 401 DISTANCE = 11.01 ANGSTROMS
REMARK 525 HOH 405 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH 406 DISTANCE = 11.47 ANGSTROMS
REMARK 525 HOH 408 DISTANCE = 12.49 ANGSTROMS
REMARK 525 HOH 410 DISTANCE = 22.08 ANGSTROMS
REMARK 525 HOH 415 DISTANCE = 12.62 ANGSTROMS
REMARK 525 HOH 417 DISTANCE = 9.01 ANGSTROMS
REMARK 525 HOH 420 DISTANCE = 11.55 ANGSTROMS
REMARK 525 HOH 423 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH 425 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH 428 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH 437 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 438 DISTANCE = 9.28 ANGSTROMS
REMARK 525 HOH 441 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH 443 DISTANCE = 11.45 ANGSTROMS
REMARK 525 HOH 445 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH 450 DISTANCE = 13.93 ANGSTROMS
REMARK 525 HOH 452 DISTANCE = 13.38 ANGSTROMS
REMARK 525 HOH 455 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH 456 DISTANCE = 12.06 ANGSTROMS
REMARK 525 HOH 460 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH 463 DISTANCE = 10.46 ANGSTROMS
REMARK 525 HOH 464 DISTANCE = 13.54 ANGSTROMS
REMARK 525 HOH 465 DISTANCE = 8.87 ANGSTROMS
REMARK 525 HOH 466 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH 469 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH 473 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH 474 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH 476 DISTANCE = 12.38 ANGSTROMS
REMARK 525 HOH 479 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH 481 DISTANCE = 10.11 ANGSTROMS
REMARK 525 HOH 483 DISTANCE = 12.18 ANGSTROMS
REMARK 525 HOH 484 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH 486 DISTANCE = 13.58 ANGSTROMS
REMARK 525 HOH 487 DISTANCE = 13.36 ANGSTROMS
REMARK 525 HOH 488 DISTANCE = 8.27 ANGSTROMS
REMARK 525 HOH 489 DISTANCE = 11.32 ANGSTROMS
REMARK 525 HOH 490 DISTANCE = 10.15 ANGSTROMS
REMARK 525 HOH 491 DISTANCE = 13.04 ANGSTROMS
REMARK 525 HOH 495 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH 496 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH 497 DISTANCE = 13.13 ANGSTROMS
REMARK 525 HOH 502 DISTANCE = 8.95 ANGSTROMS
REMARK 525 HOH 511 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH 512 DISTANCE = 13.00 ANGSTROMS
REMARK 525 HOH 513 DISTANCE = 16.53 ANGSTROMS
REMARK 525 HOH 518 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH 522 DISTANCE = 12.71 ANGSTROMS
REMARK 525 HOH 523 DISTANCE = 10.04 ANGSTROMS
REMARK 525 HOH 524 DISTANCE = 13.32 ANGSTROMS
REMARK 525 HOH 527 DISTANCE = 12.94 ANGSTROMS
REMARK 525 HOH 528 DISTANCE = 9.25 ANGSTROMS
REMARK 525 HOH 531 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 534 DISTANCE = 10.12 ANGSTROMS
REMARK 525 HOH 536 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 538 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH 539 DISTANCE = 10.18 ANGSTROMS
REMARK 525 HOH 541 DISTANCE = 8.43 ANGSTROMS
REMARK 525 HOH 542 DISTANCE = 12.12 ANGSTROMS
REMARK 525 HOH 543 DISTANCE = 8.87 ANGSTROMS
REMARK 525 HOH 544 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH 545 DISTANCE = 9.96 ANGSTROMS
REMARK 525 HOH 546 DISTANCE = 12.76 ANGSTROMS
REMARK 525 HOH 554 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH 555 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH 556 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH 557 DISTANCE = 8.26 ANGSTROMS
