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HEADER TRANSFERASE 01-DEC-03 1RO7 TITLE STRUCTURAL ANALYSIS OF THE SIALYLTRANSFERASE CSTII FROM TITLE 2 CAMPYLOBACTER JEJUNI IN COMPLEX WITH A SUBSTRATE ANALOGUE, TITLE 3 CMP-3FNEUAC. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-2,3/8-SIALYLTRANSFERASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 EC: 2.4.99.-; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAMPYLOBACTER JEJUNI; SOURCE 3 GENE: CST; 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: PET41A KEYWDS MIXED ALPHA/BETA, ROSSMANN FOLD EXPDTA X-RAY DIFFRACTION AUTHOR C.P.CHIU,A.G.WATTS,L.L.LAIRSON,M.GILBERT,D.LIM, AUTHOR 2 W.W.WAKARCHUK,S.G.WITHERS,N.C.STRYNADKA REVDAT 1 03-FEB-04 1RO7 0 JRNL AUTH C.P.CHIU,A.G.WATTS,L.L.LAIRSON,M.GILBERT,D.LIM, JRNL AUTH 2 W.W.WAKARCHUK,S.G.WITHERS,N.C.STRYNADKA JRNL TITL STRUCTURAL ANALYSIS OF THE SIALYLTRANSFERASE CSTII JRNL TITL 2 FROM CAMPYLOBACTER JEJUNI IN COMPLEX WITH A JRNL TITL 3 SUBSTRATE ANALOG. JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 163 2004 JRNL REFN US ISSN 1545-9993 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1876668.640 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 99667 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) : 0.217 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 5034 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 15501 REMARK 3 BIN R VALUE (WORKING SET) : 0.2910 REMARK 3 BIN FREE R VALUE : 0.3230 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 855 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8162 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 168 REMARK 3 SOLVENT ATOMS : 338 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.23000 REMARK 3 B22 (A**2) : 5.33000 REMARK 3 B33 (A**2) : -0.10000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -3.78000 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) : 0.22 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) : 0.25 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.66 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) : 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 : FLAT MODEL REMARK 3 KSOL : 0.34 REMARK 3 BSOL : 41.01 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 : ION.PARAM REMARK 3 PARAMETER FILE 4 : LIGAND.PAR REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2 REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3 REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4 REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RO7 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB020910. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JUN-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 9.