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HEADER TRANSFERASE 20-FEB-04 1SFR
TITLE CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS ANTIGEN
TITLE 2 85A PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIGEN 85-A;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 2.3.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: FBPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.RONNING,V.VISSA,G.S.BESRA,J.T.BELISLE,J.C.SACCHETTINI
REVDAT 2 07-SEP-04 1SFR 1 JRNL
REVDAT 1 06-JUL-04 1SFR 0
JRNL AUTH D.R.RONNING,V.VISSA,G.S.BESRA,J.T.BELISLE,
JRNL AUTH 2 J.C.SACCHETTINI
JRNL TITL MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85A AND 85C
JRNL TITL 2 STRUCTURES CONFIRM BINDING ORIENTATION AND
JRNL TITL 3 CONSERVED SUBSTRATE SPECIFICITY
JRNL REF J.BIOL.CHEM. V. 279 36771 2004
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 481759.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 50656
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) : 0.222
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2550
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7456
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 375
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6499
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.37
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.88
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) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.730 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 35.28
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.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 1SFR COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-2004.
REMARK 100 THE RCSB ID CODE IS RCSB021672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14BMC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GE 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52327
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE, SODIUM ACETATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 1/2+X,1/2-Y,-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 50.64450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.64450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 65.71500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 144.33100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 65.71500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 144.33100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.64450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 65.71500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 144.33100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 50.64450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 65.71500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 144.33100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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
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: B
