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HEADER TRANSFERASE 11-FEB-04 1VA5
TITLE ANTIGEN 85C WITH OCTYLTHIOGLUCOSIDE IN ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIGEN 85-C;
COMPND 3 CHAIN: A, B;
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: FBPC2;
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: PET29
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 1VA5 1 JRNL
REVDAT 1 06-JUL-04 1VA5 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. 2.02 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) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 507000.610
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 43409
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) : 0.187
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2172
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) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6561
REMARK 3 BIN R VALUE (WORKING SET) : 0.1830
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 318
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4406
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 252
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.75000
REMARK 3 B22 (A**2) : -3.91000
REMARK 3 B33 (A**2) : 1.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.74000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.04
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
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) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.92
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) : 1.140 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.510 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 49.99
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 : THIO.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : THIO.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VA5 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-2004.
REMARK 100 THE RCSB ID CODE IS RCSB006398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI MIRROR + NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44080
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 38.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.11400
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1DZQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: OCTYLTHIOGLUCOSIDE, SODIUM ACETATE,
REMARK 280 IMIDAZOLE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 72.40900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.05850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.40900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.05850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 2 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 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 ALA A 283
REMARK 465 THR A 284
REMARK 465 PRO A 285
REMARK 465 PRO A 286
REMARK 465 ALA A 287
REMARK 465 ALA A 288
REMARK 465 PRO A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 ALA A 294
REMARK 465 LEU A 295
REMARK 465 GLY A 296
REMARK 465 HIS 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 ALA B 283
REMARK 465 THR B 284
REMARK 465 PRO B 285
REMARK 465 PRO B 286
REMARK 465 ALA B 287
REMARK 465 ALA B 288
REMARK 465 PRO B 289
REMARK 465 ALA B 290
REMARK 465 ALA B 291
REMARK 465 PRO B 292
REMARK 465 ALA B 293
REMARK 465 ALA B 294
REMARK 465 LEU B 295
REMARK 465 GLY B 296
REMARK 465 HIS 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 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 ARG A 3 CA ARG A 3 C 0.043
REMARK 500 MET A 192 SD MET A 192 CE 0.040
REMARK 500 PRO B 4 CG PRO B 4 CD 0.035
REMARK 500 PRO B 54 CB PRO B 54 CG 0.041
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 ARG A 3 N - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO A 4 N - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 PRO A 4 C - N - CA ANGL. DEV. = 8.9 DEGREES
REMARK 500 GLY A 5 N - CA - C ANGL. DEV. =-16.3 DEGREES
REMARK 500 ASN A 52 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 PHE A 150 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 LEU A 151 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 204 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 SER A 215 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 VAL A 251 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 TRP A 262 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASN B 52 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 PHE B 150 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 LEU B 151 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 SER B 215 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 TRP B 262 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 B 2 -76.02 105.86
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DQY RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH COVALENT INHIBITOR
REMARK 900 RELATED ID: 1DQZ RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH NOTHING BOUND
REMARK 900 RELATED ID: 1F0N RELATED DB: PDB
REMARK 900 HOMOLOGOUS PROTEIN
REMARK 900 RELATED ID: 1F0P RELATED DB: PDB
REMARK 900 HOMOLOGOUS PROTEIN WITH TREHALOSE BOUND
DBREF 1VA5 A 1 294 SWS P31953 A85C_MYCTU 47 340
DBREF 1VA5 B 1 294 SWS P31953 A85C_MYCTU 47 340
SEQADV 1VA5 MET A 0 SWS P31953 INITIATING METHIONINE
SEQADV 1VA5 LEU A 295 SWS P31953 HIS TAG
SEQADV 1VA5 GLY A 296 SWS P31953 HIS TAG
SEQADV 1VA5 HIS A 297 SWS P31953 HIS TAG
SEQADV 1VA5 HIS A 298 SWS P31953 HIS TAG