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X8C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS 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 : 99748 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05400 REMARK 200 FOR THE DATA SET : 23.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.52600 REMARK 200 FOR SHELL : 2.000 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.62 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, SODIUM CHLORIDE, REMARK 280 BICINE, PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 18K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 33.01550 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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 4 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, C, D 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 ASN A 259 REMARK 465 TYR B 156 REMARK 465 GLN B 157 REMARK 465 ASN B 158 REMARK 465 GLY B 159 REMARK 465 SER B 160 REMARK 465 SER B 161 REMARK 465 TYR B 162 REMARK 465 ALA B 163 REMARK 465 PHE B 164 REMARK 465 ASP B 165 REMARK 465 THR B 166 REMARK 465 LYS B 167 REMARK 465 LYS B 179 REMARK 465 ASN B 180 REMARK 465 ASP B 181 REMARK 465 ASN B 182 REMARK 465 SER B 183 REMARK 465 HIS B 184 REMARK 465 TYR B 185 REMARK 465 ILE B 186 REMARK 465 GLY B 187 REMARK 465 ASN B 259 REMARK 465 GLN C 157 REMARK 465 ASN C 158 REMARK 465 GLY C 159 REMARK 465 SER C 160 REMARK 465 ASN C 177 REMARK 465 PHE C 178 REMARK 465 LYS C 179 REMARK 465 ASN C 180 REMARK 465 ASP C 181 REMARK 465 ASN C 182 REMARK 465 SER C 183 REMARK 465 HIS C 184 REMARK 465 TYR C 185 REMARK 465 ILE C 186 REMARK 465 ILE C 258 REMARK 465 ASN C 259 REMARK 465 GLN D 157 REMARK 465 ASN D 158 REMARK 465 GLY D 159 REMARK 465 SER D 160 REMARK 465 SER D 161 REMARK 465 TYR D 162 REMARK 465 ALA D 163 REMARK 465 PHE D 164 REMARK 465 ASP D 165 REMARK 465 THR D 166 REMARK 465 LYS D 167 REMARK 465 ASN D 177 REMARK 465 PHE D 178 REMARK 465 LYS D 179 REMARK 465 ASN D 180 REMARK 465 ASP D 181 REMARK 465 ASN D 182 REMARK 465 SER D 183 REMARK 465 HIS D 184 REMARK 465 TYR D 185 REMARK 465 ASN D 259 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 GLU B 87 CB GLU B 87 CG -0.034 REMARK 500 GLN B 168 N GLN B 168 CA 0.033 REMARK 500 SER C 161 N SER C 161 CA 0.035 REMARK 500 GLY C 187 N GLY C 187 CA 0.039 REMARK 500 GLN D 168 N GLN D 168 CA 0.033 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 LYS A 3 N - CA - C ANGL. DEV. = -6.8 DEGREES REMARK 500 GLY A 8 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 ILE A 76 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 CYS A 78 N - CA - C ANGL. DEV. = -7.5 DEGREES REMARK 500 LEU A 104 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 SER A 255 N - CA - C ANGL. DEV. = 7.5 DEGREES REMARK 500 GLY B 8 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 LYS B 46 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 GLU B 72 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 