REMARK 525 HOH 558 DISTANCE = 10.64 ANGSTROMS
REMARK 525 HOH 559 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH 560 DISTANCE = 8.81 ANGSTROMS
REMARK 525 HOH 561 DISTANCE = 17.62 ANGSTROMS
REMARK 525 HOH 562 DISTANCE = 10.37 ANGSTROMS
REMARK 525 HOH 565 DISTANCE = 10.66 ANGSTROMS
REMARK 525 HOH 569 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH 571 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH 576 DISTANCE = 12.38 ANGSTROMS
REMARK 525 HOH 580 DISTANCE = 8.61 ANGSTROMS
REMARK 525 HOH 581 DISTANCE = 11.42 ANGSTROMS
REMARK 525 HOH 582 DISTANCE = 8.50 ANGSTROMS
REMARK 525 HOH 583 DISTANCE = 12.94 ANGSTROMS
REMARK 525 HOH 586 DISTANCE = 10.12 ANGSTROMS
REMARK 525 HOH 587 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH 589 DISTANCE = 10.22 ANGSTROMS
REMARK 525 HOH 591 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH 593 DISTANCE = 8.66 ANGSTROMS
REMARK 525 HOH 595 DISTANCE = 17.22 ANGSTROMS
REMARK 525 HOH 597 DISTANCE = 11.42 ANGSTROMS
REMARK 525 HOH 599 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH 601 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH 604 DISTANCE = 16.81 ANGSTROMS
REMARK 525 HOH 605 DISTANCE = 11.32 ANGSTROMS
REMARK 525 HOH 607 DISTANCE = 11.94 ANGSTROMS
REMARK 525 HOH 610 DISTANCE = 11.08 ANGSTROMS
REMARK 525 HOH 612 DISTANCE = 11.69 ANGSTROMS
REMARK 525 HOH 617 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH 620 DISTANCE = 14.84 ANGSTROMS
REMARK 525 HOH 624 DISTANCE = 10.05 ANGSTROMS
REMARK 525 HOH 629 DISTANCE = 15.80 ANGSTROMS
REMARK 525 HOH 632 DISTANCE = 14.92 ANGSTROMS
REMARK 525 HOH 634 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH 635 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH 641 DISTANCE = 12.33 ANGSTROMS
REMARK 525 HOH 642 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH 644 DISTANCE = 15.11 ANGSTROMS
REMARK 525 HOH 649 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH 651 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH 654 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH 655 DISTANCE = 14.20 ANGSTROMS
REMARK 525 HOH 658 DISTANCE = 8.76 ANGSTROMS
REMARK 525 HOH 662 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH 664 DISTANCE = 14.09 ANGSTROMS
REMARK 525 HOH 667 DISTANCE = 14.07 ANGSTROMS
REMARK 525 HOH 674 DISTANCE = 12.63 ANGSTROMS
REMARK 525 HOH 678 DISTANCE = 10.29 ANGSTROMS
REMARK 525 HOH 680 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH 682 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH 685 DISTANCE = 8.94 ANGSTROMS
REMARK 525 HOH 691 DISTANCE = 11.04 ANGSTROMS
REMARK 525 HOH 692 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH 694 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH 701 DISTANCE = 14.64 ANGSTROMS
REMARK 525 HOH 707 DISTANCE = 13.19 ANGSTROMS
REMARK 525 HOH 708 DISTANCE = 12.17 ANGSTROMS
REMARK 525 HOH 721 DISTANCE = 7.80 ANGSTROMS
REMARK 525 HOH 727 DISTANCE = 12.89 ANGSTROMS
REMARK 525 HOH 729 DISTANCE = 12.65 ANGSTROMS
REMARK 525 HOH 734 DISTANCE = 14.30 ANGSTROMS
REMARK 525 HOH 740 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH 743 DISTANCE = 10.91 ANGSTROMS
REMARK 525 HOH 748 DISTANCE = 12.21 ANGSTROMS
REMARK 525 HOH 754 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH 760 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH 773 DISTANCE = 11.18 ANGSTROMS
