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HEADER HYDROLASE 20-AUG-03 1Q7T TITLE RV1170 (MSHB) FROM MYCOBACTERIUM TUBERCULOSIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RV1170; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: MSHB, LMBE-RELATED PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 GENE: RV1170 (MSHB); SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)(PRP); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX-HT KEYWDS MODIFIED ROSSMANN FOLD, STRUCTURAL GENOMICS, PSI, PROTEIN KEYWDS 2 STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM, KEYWDS 3 TBSGC EXPDTA X-RAY DIFFRACTION AUTHOR A.A.MCCARTHY,N.A.PETERSON,R.KNIJFF,E.N.BAKER,TB STRUCTURAL AUTHOR 2 GENOMICS CONSORTIUM (TBSGC) REVDAT 2 01-FEB-05 1Q7T 1 AUTHOR KEYWDS REMARK REVDAT 1 13-JAN-04 1Q7T 0 JRNL AUTH A.A.MCCARTHY,N.A.PETERSON,R.KNIJFF,E.N.BAKER JRNL TITL CRYSTAL STRUCTURE OF MSHB FROM MYCOBACTERIUM JRNL TITL 2 TUBERCULOSIS, A DEACETYLASE INVOLVED IN MYCOTHIOL JRNL TITL 3 BIOSYNTHESIS. JRNL REF J.MOL.BIOL. V. 335 1131 2004 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.35 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 45788 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) : 0.190 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2295 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 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) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7046 REMARK 3 BIN R VALUE (WORKING SET) : 0.2030 REMARK 3 BIN FREE R VALUE : 0.2480 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 370 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4484 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 56 REMARK 3 SOLVENT ATOMS : 326 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.15000 REMARK 3 B22 (A**2) : -0.11000 REMARK 3 B33 (A**2) : -0.04000 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) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : 0.09 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) : 0.23 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.73 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) : 1.480 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.360 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.160 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.300 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.37 REMARK 3 BSOL : 40.21 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 : BOG.PARAM REMARK 3 PARAMETER FILE 4 : SULFATE.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Q7T COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB020024. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-APR-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.30 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL 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 : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45788 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.07100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.8300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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: MIR REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, AMMONIUM SULFATE, SODIUM REMARK 280 CACODYLATE, BETA-OCTYLGLUCOSIDE, PH 6.3, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 35.84500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.82500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.87000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.82500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.84500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.87000 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 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -24 REMARK 465 SER A -23 REMARK 465 TYR A -22 REMARK 465 TYR A -21 REMARK 465 HIS A -20 REMARK 465 HIS A -19 REMARK 465 HIS A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 ASP A -14 REMARK 465 TYR A -13 REMARK 465 SER A 165 REMARK 465 GLY A 166 REMARK 465 THR A 167 REMARK 465 ALA A 168 REMARK 465 ASP A 169 REMARK 465 HIS A 170 REMARK 465 MET B -24 REMARK 465 SER B -23 REMARK 465 TYR B -22 REMARK 465 TYR B -21 REMARK 465 HIS B -20 REMARK 465 HIS B -19 REMARK 465 HIS B -18 REMARK 465 HIS B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 ASP B -14 REMARK 465 TYR B -13 REMARK 465 ASP B -12 REMARK 465 ILE B -11 REMARK 465 PRO B -10 REMARK 465 THR B -9 REMARK 465 THR B -8 REMARK 465 GLU B -7 REMARK 465 ASN B -6 REMARK 465 LEU B -5 REMARK 465 TYR B -4 REMARK 465 PHE B -3 REMARK 465 GLN B -2 REMARK 465 GLY B -1 REMARK 465 ALA B 0 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 SER B 165 REMARK 465 GLY B 166 REMARK 465 THR B 167 REMARK 465 ALA B 168 REMARK 465 ASP B 169 REMARK 465 HIS B 170 REMARK 465 ALA B 300 REMARK 465 SER B 301 REMARK 465 GLY B 302 REMARK 465 THR B 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 PRO A 130 CB PRO A 130 CG 0.030 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 GLN A -2 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 GLY A -1 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 SER A 82 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 ASP A 95 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 TRP A 182 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 ARG A 203 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 VAL A 227 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 GLU A 289 N - CA - C ANGL. DEV. =-11.6 DEGREES REMARK 500 SER B 82 N - CA - C ANGL. DEV. = 7.5 DEGREES REMARK 500 ASP B 95 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 PRO B 204 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 