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HEADER HYDROLASE 05-DEC-02 1J1I
TITLE CRYSTAL STRUCTURE OF A HIS-TAGGED SERINE HYDROLASE INVOLVED
TITLE 2 IN THE CARBAZOLE DEGRADATION (CARC ENZYME)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: META CLEAVAGE COMPOUND HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SERINE HYDROLASE INVOLVED IN THE CARBAZOLE
COMPND 5 DEGRADATION, CARC;
COMPND 6 EC: 3.7.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: JANTHINOBACTERIUM;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: J3;
SOURCE 5 GENE: CARC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET26B(+);
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PECJ3
KEYWDS CARBAZOLE DEGRADATION, META CLEAVAGE PRODUCT HYDROLASE,
KEYWDS 2 HISTIDINE TAGGED PROTEIN, ALPHA/BETA-HYDROLASE, BETA-
KEYWDS 3 KETOLASE, DIOXIN, AROMATIC COMPOUNDS, DIBENZOFURAN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HABE,K.MORII,S.FUSHINOBU,J.W.NAM,Y.AYABE,T.YOSHIDA,
AUTHOR 2 T.WAKAGI,H.YAMANE,H.NOJIRI,T.OMORI
REVDAT 1 17-JUN-03 1J1I 0
JRNL AUTH H.HABE,K.MORII,S.FUSHINOBU,J.W.NAM,Y.AYABE,
JRNL AUTH 2 T.YOSHIDA,T.WAKAGI,H.YAMANE,H.NOJIRI,T.OMORI
JRNL TITL CRYSTAL STRUCTURE OF A HISTIDINE-TAGGED SERINE
JRNL TITL 2 HYDROLASE INVOLVED IN THE CARBAZOLE DEGRADATION
JRNL TITL 3 (CARC ENZYME).
JRNL REF BIOCHEM.BIOPHYS.RES.COMM. V. 303 631 2003
JRNL REFN ASTM BBRCA9 US ISSN 0006-291X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.NOJIRI,H.TAIRA,K.IWATA,K.MORII,J.W.NAM,T.YOSHIDA,
REMARK 1 AUTH 2 H.HABE,S.NAKAMURA,K.SHIMIZU,H.YAMANE,T.OMORI
REMARK 1 TITL THE C-C BOND HYDROLASE FROM A CARBAZOLE-DEGRADER
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 30496
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 SET) : 0.215
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1534
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4698
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 274
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2021
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.42000
REMARK 3 B22 (A**2) : 1.42000
REMARK 3 B33 (A**2) : -2.84000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.67
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.130 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.700 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 49.21
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J1I COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-2002.
REMARK 100 THE RCSB ID CODE IS RCSB005512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU ULTRAX18
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR 1.3
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR 1.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30496
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 33.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.28600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
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: PDB ENTRY 1IUP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, CITRATE, PH 5.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1/2-X,1/2-Y,1/2+Z
REMARK 290 11555 1/2-Y,1/2+X,1/2+Z
REMARK 290 12555 1/2+Y,1/2-X,1/2+Z
REMARK 290 13555 1/2-X,1/2+Y,1/2-Z
REMARK 290 14555 1/2+X,1/2-Y,1/2-Z
REMARK 290 15555 1/2+Y,1/2+X,1/2-Z
REMARK 290 16555 1/2-Y,1/2-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 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 0.00000
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 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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 65.13400
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 42.24550
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 65.13400
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 42.24550
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 65.13400
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 42.24550
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 65.13400
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 42.24550
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 65.13400
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 42.24550
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 65.13400
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 42.24550
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 65.13400
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 42.24550
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 65.13400
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 65.13400
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 42.24550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 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