SEQADV 1VA5 HIS A 299 SWS P31953 HIS TAG
SEQADV 1VA5 HIS A 300 SWS P31953 HIS TAG
SEQADV 1VA5 HIS A 301 SWS P31953 HIS TAG
SEQADV 1VA5 HIS A 302 SWS P31953 HIS TAG
SEQADV 1VA5 MET B 0 SWS P31953 INITIATING METHIONINE
SEQADV 1VA5 LEU B 295 SWS P31953 HIS TAG
SEQADV 1VA5 GLY B 296 SWS P31953 HIS TAG
SEQADV 1VA5 HIS B 297 SWS P31953 HIS TAG
SEQADV 1VA5 HIS B 298 SWS P31953 HIS TAG
SEQADV 1VA5 HIS B 299 SWS P31953 HIS TAG
SEQADV 1VA5 HIS B 300 SWS P31953 HIS TAG
SEQADV 1VA5 HIS B 301 SWS P31953 HIS TAG
SEQADV 1VA5 HIS B 302 SWS P31953 HIS TAG
SEQRES 1 A 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 A 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 A 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 A 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 A 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 A 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 A 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 A 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 A 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 A 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 A 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 A 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 A 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 A 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 A 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 A 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 A 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 A 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 A 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 A 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 A 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 A 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 A 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLY HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 B 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 B 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 B 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 B 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 B 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 B 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 B 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 B 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 B 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 B 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 B 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 B 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 B 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 B 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 B 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 B 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 B 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 B 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 B 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 B 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 B 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 B 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLY HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET SOG 1001 20
HET SOG 1002 20
HET SOG 1003 20
HET SOG 1004 20
HETNAM SOG 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,
HETNAM 2 SOG 5-TRIOL
HETSYN SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE
FORMUL 3 SOG 4(C14 H28 O5 S1)
FORMUL 7 HOH *252(H2 O1)
HELIX 1 1 ASN A 47 THR A 53 1 7
HELIX 2 2 PRO A 54 TYR A 60 1 7
HELIX 3 3 LYS A 94 ARG A 101 1 8
HELIX 4 4 ARG A 101 GLY A 112 1 12
HELIX 5 5 SER A 124 TYR A 137 1 14
HELIX 6 6 TRP A 157 SER A 169 1 13
HELIX 7 7 ASN A 173 GLY A 179 1 7
HELIX 8 8 ASP A 183 ASN A 189 1 7
HELIX 9 9 GLN A 194 ASN A 202 1 9
HELIX 10 10 ASN A 221 ASP A 245 1 25
HELIX 11 11 SER A 261 GLY A 282 1 22
HELIX 12 12 ASN B 47 THR B 53 1 7
HELIX 13 13 PRO B 54 TYR B 60 1 7
HELIX 14 14 LYS B 94 ARG B 101 1 8
HELIX 15 15 ARG B 101 GLY B 112 1 12
HELIX 16 16 SER B 124 TYR B 137 1 14
HELIX 17 17 TRP B 157 SER B 169 1 13
HELIX 18 18 ASN B 173 GLY B 179 1 7
HELIX 19 19 PRO B 184 ASN B 189 1 6
HELIX 20 20 GLN B 194 ASN B 201 1 8
HELIX 21 21 ASN B 221 ASP B 245 1 25
HELIX 22 22 SER B 261 GLY B 282 1 22
SHEET 1 A 8 VAL A 8 SER A 15 0
SHEET 2 A 8 ARG A 20 GLN A 27 -1 O PHE A 26 N GLU A 9
SHEET 3 A 8 SER A 65 PRO A 69 -1 O MET A 68 N GLN A 25
SHEET 4 A 8 ALA A 33 LEU A 36 1 N LEU A 36 O ILE A 67
SHEET 5 A 8 ALA A 119 LEU A 123 1 O ALA A 119 N TYR A 35
SHEET 6 A 8 TYR A 143 LEU A 147 1 O ALA A 145 N ALA A 120
SHEET 7 A 8 ARG A 204 TYR A 208 1 O TYR A 208 N SER A 146
SHEET 8 A 8 GLY A 250 ASN A 253 1 O VAL A 251 N VAL A 207
SHEET 1 B 8 VAL B 8 SER B 15 0
SHEET 2 B 8 ARG B 20 GLN B 27 -1 O PHE B 26 N GLU B 9
SHEET 3 B 8 SER B 65 PRO B 69 -1 O MET B 68 N GLN B 25
SHEET 4 B 8 ALA B 33 LEU B 36 1 N LEU B 36 O ILE B 67
SHEET 5 B 8 ALA B 119 LEU B 123 1 O ALA B 119 N TYR B 35
SHEET 6 B 8 TYR B 143 LEU B 147 1 O ALA B 145 N ALA B 120
SHEET 7 B 8 ARG B 204 TYR B 208 1 O TYR B 208 N SER B 146
SHEET 8 B 8 GLY B 250 ASN B 253 1 O VAL B 251 N VAL B 207
CRYST1 144.818 68.117 82.281 90.00 119.60 90.00 C 1 2 1 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 0.006905 0.000000 0.003923 0.00000
SCALE2 0.000000 0.014681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013978 0.00000
TER 2204 GLY A 282
TER 4408 GLY B 282
MASTER 339 0 4 22 16 0 0 6 4738 2 80 48
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