VAL B 227 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 GLU B 289 N - CA - C ANGL. DEV. =-11.6 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 ALA A 99 146.45 62.11 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: RV1170 RELATED DB: TARGETDB DBREF 1Q7T A 1 303 UNP O50426 O50426_MYCTU 1 303 DBREF 1Q7T B 1 303 UNP O50426 O50426_MYCTU 1 303 SEQADV 1Q7T MET A -24 UNP O50426 HIS TAG SEQADV 1Q7T SER A -23 UNP O50426 HIS TAG SEQADV 1Q7T TYR A -22 UNP O50426 HIS TAG SEQADV 1Q7T TYR A -21 UNP O50426 HIS TAG SEQADV 1Q7T HIS A -20 UNP O50426 HIS TAG SEQADV 1Q7T HIS A -19 UNP O50426 HIS TAG SEQADV 1Q7T HIS A -18 UNP O50426 HIS TAG SEQADV 1Q7T HIS A -17 UNP O50426 HIS TAG SEQADV 1Q7T HIS A -16 UNP O50426 HIS TAG SEQADV 1Q7T HIS A -15 UNP O50426 HIS TAG SEQADV 1Q7T ASP A -14 UNP O50426 HIS TAG SEQADV 1Q7T TYR A -13 UNP O50426 HIS TAG SEQADV 1Q7T ASP A -12 UNP O50426 HIS TAG SEQADV 1Q7T ILE A -11 UNP O50426 HIS TAG SEQADV 1Q7T PRO A -10 UNP O50426 HIS TAG SEQADV 1Q7T THR A -9 UNP O50426 HIS TAG SEQADV 1Q7T THR A -8 UNP O50426 HIS TAG SEQADV 1Q7T GLU A -7 UNP O50426 HIS TAG SEQADV 1Q7T ASN A -6 UNP O50426 HIS TAG SEQADV 1Q7T LEU A -5 UNP O50426 HIS TAG SEQADV 1Q7T TYR A -4 UNP O50426 HIS TAG SEQADV 1Q7T PHE A -3 UNP O50426 HIS TAG SEQADV 1Q7T GLN A -2 UNP O50426 HIS TAG SEQADV 1Q7T GLY A -1 UNP O50426 HIS TAG SEQADV 1Q7T ALA A 0 UNP O50426 HIS TAG SEQADV 1Q7T MET B -24 UNP O50426 HIS TAG SEQADV 1Q7T SER B -23 UNP O50426 HIS TAG SEQADV 1Q7T TYR B -22 UNP O50426 HIS TAG SEQADV 1Q7T TYR B -21 UNP O50426 HIS TAG SEQADV 1Q7T HIS B -20 UNP O50426 HIS TAG SEQADV 1Q7T HIS B -19 UNP O50426 HIS TAG SEQADV 1Q7T HIS B -18 UNP O50426 HIS TAG SEQADV 1Q7T HIS B -17 UNP O50426 HIS TAG SEQADV 1Q7T HIS B -16 UNP O50426 HIS TAG SEQADV 1Q7T HIS B -15 UNP O50426 HIS TAG SEQADV 1Q7T ASP B -14 UNP O50426 HIS TAG SEQADV 1Q7T TYR B -13 UNP O50426 HIS TAG SEQADV 1Q7T ASP B -12 UNP O50426 HIS TAG SEQADV 1Q7T ILE B -11 UNP O50426 HIS TAG SEQADV 1Q7T PRO B -10 UNP O50426 HIS TAG SEQADV 1Q7T THR B -9 UNP O50426 HIS TAG SEQADV 1Q7T THR B -8 UNP O50426 HIS TAG SEQADV 1Q7T GLU B -7 UNP O50426 HIS TAG SEQADV 1Q7T ASN B -6 UNP O50426 HIS TAG SEQADV 1Q7T LEU B -5 UNP O50426 HIS TAG SEQADV 1Q7T TYR B -4 UNP O50426 HIS TAG SEQADV 1Q7T PHE B -3 UNP O50426 HIS TAG SEQADV 1Q7T GLN B -2 UNP O50426 HIS TAG SEQADV 1Q7T GLY B -1 UNP O50426 HIS TAG SEQADV 1Q7T ALA B 0 UNP O50426 HIS TAG SEQRES 1 A 328 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP SEQRES 2 A 328 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET SEQRES 3 A 328 SER GLU THR PRO ARG LEU LEU PHE VAL HIS ALA HIS PRO SEQRES 4 A 328 ASP ASP GLU SER LEU SER ASN GLY ALA THR ILE ALA HIS SEQRES 5 A 328 TYR THR SER ARG GLY ALA GLN VAL HIS VAL VAL THR CYS SEQRES 6 A 328 THR LEU GLY GLU GLU GLY GLU VAL ILE GLY ASP ARG TRP SEQRES 7 A 328 ALA GLN LEU THR