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 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 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 THR A 288
REMARK 465 GLY A 289
REMARK 465 PRO A 290
REMARK 465 ALA A 291
REMARK 465 PRO A 292
REMARK 465 GLN A 293
REMARK 465 GLY A 294
REMARK 465 ALA A 295
REMARK 465 LEU A 296
REMARK 465 GLY A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 THR B 288
REMARK 465 GLY B 289
REMARK 465 PRO B 290
REMARK 465 ALA B 291
REMARK 465 PRO B 292
REMARK 465 GLN B 293
REMARK 465 GLY B 294
REMARK 465 ALA B 295
REMARK 465 LEU B 296
REMARK 465 GLY B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 ALA C 0
REMARK 465 PHE C 1
REMARK 465 SER C 2
REMARK 465 ARG C 3
REMARK 465 PRO C 4
REMARK 465 GLY C 5
REMARK 465 LEU C 6
REMARK 465 PRO C 7
REMARK 465 PRO C 286
REMARK 465 ASN C 287
REMARK 465 THR C 288
REMARK 465 GLY C 289
REMARK 465 PRO C 290
REMARK 465 ALA C 291
REMARK 465 PRO C 292
REMARK 465 GLN C 293
REMARK 465 GLY C 294
REMARK 465 ALA C 295
REMARK 465 LEU C 296
REMARK 465 GLY C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
REMARK 465 HIS C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
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 168 CG MET A 168 SD -0.045
REMARK 500 MET B 70 SD MET B 70 CE 0.045
REMARK 500 MET B 179 SD MET B 179 CE 0.040
REMARK 500 MET C 159 SD MET C 159 CE 0.058
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 PRO A 7 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 TYR A 10 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLN A 25 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASN A 54 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU A 125 CA - CB - CG ANGL. DEV. = -7.9 DEGREES
REMARK 500 LEU A 152 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 LEU A 153 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 LEU A 194 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP A 264 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 TYR B 10 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 GLN B 12 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASN B 54 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 LYS B 96 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASN B 112 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 LEU B 152 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU B 153 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 PRO B 155 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 LEU C 125 CA - CB - CG ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU C 152 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 HIS C 250 N - CA - C ANGL. DEV. = -9.1 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 126 -117.12 54.66
REMARK 500 ALA A 158 -119.79 46.41
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DQY RELATED DB: PDB
REMARK 900 RELATED ID: 1DQZ RELATED DB: PDB
REMARK 900 RELATED ID: 1F0P RELATED DB: PDB
REMARK 900 RELATED ID: 1F0N RELATED DB: PDB
REMARK 900 RELATED ID: 1VA5 RELATED DB: PDB
DBREF 1SFR A 0 295 SWS P17944 A85A_MYCTU 43 338