ILE B 76 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 CYS B 78 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 LEU B 104 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ILE C 5 N - CA - C ANGL. DEV. = -6.8 DEGREES REMARK 500 GLY C 8 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 ASP C 17 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 LYS C 46 N - CA - C ANGL. DEV. = -7.3 DEGREES REMARK 500 ILE C 76 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 LEU C 104 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLY D 8 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 ASP D 26 N - CA - C ANGL. DEV. = -7.1 DEGREES REMARK 500 LYS D 46 N - CA - C ANGL. DEV. = -7.3 DEGREES REMARK 500 ILE D 76 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 CYS D 78 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 PHE D 95 N - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 PRO D 100 N - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 LEU D 104 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 LEU D 112 N - CA - C ANGL. DEV. = -7.1 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 ASN A 31 -117.96 40.41 REMARK 500 HIS C 188 -114.08 60.72 REMARK 500 SER C 189 153.80 67.21 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1RO8 RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH CMP DBREF 1RO7 A 1 259 UNP Q9LAK3 Q9LAK3_CAMJE 1 259 DBREF 1RO7 B 1 259 UNP Q9LAK3 Q9LAK3_CAMJE 1 259 DBREF 1RO7 C 1 259 UNP Q9LAK3 Q9LAK3_CAMJE 1 259 DBREF 1RO7 D 1 259 UNP Q9LAK3 Q9LAK3_CAMJE 1 259 SEQADV 1RO7 MSE A 1 UNP Q9LAK3 MET 1 MODIFIED RESIDUE SEQADV 1RO7 SER A 53 UNP Q9LAK3 ILE 53 ENGINEERED SEQADV 1RO7 MSE A 77 UNP Q9LAK3 MET 77 MODIFIED RESIDUE SEQADV 1RO7 MSE A 136 UNP Q9LAK3 MET 136 MODIFIED RESIDUE SEQADV 1RO7 MSE B 1 UNP Q9LAK3 MET 1 MODIFIED RESIDUE SEQADV 1RO7 SER B 53 UNP Q9LAK3 ILE 53 ENGINEERED SEQADV 1RO7 MSE B 77 UNP Q9LAK3 MET 77 MODIFIED RESIDUE SEQADV 1RO7 MSE B 136 UNP Q9LAK3 MET 136 MODIFIED RESIDUE SEQADV 1RO7 MSE C 1 UNP Q9LAK3 MET 1 MODIFIED RESIDUE SEQADV 1RO7 SER C 53 UNP Q9LAK3 ILE 53 ENGINEERED SEQADV 1RO7 MSE C 77 UNP Q9LAK3 MET 77 MODIFIED RESIDUE SEQADV 1RO7 MSE C 136 UNP Q9LAK3 MET 136 MODIFIED RESIDUE SEQADV 1RO7 MSE D 1 UNP Q9LAK3 MET 1 MODIFIED RESIDUE SEQADV 1RO7 SER D 53 UNP Q9LAK3 ILE 53 ENGINEERED SEQADV 1RO7 MSE D 77 UNP Q9LAK3 MET 77 MODIFIED RESIDUE SEQADV 1RO7 MSE D 136 UNP Q9LAK3 MET 136 MODIFIED RESIDUE SEQRES 1 A 259 MSE LYS LYS VAL ILE ILE ALA GLY ASN GLY PRO SER LEU SEQRES 2 A 259 LYS GLU ILE ASP TYR SER ARG LEU PRO ASN ASP PHE ASP SEQRES 3 A 259 VAL PHE ARG CYS ASN GLN PHE TYR PHE GLU ASP LYS TYR SEQRES 4 A 259 TYR LEU GLY LYS LYS CYS LYS ALA VAL PHE TYR ASN PRO SEQRES 5 A 259 SER LEU PHE PHE GLU GLN TYR TYR THR LEU LYS HIS LEU SEQRES 6 A 259 ILE GLN ASN GLN GLU TYR GLU