ALA ASP HIS ALA ASP GLN LEU GLY GLY SEQRES 8 A 328 TYR ARG ILE GLY GLU LEU THR ALA ALA LEU ARG ALA LEU SEQRES 9 A 328 GLY VAL SER ALA PRO ILE TYR LEU GLY GLY ALA GLY ARG SEQRES 10 A 328 TRP ARG ASP SER GLY MET ALA GLY THR ASP GLN ARG SER SEQRES 11 A 328 GLN ARG ARG PHE VAL ASP ALA ASP PRO ARG GLN THR VAL SEQRES 12 A 328 GLY ALA LEU VAL ALA ILE ILE ARG GLU LEU ARG PRO HIS SEQRES 13 A 328 VAL VAL VAL THR TYR ASP PRO ASN GLY GLY TYR GLY HIS SEQRES 14 A 328 PRO ASP HIS VAL HIS THR HIS THR VAL THR THR ALA ALA SEQRES 15 A 328 VAL ALA ALA ALA GLY VAL GLY SER GLY THR ALA ASP HIS SEQRES 16 A 328 PRO GLY ASP PRO TRP THR VAL PRO LYS PHE TYR TRP THR SEQRES 17 A 328 VAL LEU GLY LEU SER ALA LEU ILE SER GLY ALA ARG ALA SEQRES 18 A 328 LEU VAL PRO ASP ASP LEU ARG PRO GLU TRP VAL LEU PRO SEQRES 19 A 328 ARG ALA ASP GLU ILE ALA PHE GLY TYR SER ASP ASP GLY SEQRES 20 A 328 ILE ASP ALA VAL VAL GLU ALA ASP GLU GLN ALA ARG ALA SEQRES 21 A 328 ALA LYS VAL ALA ALA LEU ALA ALA HIS ALA THR GLN VAL SEQRES 22 A 328 VAL VAL GLY PRO THR GLY ARG ALA ALA ALA LEU SER ASN SEQRES 23 A 328 ASN LEU ALA LEU PRO ILE LEU ALA ASP GLU HIS TYR VAL SEQRES 24 A 328 LEU ALA GLY GLY SER ALA GLY ALA ARG ASP GLU ARG GLY SEQRES 25 A 328 TRP GLU THR ASP LEU LEU ALA GLY LEU GLY PHE THR ALA SEQRES 26 A 328 SER GLY THR SEQRES 1 B 328 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP SEQRES 2 B 328 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET SEQRES 3 B 328 SER GLU THR PRO ARG LEU LEU PHE VAL HIS ALA HIS PRO SEQRES 4 B 328 ASP ASP GLU SER LEU SER ASN GLY ALA THR ILE ALA HIS SEQRES 5 B 328 TYR THR SER ARG GLY ALA GLN VAL HIS VAL VAL THR CYS SEQRES 6 B 328 THR LEU GLY GLU GLU GLY GLU VAL ILE GLY ASP ARG TRP SEQRES 7 B 328 ALA GLN LEU THR ALA ASP HIS ALA ASP GLN LEU GLY GLY SEQRES 8 B 328 TYR ARG ILE GLY GLU LEU THR ALA ALA LEU ARG ALA LEU SEQRES 9 B 328 GLY VAL SER ALA PRO ILE TYR LEU GLY GLY ALA GLY ARG SEQRES 10 B 328 TRP ARG ASP SER GLY MET ALA GLY THR ASP GLN ARG SER SEQRES 11 B 328 GLN ARG ARG PHE VAL ASP ALA ASP PRO ARG GLN THR VAL SEQRES 12 B 328 GLY ALA LEU VAL ALA ILE ILE ARG GLU LEU ARG PRO HIS SEQRES 13 B 328 VAL VAL VAL THR TYR ASP PRO ASN GLY GLY TYR GLY HIS SEQRES 14 B 328 PRO ASP HIS VAL HIS THR HIS THR VAL THR THR ALA ALA SEQRES 15 B 328 VAL ALA ALA ALA GLY VAL GLY SER GLY THR ALA ASP HIS SEQRES 16 B 328 PRO GLY ASP PRO TRP THR VAL PRO LYS PHE TYR TRP THR SEQRES 17 B 328 VAL LEU GLY LEU SER ALA LEU ILE SER GLY ALA ARG ALA SEQRES 18 B 328 LEU VAL PRO ASP ASP LEU ARG PRO GLU TRP VAL LEU PRO SEQRES 19 B 328 ARG ALA ASP GLU ILE ALA PHE GLY TYR SER ASP ASP GLY SEQRES 20 B 328 ILE ASP ALA VAL VAL GLU ALA ASP GLU GLN ALA ARG ALA SEQRES 21 B 328 ALA LYS VAL ALA ALA LEU ALA ALA HIS ALA THR GLN VAL SEQRES 22 B 328 VAL VAL GLY PRO THR GLY ARG ALA ALA ALA LEU SER ASN SEQRES 23 B 328 ASN LEU ALA LEU PRO ILE LEU ALA ASP