DBREF 1KEZ A 4 283 SWS Q03133 ERY3_SACER 2893 3172
DBREF 1KEZ B 4 283 SWS Q03133 ERY3_SACER 2893 3172
DBREF 1KEZ C 4 283 SWS Q03133 ERY3_SACER 2893 3172
SEQADV 1KEZ MET A 1 Q03133 CLONING ARTIFACT
SEQADV 1KEZ ALA A 2 Q03133 CLONING ARTIFACT
SEQADV 1KEZ SER A 3 Q03133 CLONING ARTIFACT
SEQADV 1KEZ SER A 284 Q03133 HIS TAG
SEQADV 1KEZ SER A 285 Q03133 HIS TAG
SEQADV 1KEZ VAL A 286 Q03133 HIS TAG
SEQADV 1KEZ ASP A 287 Q03133 HIS TAG
SEQADV 1KEZ LYS A 288 Q03133 HIS TAG
SEQADV 1KEZ LEU A 289 Q03133 HIS TAG
SEQADV 1KEZ ALA A 290 Q03133 HIS TAG
SEQADV 1KEZ ALA A 291 Q03133 HIS TAG
SEQADV 1KEZ ALA A 292 Q03133 HIS TAG
SEQADV 1KEZ LEU A 293 Q03133 HIS TAG
SEQADV 1KEZ GLU A 294 Q03133 HIS TAG
SEQADV 1KEZ HIS A 295 Q03133 HIS TAG
SEQADV 1KEZ HIS A 296 Q03133 HIS TAG
SEQADV 1KEZ HIS A 297 Q03133 HIS TAG
SEQADV 1KEZ HIS A 298 Q03133 HIS TAG
SEQADV 1KEZ HIS A 299 Q03133 HIS TAG
SEQADV 1KEZ HIS A 300 Q03133 HIS TAG
SEQADV 1KEZ MET B 1 Q03133 CLONING ARTIFACT
SEQADV 1KEZ ALA B 2 Q03133 CLONING ARTIFACT
SEQADV 1KEZ SER B 3 Q03133 CLONING ARTIFACT
SEQADV 1KEZ SER B 284 Q03133 HIS TAG
SEQADV 1KEZ SER B 285 Q03133 HIS TAG
SEQADV 1KEZ VAL B 286 Q03133 HIS TAG
SEQADV 1KEZ ASP B 287 Q03133 HIS TAG
SEQADV 1KEZ LYS B 288 Q03133 HIS TAG
SEQADV 1KEZ LEU B 289 Q03133 HIS TAG
SEQADV 1KEZ ALA B 290 Q03133 HIS TAG
SEQADV 1KEZ ALA B 291 Q03133 HIS TAG
SEQADV 1KEZ ALA B 292 Q03133 HIS TAG
SEQADV 1KEZ LEU B 293 Q03133 HIS TAG
SEQADV 1KEZ GLU B 294 Q03133 HIS TAG
SEQADV 1KEZ HIS B 295 Q03133 HIS TAG
SEQADV 1KEZ HIS B 296 Q03133 HIS TAG
SEQADV 1KEZ HIS B 297 Q03133 HIS TAG
SEQADV 1KEZ HIS B 298 Q03133 HIS TAG
SEQADV 1KEZ HIS B 299 Q03133 HIS TAG
SEQADV 1KEZ HIS B 300 Q03133 HIS TAG
SEQADV 1KEZ MET C 1 Q03133 CLONING ARTIFACT
SEQADV 1KEZ ALA C 2 Q03133 CLONING ARTIFACT
SEQADV 1KEZ SER C 3 Q03133 CLONING ARTIFACT
SEQADV 1KEZ SER C 284 Q03133 HIS TAG
SEQADV 1KEZ SER C 285 Q03133 HIS TAG
SEQADV 1KEZ VAL C 286 Q03133 HIS TAG
SEQADV 1KEZ ASP C 287 Q03133 HIS TAG
SEQADV 1KEZ LYS C 288 Q03133 HIS TAG
SEQADV 1KEZ LEU C 289 Q03133 HIS TAG
SEQADV 1KEZ ALA C 290 Q03133 HIS TAG
SEQADV 1KEZ ALA C 291 Q03133 HIS TAG
SEQADV 1KEZ ALA C 292 Q03133 HIS TAG
SEQADV 1KEZ LEU C 293 Q03133 HIS TAG
SEQADV 1KEZ GLU C 294 Q03133 HIS TAG
SEQADV 1KEZ HIS C 295 Q03133 HIS TAG
SEQADV 1KEZ HIS C 296 Q03133 HIS TAG
SEQADV 1KEZ HIS C 297 Q03133 HIS TAG
SEQADV 1KEZ HIS C 298 Q03133 HIS TAG
SEQADV 1KEZ HIS C 299 Q03133 HIS TAG
SEQADV 1KEZ HIS C 300 Q03133 HIS TAG
SEQRES 1 A 300 MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU
SEQRES 2 A 300 ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY
SEQRES 3 A 300 VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA
SEQRES 4 A 300 GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP
SEQRES 5 A 300 GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO
SEQRES 6 A 300 GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA
SEQRES 7 A 300 ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA
SEQRES 8 A 300 LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO
SEQRES 9 A 300 GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA
SEQRES 10 A 300 ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR
SEQRES 11 A 300 GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA
SEQRES 12 A 300 GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU
SEQRES 13 A 300 ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP
SEQRES 14 A 300 VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP
SEQRES 15 A 300 LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR
SEQRES 16 A 300 VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA
SEQRES 17 A 300 TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR
SEQRES 18 A 300 GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET
SEQRES 19 A 300 GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO
SEQRES 20 A 300 PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE
SEQRES 21 A 300 THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS
SEQRES 22 A 300 ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL
SEQRES 23 A 300 ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 A 300 HIS
SEQRES 1 B 300 MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU
SEQRES 2 B 300 ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY
SEQRES 3 B 300 VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA
SEQRES 4 B 300 GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP
SEQRES 5 B 300 GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO
SEQRES 6 B 300 GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA
SEQRES 7 B 300 ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA
SEQRES 8 B 300 LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO
SEQRES 9 B 300 GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA
SEQRES 10 B 300 ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR
SEQRES 11 B 300 GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA
SEQRES 12 B 300 GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU
SEQRES 13 B 300 ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP
SEQRES 14 B 300 VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP
SEQRES 15 B 300 LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR
SEQRES 16 B 300 VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA
SEQRES 17 B 300 TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR
SEQRES 18 B 300 GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET
SEQRES 19 B 300 GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO
SEQRES 20 B 300 PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE
SEQRES 21 B 300 THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS
SEQRES 22 B 300 ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL
SEQRES 23 B 300 ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 B 300 HIS
SEQRES 1 C 300 MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU
SEQRES 2 C 300 ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY
SEQRES 3 C 300 VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA
SEQRES 4 C 300 GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP
SEQRES 5 C 300 GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO
SEQRES 6 C 300 GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA
SEQRES 7 C 300 ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA
SEQRES 8 C 300 LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO
SEQRES 9 C 300 GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA
SEQRES 10 C 300 ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR
SEQRES 11 C 300 GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA
SEQRES 12 C 300 GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU
SEQRES 13 C 300 ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP
SEQRES 14 C 300 VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP
SEQRES 15 C 300 LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR
SEQRES 16 C 300 VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA
SEQRES 17 C 300 TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR
SEQRES 18 C 300 GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET
SEQRES 19 C 300 GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO
SEQRES 20 C 300 PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE
SEQRES 21 C 300 THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS
SEQRES 22 C 300 ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL
SEQRES 23 C 300 ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 C 300 HIS
FORMUL 4 HOH *393(H2 O1)
HELIX 1 1 SER A 16 VAL A 27 1 12
HELIX 2 2 VAL A 31 ASP A 57 1 27
HELIX 3 3 GLY A 81 GLU A 84 5 4
HELIX 4 4 PHE A 85 LEU A 92 1 8
HELIX 5 5 SER A 115 GLY A 132 1 18
HELIX 6 6 SER A 142 ASP A 157 1 16
HELIX 7 7 GLN A 176 LEU A 190 1 15
HELIX 8 8 ASP A 199 TRP A 216 1 18
HELIX 9 9 THR A 261 HIS A 266 1 6
HELIX 10 10 HIS A 266 GLY A 279 1 14
HELIX 11 11 SER B 16 VAL B 27 1 12
HELIX 12 12 VAL B 31 ASP B 57 1 27
HELIX 13 13 GLY B 81 GLU B 84 5 4
HELIX 14 14 PHE B 85 LEU B 92 1 8
HELIX 15 15 SER B 115 GLY B 132 1 18
HELIX 16 16 SER B 142 ASP B 157 1 16
HELIX 17 17 GLN B 176 LEU B 190 1 15
HELIX 18 18 ASP B 199 TRP B 216 1 18
HELIX 19 19 THR B 261 HIS B 266 1 6
HELIX 20 20 HIS B 266 GLY B 279 1 14
HELIX 21 21 SER C 16 VAL C 27 1 12
HELIX 22 22 VAL C 31 ASP C 57 1 27
HELIX 23 23 GLY C 81 GLU C 84 5 4
HELIX 24 24 PHE C 85 LEU C 92 1 8
HELIX 25 25 SER C 115 GLN C 131 1 17
HELIX 26 26 SER C 142 ASP C 157 1 16
HELIX 27 27 GLN C 176 THR C 189 1 14
HELIX 28 28 ASP C 199 TRP C 216 1 18
HELIX 29 29 THR C 261 HIS C 266 1 6
HELIX 30 30 HIS C 266 LEU C 278 1 13
SHEET 1 A 2 HIS A 47 PHE A 48 0
SHEET 2 A 2 LEU A 112 PRO A 113 1 O LEU A 112 N PHE A 48
SHEET 1 B 7 VAL A 59 ALA A 62 0
SHEET 2 B 7 VAL A 98 VAL A 101 -1 O VAL A 98 N ALA A 62
SHEET 3 B 7 THR A 69 CYS A 73 1 N CYS A 72 O VAL A 101
SHEET 4 B 7 PHE A 136 HIS A 141 1 O ALA A 139 N CYS A 73
SHEET 5 B 7 GLY A 164 ILE A 168 1 O ILE A 168 N GLY A 140
SHEET 6 B 7 THR A 225 GLU A 232 1 O LEU A 226 N LEU A 167
SHEET 7 B 7 ASP A 251 ASP A 258 1 O ASP A 251 N LEU A 227
SHEET 1 C 2 HIS B 47 PHE B 48 0
SHEET 2 C 2 LEU B 112 PRO B 113 1 O LEU B 112 N PHE B 48
SHEET 1 D 7 VAL B 59 ALA B 62 0
SHEET 2 D 7 VAL B 98 VAL B 101 -1 O VAL B 98 N ALA B 62
SHEET 3 D 7 THR B 69 CYS B 73 1 N CYS B 72 O VAL B 101
SHEET 4 D 7 PHE B 136 HIS B 141 1 O VAL B 137 N ILE B 71
SHEET 5 D 7 VAL B 165 ILE B 168 1 O VAL B 166 N GLY B 140
SHEET 6 D 7 THR B 225 GLU B 232 1 O LEU B 226 N VAL B 165
SHEET 7 D 7 ASP B 251 ASP B 258 1 O ASP B 251 N LEU B 227
SHEET 1 E 2 HIS C 47 PHE C 48 0
SHEET 2 E 2 LEU C 112 PRO C 113 1 O LEU C 112 N PHE C 48
SHEET 1 F 7 VAL C 59 ALA C 62 0
SHEET 2 F 7 VAL C 98 VAL C 101 -1 O ALA C 100 N VAL C 59
SHEET 3 F 7 THR C 69 CYS C 73 1 N CYS C 72 O ARG C 99
SHEET 4 F 7 PHE C 136 HIS C 141 1 O VAL C 137 N ILE C 71
SHEET 5 F 7 VAL C 165 ILE C 168 1 O ILE C 168 N GLY C 140
SHEET 6 F 7 THR C 225 ALA C 230 1 O LEU C 226 N LEU C 167
SHEET 7 F 7 ASP C 251 VAL C 255 1 O VAL C 253 N SER C 229
CRYST1 130.500 130.500 208.500 90.00 90.00 120.00 P 31 2 1 18
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 0.007663 0.004424 0.000000 0.00000
SCALE2 0.000000 0.008848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004796 0.00000
END |