DBREF 1SFR B 0 295 SWS P17944 A85A_MYCTU 43 338
DBREF 1SFR C 0 295 SWS P17944 A85A_MYCTU 43 338
SEQADV 1SFR LEU A 296 SWS P17944 HIS TAG
SEQADV 1SFR GLY A 297 SWS P17944 HIS TAG
SEQADV 1SFR HIS A 298 SWS P17944 HIS TAG
SEQADV 1SFR HIS A 299 SWS P17944 HIS TAG
SEQADV 1SFR HIS A 300 SWS P17944 HIS TAG
SEQADV 1SFR HIS A 301 SWS P17944 HIS TAG
SEQADV 1SFR HIS A 302 SWS P17944 HIS TAG
SEQADV 1SFR HIS A 303 SWS P17944 HIS TAG
SEQADV 1SFR LEU B 296 SWS P17944 HIS TAG
SEQADV 1SFR GLY B 297 SWS P17944 HIS TAG
SEQADV 1SFR HIS B 298 SWS P17944 HIS TAG
SEQADV 1SFR HIS B 299 SWS P17944 HIS TAG
SEQADV 1SFR HIS B 300 SWS P17944 HIS TAG
SEQADV 1SFR HIS B 301 SWS P17944 HIS TAG
SEQADV 1SFR HIS B 302 SWS P17944 HIS TAG
SEQADV 1SFR HIS B 303 SWS P17944 HIS TAG
SEQADV 1SFR LEU C 296 SWS P17944 HIS TAG
SEQADV 1SFR GLY C 297 SWS P17944 HIS TAG
SEQADV 1SFR HIS C 298 SWS P17944 HIS TAG
SEQADV 1SFR HIS C 299 SWS P17944 HIS TAG
SEQADV 1SFR HIS C 300 SWS P17944 HIS TAG
SEQADV 1SFR HIS C 301 SWS P17944 HIS TAG
SEQADV 1SFR HIS C 302 SWS P17944 HIS TAG
SEQADV 1SFR HIS C 303 SWS P17944 HIS TAG
SEQRES 1 A 304 ALA PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 A 304 VAL PRO SER PRO SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 A 304 PHE GLN SER GLY GLY ALA ASN SER PRO ALA LEU TYR LEU
SEQRES 4 A 304 LEU ASP GLY LEU ARG ALA GLN ASP ASP PHE SER GLY TRP
SEQRES 5 A 304 ASP ILE ASN THR PRO ALA PHE GLU TRP TYR ASP GLN SER
SEQRES 6 A 304 GLY LEU SER VAL VAL MET PRO VAL GLY GLY GLN SER SER
SEQRES 7 A 304 PHE TYR SER ASP TRP TYR GLN PRO ALA CYS GLY LYS ALA
SEQRES 8 A 304 GLY CYS GLN THR TYR LYS TRP GLU THR PHE LEU THR SER
SEQRES 9 A 304 GLU LEU PRO GLY TRP LEU GLN ALA ASN ARG HIS VAL LYS
SEQRES 10 A 304 PRO THR GLY SER ALA VAL VAL GLY LEU SER MET ALA ALA
SEQRES 11 A 304 SER SER ALA LEU THR LEU ALA ILE TYR HIS PRO GLN GLN
SEQRES 12 A 304 PHE VAL TYR ALA GLY ALA MET SER GLY LEU LEU ASP PRO
SEQRES 13 A 304 SER GLN ALA MET GLY PRO THR LEU ILE GLY LEU ALA MET
SEQRES 14 A 304 GLY ASP ALA GLY GLY TYR LYS ALA SER ASP MET TRP GLY
SEQRES 15 A 304 PRO LYS GLU ASP PRO ALA TRP GLN ARG ASN ASP PRO LEU
SEQRES 16 A 304 LEU ASN VAL GLY LYS LEU ILE ALA ASN ASN THR ARG VAL
SEQRES 17 A 304 TRP VAL TYR CYS GLY ASN GLY LYS PRO SER ASP LEU GLY
SEQRES 18 A 304 GLY ASN ASN LEU PRO ALA LYS PHE LEU GLU GLY PHE VAL
SEQRES 19 A 304 ARG THR SER ASN ILE LYS PHE GLN ASP ALA TYR ASN ALA
SEQRES 20 A 304 GLY GLY GLY HIS ASN GLY VAL PHE ASP PHE PRO ASP SER
SEQRES 21 A 304 GLY THR HIS SER TRP GLU TYR TRP GLY ALA GLN LEU ASN
SEQRES 22 A 304 ALA MET LYS PRO ASP LEU GLN ARG ALA LEU GLY ALA THR
SEQRES 23 A 304 PRO ASN THR GLY PRO ALA PRO GLN GLY ALA LEU GLY HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
SEQRES 1 B 304 ALA PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 B 304 VAL PRO SER PRO SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 B 304 PHE GLN SER GLY GLY ALA ASN SER PRO ALA LEU TYR LEU
SEQRES 4 B 304 LEU ASP GLY LEU ARG ALA GLN ASP ASP PHE SER GLY TRP
SEQRES 5 B 304 ASP ILE ASN THR PRO ALA PHE GLU TRP TYR ASP GLN SER