GLU HIS TYR VAL SEQRES 24 B 328 LEU ALA GLY GLY SER ALA GLY ALA ARG ASP GLU ARG GLY SEQRES 25 B 328 TRP GLU THR ASP LEU LEU ALA GLY LEU GLY PHE THR ALA SEQRES 26 B 328 SER GLY THR HET BOG 401 20 HET BOG 402 13 HET BOG 403 13 HET SO4 501 5 HET SO4 502 5 HETNAM BOG B-OCTYLGLUCOSIDE HETNAM SO4 SULFATE ION FORMUL 3 BOG 3(C14 H28 O6) FORMUL 6 SO4 2(O4 S 2-) FORMUL 8 HOH *326(H2 O) HELIX 1 1 ASP A 15 ARG A 31 1 17 HELIX 2 2 TRP A 53 THR A 57 5 5 HELIX 3 3 GLN A 63 LEU A 79 1 17 HELIX 4 4 ARG A 108 ALA A 112 5 5 HELIX 5 5 ASP A 113 ARG A 129 1 17 HELIX 6 6 HIS A 144 GLY A 162 1 19 HELIX 7 7 LEU A 187 ALA A 196 1 10 HELIX 8 8 VAL A 198 LEU A 202 5 5 HELIX 9 9 ARG A 210 ILE A 214 5 5 HELIX 10 10 ASP A 230 HIS A 244 1 15 HELIX 11 11 ASP B 15 ARG B 31 1 17 HELIX 12 12 TRP B 53 THR B 57 5 5 HELIX 13 13 GLN B 63 LEU B 79 1 17 HELIX 14 14 ARG B 108 ALA B 112 5 5 HELIX 15 15 ASP B 113 ARG B 129 1 17 HELIX 16 16 HIS B 144 ALA B 161 1 18 HELIX 17 17 GLY B 186 ALA B 196 1 11 HELIX 18 18 VAL B 198 LEU B 202 5 5 HELIX 19 19 ARG B 210 ILE B 214 5 5 HELIX 20 20 ASP B 230 HIS B 244 1 15 SHEET 1 A 3 MET A 1 SER A 2 0 SHEET 2 A 3 TYR A -4 GLN A -2 -1 N GLN A -2 O MET A 1 SHEET 3 A 3 PHE A 298 ALA A 300 -1 O THR A 299 N PHE A -3 SHEET 1 B 6 ILE A 85 TYR A 86 0 SHEET 2 B 6 GLN A 34 THR A 39 1 N THR A 39 O ILE A 85 SHEET 3 B 6 ARG A 6 HIS A 11 1 N HIS A 11 O VAL A 38 SHEET 4 B 6 VAL A 132 TYR A 136 1 O VAL A 132 N LEU A 8 SHEET 5 B 6 LYS A 179 GLY A 186 1 O TYR A 181 N VAL A 133 SHEET 6 B 6 GLY A 217 TYR A 218 1 O TYR A 218 N LEU A 185 SHEET 1 C 7 ILE A 85 TYR A 86 0 SHEET 2 C 7 GLN A 34 THR A 39 1 N THR A 39 O ILE A 85 SHEET 3 C 7 ARG A 6 HIS A 11 1 N HIS A 11 O VAL A 38 SHEET 4 C 7 VAL A 132 TYR A 136 1 O VAL A 132 N LEU A 8 SHEET 5 C 7 LYS A 179 GLY A 186 1 O TYR A 181 N VAL A 133 SHEET 6 C 7 ASP A 270 GLY A 277 -1 O ALA A 276 N PHE A 180 SHEET 7 C 7 ALA A 225 GLU A 228 -1 N ALA A 225 O TYR A 273 SHEET 1 D 3 VAL A 249 VAL A 250 0 SHEET 2 D 3 ALA A 256 ALA A 258 -1 O ALA A 258 N VAL A 249 SHEET 3 D 3 ALA A 264 PRO A 266 -1 O LEU A 265 N ALA A 257 SHEET 1 E 7 ILE B 85 TYR B 86 0 SHEET 2 E 7 GLN B 34 THR B 39 1 N THR B 39 O ILE B 85 SHEET 3 E 7 ARG B 6 HIS B 11 1 N HIS B 11 O VAL B 38 SHEET 4 E 7 VAL B 132 TYR B 136 1 O VAL B 132 N LEU B 8 SHEET 5 E 7 LYS B 179 VAL B 184 1 O TYR B 181 N VAL B 133 SHEET 6 E 7 ASP B 270 GLY B 277 -1 O ALA B 276 N PHE B 180 SHEET 7 E 7 ALA B 225 GLU B 228 -1 N ALA B 225 O TYR B 273 SHEET 1 F 3 VAL B 249 VAL B 250 0 SHEET 2 F 3 ALA B 256 ALA B 258 -1 O ALA B 258 N VAL B 249 SHEET 3 F 3 ALA B 264 PRO B 266 -1 O LEU B 265 N ALA B 257 CRYST1 71.690 83.740 95.650 90.00 90.00 90.00 P 21 21 21 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 0.013949 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011942 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010455 0.00000