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 BIOMT1 2 0.000000 -1.000000 0.000000 65.13400
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 65.13400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 42.24550
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 LEU A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 GLN A 7
REMARK 465 ILE A 8
REMARK 465 SER A 9
REMARK 465 GLU A 10
REMARK 465 LYS A 11
REMARK 465 SER A 12
REMARK 465 GLU A 13
REMARK 465 ARG A 14
REMARK 465 ILE A 146
REMARK 465 HIS A 147
REMARK 465 GLU A 148
REMARK 465 ASP A 149
REMARK 465 LEU A 150
REMARK 465 ARG A 151
REMARK 465 PRO A 152
REMARK 465 ILE A 153
REMARK 465 ILE A 154
REMARK 465 ASN A 155
REMARK 465 VAL A 283
REMARK 465 ASP A 284
REMARK 465 ILE A 285
REMARK 465 THR A 286
REMARK 465 PRO A 287
REMARK 465 ALA A 288
REMARK 465 ALA A 289
REMARK 465 ALA A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
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 TYR A 156 N TYR A 156 CA 0.035
REMARK 500 PRO A 257 CG PRO A 257 CD 0.034
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 SER A 51 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP A 55 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 67 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLU A 145 N - CA - C ANGL. DEV. =-23.9 DEGREES
REMARK 500 TRP A 252 N - CA - C ANGL. DEV. = -8.0 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 114 -115.42 39.04
DBREF 1J1I A 1 284 GB 28201210 BAC56745 1 284
SEQADV 1J1I TYR A 16 GB 28201210 PHE 16 CLONING ARTIFACT
SEQADV 1J1I ILE A 285 GB 28201210 HIS TAG
SEQADV 1J1I THR A 286 GB 28201210 HIS TAG
SEQADV 1J1I PRO A 287 GB 28201210 HIS TAG
SEQADV 1J1I ALA A 288 GB 28201210 HIS TAG
SEQADV 1J1I ALA A 289 GB 28201210 HIS TAG
SEQADV 1J1I ALA A 290 GB 28201210 HIS TAG
SEQADV 1J1I HIS A 291 GB 28201210 HIS TAG
SEQADV 1J1I HIS A 292 GB 28201210 HIS TAG
SEQADV 1J1I HIS A 293 GB 28201210 HIS TAG
SEQADV 1J1I HIS A 294 GB 28201210 HIS TAG
SEQADV 1J1I HIS A 295 GB 28201210 HIS TAG
SEQADV 1J1I HIS A 296 GB 28201210 HIS TAG
SEQRES 1 A 296 MET LEU ASN LYS ALA GLU GLN ILE SER GLU LYS SER GLU
SEQRES 2 A 296 ARG ALA TYR VAL GLU ARG PHE VAL ASN ALA GLY GLY VAL
SEQRES 3 A 296 GLU THR ARG TYR LEU GLU ALA GLY LYS GLY GLN PRO VAL
SEQRES 4 A 296 ILE LEU ILE HIS GLY GLY GLY ALA GLY ALA GLU SER GLU
SEQRES 5 A 296 GLY ASN TRP ARG ASN VAL ILE PRO ILE LEU ALA ARG HIS
SEQRES 6 A 296 TYR ARG VAL ILE ALA MET ASP MET LEU GLY PHE GLY LYS
SEQRES 7 A 296 THR ALA LYS PRO ASP ILE GLU TYR THR GLN ASP ARG ARG
SEQRES 8 A 296 ILE ARG HIS LEU HIS ASP PHE ILE LYS ALA MET ASN PHE
SEQRES 9 A 296 ASP GLY LYS VAL SER ILE VAL GLY ASN SER MET GLY GLY
SEQRES 10 A 296 ALA THR GLY LEU GLY VAL SER VAL LEU HIS SER GLU LEU
SEQRES 11 A 296 VAL ASN ALA LEU VAL LEU MET GLY SER ALA GLY LEU VAL
SEQRES 12 A 296 VAL GLU ILE HIS GLU ASP LEU ARG PRO ILE ILE ASN TYR
SEQRES 13 A 296 ASP PHE THR ARG GLU GLY MET VAL HIS LEU VAL LYS ALA
SEQRES 14 A 296 LEU THR ASN ASP GLY PHE LYS ILE ASP ASP ALA MET ILE
SEQRES 15 A 296 ASN SER ARG TYR THR TYR ALA THR ASP GLU ALA THR ARG
SEQRES 16 A 296 LYS ALA TYR VAL ALA THR MET GLN TRP ILE ARG GLU GLN
SEQRES 17 A 296 GLY GLY LEU PHE TYR ASP PRO GLU PHE ILE ARG LYS VAL
SEQRES 18 A 296 GLN VAL PRO THR LEU VAL VAL GLN GLY LYS ASP ASP LYS
SEQRES 19 A 296 VAL VAL PRO VAL GLU THR ALA TYR LYS PHE LEU ASP LEU
SEQRES 20 A 296 ILE ASP ASP SER TRP GLY TYR ILE ILE PRO HIS CYS GLY
SEQRES 21 A 296 HIS TRP ALA MET ILE GLU HIS PRO GLU ASP PHE ALA ASN
SEQRES 22 A 296 ALA THR LEU SER PHE LEU SER LEU ARG VAL ASP ILE THR
SEQRES 23 A 296 PRO ALA ALA ALA HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *174(H2 O1)
HELIX 1 1 GLU A 50 ARG A 56 1 7
HELIX 2 2 VAL A 58 ALA A 63 1 6
HELIX 3 3 THR A 87 MET A 102 1 16
HELIX 4 4 SER A 114 HIS A 127 1 14
HELIX 5 5 THR A 159 THR A 171 1 13
HELIX 6 6 ASP A 178 ASP A 191 1 14
HELIX 7 7 ASP A 191 GLN A 208 1 18
HELIX 8 8 ASP A 214 ARG A 219 1 6
HELIX 9 9 PRO A 237 ILE A 248 1 12
HELIX 10 10 TRP A 262 HIS A 267 1 6
HELIX 11 11 HIS A 267 ARG A 282 1 16
SHEET 1 A 8 VAL A 17 ALA A 23 0
SHEET 2 A 8 VAL A 26 ALA A 33 -1 O THR A 28 N VAL A 21
SHEET 3 A 8 ARG A 67 MET A 71 -1 O VAL A 68 N ALA A 33
SHEET 4 A 8 PRO A 38 ILE A 42 1 N VAL A 39 O ILE A 69
SHEET 5 A 8 VAL A 108 ASN A 113 1 O VAL A 111 N ILE A 42
SHEET 6 A 8 VAL A 131 MET A 137 1 O VAL A 135 N ILE A 110
SHEET 7 A 8 THR A 225 GLY A 230 1 O VAL A 228 N LEU A 136
SHEET 8 A 8 SER A 251 ILE A 256 1 O TRP A 252 N THR A 225
CRYST1 130.268 130.268 84.491 90.00 90.00 90.00 I 4 2 2 16
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 0.007676 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007676 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011836 0.00000
TER 2022 ARG A 282
MASTER 363 0 0 11 8 0 0 6 2195 1 0 23
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