THR GLU LEU ILE MSE CYS SEQRES 7 A 259 SER ASN TYR ASN GLN ALA HIS LEU GLU ASN GLU ASN PHE SEQRES 8 A 259 VAL LYS THR PHE TYR ASP TYR PHE PRO ASP ALA HIS LEU SEQRES 9 A 259 GLY TYR ASP PHE PHE LYS GLN LEU LYS ASP PHE ASN ALA SEQRES 10 A 259 TYR PHE LYS PHE HIS GLU ILE TYR PHE ASN GLN ARG ILE SEQRES 11 A 259 THR SER GLY VAL TYR MSE CYS ALA VAL ALA ILE ALA LEU SEQRES 12 A 259 GLY TYR LYS GLU ILE TYR LEU SER GLY ILE ASP PHE TYR SEQRES 13 A 259 GLN ASN GLY SER SER TYR ALA PHE ASP THR LYS GLN LYS SEQRES 14 A 259 ASN LEU LEU LYS LEU ALA PRO ASN PHE LYS ASN ASP ASN SEQRES 15 A 259 SER HIS TYR ILE GLY HIS SER LYS ASN THR ASP ILE LYS SEQRES 16 A 259 ALA LEU GLU PHE LEU GLU LYS THR TYR LYS ILE LYS LEU SEQRES 17 A 259 TYR CYS LEU CYS PRO ASN SER LEU LEU ALA ASN PHE ILE SEQRES 18 A 259 GLU LEU ALA PRO ASN LEU ASN SER ASN PHE ILE ILE GLN SEQRES 19 A 259 GLU LYS ASN ASN TYR THR LYS ASP ILE LEU ILE PRO SER SEQRES 20 A 259 SER GLU ALA TYR GLY LYS PHE SER LYS ASN ILE ASN SEQRES 1 B 259 MSE LYS LYS VAL ILE ILE ALA GLY ASN GLY PRO SER LEU SEQRES 2 B 259 LYS GLU ILE ASP TYR SER ARG LEU PRO ASN ASP PHE ASP SEQRES 3 B 259 VAL PHE ARG CYS ASN GLN PHE TYR PHE GLU ASP LYS TYR SEQRES 4 B 259 TYR LEU GLY LYS LYS CYS LYS ALA VAL PHE TYR ASN PRO SEQRES 5 B 259 SER LEU PHE PHE GLU GLN TYR TYR THR LEU LYS HIS LEU SEQRES 6 B 259 ILE GLN ASN GLN GLU TYR GLU THR GLU LEU ILE MSE CYS SEQRES 7 B 259 SER ASN TYR ASN GLN ALA HIS LEU GLU ASN GLU ASN PHE SEQRES 8 B 259 VAL LYS THR PHE TYR ASP TYR PHE PRO ASP ALA HIS LEU SEQRES 9 B 259 GLY TYR ASP PHE PHE LYS GLN LEU LYS ASP PHE ASN ALA SEQRES 10 B 259 TYR PHE LYS PHE HIS GLU ILE TYR PHE ASN GLN ARG ILE SEQRES 11 B 259 THR SER GLY VAL TYR MSE CYS ALA VAL ALA ILE ALA LEU SEQRES 12 B 259 GLY TYR LYS GLU ILE TYR LEU SER GLY ILE ASP PHE TYR SEQRES 13 B 259 GLN ASN GLY SER SER TYR ALA PHE ASP THR LYS GLN LYS SEQRES 14 B 259 ASN LEU LEU LYS LEU ALA PRO ASN PHE LYS ASN ASP ASN SEQRES 15 B 259 SER HIS TYR ILE GLY HIS SER LYS ASN THR ASP ILE LYS SEQRES 16 B 259 ALA LEU GLU PHE LEU GLU LYS THR TYR LYS ILE LYS LEU SEQRES 17 B 259 TYR CYS LEU CYS PRO ASN SER LEU LEU ALA ASN PHE ILE SEQRES 18 B 259 GLU LEU ALA PRO ASN LEU ASN SER ASN PHE ILE ILE GLN SEQRES 19 B 259 GLU LYS ASN ASN TYR THR LYS ASP ILE LEU ILE PRO SER SEQRES 20 B 259 SER GLU ALA TYR GLY LYS PHE SER LYS ASN ILE ASN SEQRES 1 C 259 MSE LYS LYS VAL ILE ILE ALA GLY ASN GLY PRO SER LEU SEQRES 2 C 259 LYS GLU ILE ASP TYR SER ARG LEU PRO ASN ASP PHE ASP SEQRES 3 C 259 VAL PHE ARG CYS ASN GLN PHE TYR PHE GLU ASP LYS TYR SEQRES 4 C 259 TYR LEU GLY LYS LYS CYS LYS ALA VAL PHE TYR ASN PRO SEQRES 5 C 259 SER LEU PHE PHE GLU GLN TYR TYR THR LEU LYS HIS LEU SEQRES 6 C 259 ILE GLN ASN GLN GLU TYR GLU THR GLU LEU ILE MSE CYS SEQRES 7 C 259 SER ASN TYR ASN GLN ALA HIS LEU GLU ASN GLU ASN PHE SEQRES 8 C 259 VAL LYS THR PHE TYR