SEQRES 6 B 304 GLY LEU SER VAL VAL MET PRO VAL GLY GLY GLN SER SER
SEQRES 7 B 304 PHE TYR SER ASP TRP TYR GLN PRO ALA CYS GLY LYS ALA
SEQRES 8 B 304 GLY CYS GLN THR TYR LYS TRP GLU THR PHE LEU THR SER
SEQRES 9 B 304 GLU LEU PRO GLY TRP LEU GLN ALA ASN ARG HIS VAL LYS
SEQRES 10 B 304 PRO THR GLY SER ALA VAL VAL GLY LEU SER MET ALA ALA
SEQRES 11 B 304 SER SER ALA LEU THR LEU ALA ILE TYR HIS PRO GLN GLN
SEQRES 12 B 304 PHE VAL TYR ALA GLY ALA MET SER GLY LEU LEU ASP PRO
SEQRES 13 B 304 SER GLN ALA MET GLY PRO THR LEU ILE GLY LEU ALA MET
SEQRES 14 B 304 GLY ASP ALA GLY GLY TYR LYS ALA SER ASP MET TRP GLY
SEQRES 15 B 304 PRO LYS GLU ASP PRO ALA TRP GLN ARG ASN ASP PRO LEU
SEQRES 16 B 304 LEU ASN VAL GLY LYS LEU ILE ALA ASN ASN THR ARG VAL
SEQRES 17 B 304 TRP VAL TYR CYS GLY ASN GLY LYS PRO SER ASP LEU GLY
SEQRES 18 B 304 GLY ASN ASN LEU PRO ALA LYS PHE LEU GLU GLY PHE VAL
SEQRES 19 B 304 ARG THR SER ASN ILE LYS PHE GLN ASP ALA TYR ASN ALA
SEQRES 20 B 304 GLY GLY GLY HIS ASN GLY VAL PHE ASP PHE PRO ASP SER
SEQRES 21 B 304 GLY THR HIS SER TRP GLU TYR TRP GLY ALA GLN LEU ASN
SEQRES 22 B 304 ALA MET LYS PRO ASP LEU GLN ARG ALA LEU GLY ALA THR
SEQRES 23 B 304 PRO ASN THR GLY PRO ALA PRO GLN GLY ALA LEU GLY HIS
SEQRES 24 B 304 HIS HIS HIS HIS HIS
SEQRES 1 C 304 ALA PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 C 304 VAL PRO SER PRO SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 C 304 PHE GLN SER GLY GLY ALA ASN SER PRO ALA LEU TYR LEU
SEQRES 4 C 304 LEU ASP GLY LEU ARG ALA GLN ASP ASP PHE SER GLY TRP
SEQRES 5 C 304 ASP ILE ASN THR PRO ALA PHE GLU TRP TYR ASP GLN SER
SEQRES 6 C 304 GLY LEU SER VAL VAL MET PRO VAL GLY GLY GLN SER SER
SEQRES 7 C 304 PHE TYR SER ASP TRP TYR GLN PRO ALA CYS GLY LYS ALA
SEQRES 8 C 304 GLY CYS GLN THR TYR LYS TRP GLU THR PHE LEU THR SER
SEQRES 9 C 304 GLU LEU PRO GLY TRP LEU GLN ALA ASN ARG HIS VAL LYS
SEQRES 10 C 304 PRO THR GLY SER ALA VAL VAL GLY LEU SER MET ALA ALA
SEQRES 11 C 304 SER SER ALA LEU THR LEU ALA ILE TYR HIS PRO GLN GLN
SEQRES 12 C 304 PHE VAL TYR ALA GLY ALA MET SER GLY LEU LEU ASP PRO
SEQRES 13 C 304 SER GLN ALA MET GLY PRO THR LEU ILE GLY LEU ALA MET
SEQRES 14 C 304 GLY ASP ALA GLY GLY TYR LYS ALA SER ASP MET TRP GLY
SEQRES 15 C 304 PRO LYS GLU ASP PRO ALA TRP GLN ARG ASN ASP PRO LEU
SEQRES 16 C 304 LEU ASN VAL GLY LYS LEU ILE ALA ASN ASN THR ARG VAL
SEQRES 17 C 304 TRP VAL TYR CYS GLY ASN GLY LYS PRO SER ASP LEU GLY
SEQRES 18 C 304 GLY ASN ASN LEU PRO ALA LYS PHE LEU GLU GLY PHE VAL
SEQRES 19 C 304 ARG THR SER ASN ILE LYS PHE GLN ASP ALA TYR ASN ALA
SEQRES 20 C 304 GLY GLY GLY HIS ASN GLY VAL PHE ASP PHE PRO ASP SER
SEQRES 21 C 304 GLY THR HIS SER TRP GLU TYR TRP GLY ALA GLN LEU ASN
SEQRES 22 C 304 ALA MET LYS PRO ASP LEU GLN ARG ALA LEU GLY ALA THR
SEQRES 23 C 304 PRO ASN THR GLY PRO ALA PRO GLN GLY ALA LEU GLY HIS
SEQRES 24 C 304 HIS HIS HIS HIS HIS
FORMUL 4 HOH *58(H2 O1)
HELIX 1 1 SER A 49 THR A 55 1 7
HELIX 2 2 PRO A 56 ASP A 62 1 7
HELIX 3 3 LYS A 96 SER A 103 1 8
HELIX 4 4 SER A 103 HIS A 114 1 12
HELIX 5 5 SER A 126 HIS A 139 1 14
HELIX 6 6 MET A 159 ALA A 171 1 13
HELIX 7 7 LYS A 175 GLY A 181 1 7
HELIX 8 8 PRO A 186 ASN A 191 1 6
HELIX 9 9 ASN A 196 ASN A 204 1 9
HELIX 10 10 ASN A 223 GLY A 247 1 25
HELIX 11 11 SER A 263 MET A 274 1 12
HELIX 12 12 MET A 274 GLY A 283 1 10
HELIX 13 13 SER B 49 THR B 55 1 7
HELIX 14 14 PRO B 56 ASP B 62 1 7
HELIX 15 15 LYS B 96 SER B 103 1 8
HELIX 16 16 SER B 103 HIS B 114 1 12
HELIX 17 17 SER B 126 HIS B 139 1 14
HELIX 18 18 MET B 159 ALA B 171 1 13
HELIX 19 19 LYS B 175 GLY B 181 1 7
HELIX 20 20 ASP B 185 ASN B 191 1 7
HELIX 21 21 PRO B 193 LEU B 195 5 3
HELIX 22 22 ASN B 196 ASN B 203 1 8
HELIX 23 23 ASN B 223 GLY B 247 1 25
HELIX 24 24 SER B 263 GLY B 283 1 21
HELIX 25 25 SER C 49 ASN C 54 1 6
HELIX 26 26 PRO C 56 TYR C 61 1 6
HELIX 27 27 LYS C 96 SER C 103 1 8
HELIX 28 28 SER C 103 ASN C 112 1 10
HELIX 29 29 SER C 126 HIS C 139 1 14
HELIX 30 30 MET C 159 ALA C 171 1 13
HELIX 31 31 LYS C 175 GLY C 181 1 7
HELIX 32 32 PRO C 186 ASN C 191 1 6
HELIX 33 33 ASP C 192 ASN C 203 1 12
HELIX 34 34 ASN C 223 GLY C 247 1 25
HELIX 35 35 SER C 263 MET C 274 1 12
HELIX 36 36 MET C 274 GLY C 283 1 10
SHEET 1 A 8 GLU A 9 SER A 15 0
SHEET 2 A 8 ARG A 20 GLN A 27 -1 O ILE A 22 N VAL A 13
SHEET 3 A 8 SER A 67 PRO A 71 -1 O MET A 70 N GLN A 25
SHEET 4 A 8 ALA A 35 LEU A 39 1 N LEU A 36 O SER A 67
SHEET 5 A 8 SER A 120 LEU A 125 1 O ALA A 121 N TYR A 37
SHEET 6 A 8 PHE A 143 MET A 149 1 O GLY A 147 N GLY A 124
SHEET 7 A 8 ARG A 206 TYR A 210 1 O TYR A 210 N ALA A 148
SHEET 8 A 8 GLY A 252 ASP A 255 1 O VAL A 253 N VAL A 209
SHEET 1 B 2 ALA A 86 GLY A 88 0
SHEET 2 B 2 GLY A 91 GLN A 93 -1 O GLN A 93 N ALA A 86
SHEET 1 C 8 GLU B 9 SER B 15 0
SHEET 2 C 8 ARG B 20 GLN B 27 -1 O PHE B 26 N GLU B 9
SHEET 3 C 8 SER B 67 PRO B 71 -1 O MET B 70 N GLN B 25
SHEET 4 C 8 ALA B 35 LEU B 39 1 N LEU B 38 O VAL B 69
SHEET 5 C 8 SER B 120 LEU B 125 1 O ALA B 121 N TYR B 37
SHEET 6 C 8 PHE B 143 MET B 149 1 O GLY B 147 N VAL B 122
SHEET 7 C 8 ARG B 206 TYR B 210 1 O ARG B 206 N ALA B 146
SHEET 8 C 8 GLY B 252 ASP B 255 1 O VAL B 253 N VAL B 207
SHEET 1 D 2 ALA B 86 GLY B 88 0
SHEET 2 D 2 GLY B 91 GLN B 93 -1 O GLN B 93 N ALA B 86
SHEET 1 E 8 GLU C 9 SER C 15 0
SHEET 2 E 8 ARG C 20 GLN C 27 -1 O ILE C 22 N VAL C 13
SHEET 3 E 8 SER C 67 PRO C 71 -1 O MET C 70 N GLN C 25
SHEET 4 E 8 ALA C 35 LEU C 39 1 N LEU C 36 O SER C 67
SHEET 5 E 8 SER C 120 LEU C 125 1 O ALA C 121 N TYR C 37
SHEET 6 E 8 PHE C 143 MET C 149 1 O GLY C 147 N VAL C 122
SHEET 7 E 8 ARG C 206 TYR C 210 1 O ARG C 206 N VAL C 144
SHEET 8 E 8 GLY C 252 ASP C 255 1 O VAL C 253 N VAL C 207
SSBOND 1 CYS A 87 CYS A 92
SSBOND 2 CYS B 87 CYS B 92
SSBOND 3 CYS C 87 CYS C 92
CRYST1 131.430 288.662 101.289 90.00 90.00 90.00 C 2 2 21 24
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 0.007609 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009873 0.00000
TER 2192 ASN A 287
TER 4384 ASN B 287
TER 6502 THR C 285
MASTER 377 0 0 36 28 0 0 6 6557 3 6 72
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