ASP TYR PHE PRO ASP ALA HIS LEU SEQRES 9 C 259 GLY TYR ASP PHE PHE LYS GLN LEU LYS ASP PHE ASN ALA SEQRES 10 C 259 TYR PHE LYS PHE HIS GLU ILE TYR PHE ASN GLN ARG ILE SEQRES 11 C 259 THR SER GLY VAL TYR MSE CYS ALA VAL ALA ILE ALA LEU SEQRES 12 C 259 GLY TYR LYS GLU ILE TYR LEU SER GLY ILE ASP PHE TYR SEQRES 13 C 259 GLN ASN GLY SER SER TYR ALA PHE ASP THR LYS GLN LYS SEQRES 14 C 259 ASN LEU LEU LYS LEU ALA PRO ASN PHE LYS ASN ASP ASN SEQRES 15 C 259 SER HIS TYR ILE GLY HIS SER LYS ASN THR ASP ILE LYS SEQRES 16 C 259 ALA LEU GLU PHE LEU GLU LYS THR TYR LYS ILE LYS LEU SEQRES 17 C 259 TYR CYS LEU CYS PRO ASN SER LEU LEU ALA ASN PHE ILE SEQRES 18 C 259 GLU LEU ALA PRO ASN LEU ASN SER ASN PHE ILE ILE GLN SEQRES 19 C 259 GLU LYS ASN ASN TYR THR LYS ASP ILE LEU ILE PRO SER SEQRES 20 C 259 SER GLU ALA TYR GLY LYS PHE SER LYS ASN ILE ASN SEQRES 1 D 259 MSE LYS LYS VAL ILE ILE ALA GLY ASN GLY PRO SER LEU SEQRES 2 D 259 LYS GLU ILE ASP TYR SER ARG LEU PRO ASN ASP PHE ASP SEQRES 3 D 259 VAL PHE ARG CYS ASN GLN PHE TYR PHE GLU ASP LYS TYR SEQRES 4 D 259 TYR LEU GLY LYS LYS CYS LYS ALA VAL PHE TYR ASN PRO SEQRES 5 D 259 SER LEU PHE PHE GLU GLN TYR TYR THR LEU LYS HIS LEU SEQRES 6 D 259 ILE GLN ASN GLN GLU TYR GLU THR GLU LEU ILE MSE CYS SEQRES 7 D 259 SER ASN TYR ASN GLN ALA HIS LEU GLU ASN GLU ASN PHE SEQRES 8 D 259 VAL LYS THR PHE TYR ASP TYR PHE PRO ASP ALA HIS LEU SEQRES 9 D 259 GLY TYR ASP PHE PHE LYS GLN LEU LYS ASP PHE ASN ALA SEQRES 10 D 259 TYR PHE LYS PHE HIS GLU ILE TYR PHE ASN GLN ARG ILE SEQRES 11 D 259 THR SER GLY VAL TYR MSE CYS ALA VAL ALA ILE ALA LEU SEQRES 12 D 259 GLY TYR LYS GLU ILE TYR LEU SER GLY ILE ASP PHE TYR SEQRES 13 D 259 GLN ASN GLY SER SER TYR ALA PHE ASP THR LYS GLN LYS SEQRES 14 D 259 ASN LEU LEU LYS LEU ALA PRO ASN PHE LYS ASN ASP ASN SEQRES 15 D 259 SER HIS TYR ILE GLY HIS SER LYS ASN THR ASP ILE LYS SEQRES 16 D 259 ALA LEU GLU PHE LEU GLU LYS THR TYR LYS ILE LYS LEU SEQRES 17 D 259 TYR CYS LEU CYS PRO ASN SER LEU LEU ALA ASN PHE ILE SEQRES 18 D 259 GLU LEU ALA PRO ASN LEU ASN SER ASN PHE ILE ILE GLN SEQRES 19 D 259 GLU LYS ASN ASN TYR THR LYS ASP ILE LEU ILE PRO SER SEQRES 20 D 259 SER GLU ALA TYR GLY LYS PHE SER LYS ASN ILE ASN MODRES 1RO7 MSE A 1 MET SELENOMETHIONINE MODRES 1RO7 MSE A 77 MET SELENOMETHIONINE MODRES 1RO7 MSE A 136 MET SELENOMETHIONINE MODRES 1RO7 MSE B 1 MET SELENOMETHIONINE MODRES 1RO7 MSE B 77 MET SELENOMETHIONINE MODRES 1RO7 MSE B 136 MET SELENOMETHIONINE MODRES 1RO7 MSE C 1 MET SELENOMETHIONINE MODRES 1RO7 MSE C 77 MET SELENOMETHIONINE MODRES 1RO7 MSE C 136 MET SELENOMETHIONINE MODRES 1RO7 MSE D 1 MET SELENOMETHIONINE MODRES 1RO7 MSE D 77 MET SELENOMETHIONINE MODRES 1RO7 MSE D 136 MET SELENOMETHIONINE HET MSE A 1 8 HET MSE A 77 8 HET MSE A 136 8 HET MSE B 1 8 HET MSE B 77 8 HET MSE B 136 8 HET MSE C 1 8 HET MSE C 77 8 HET MSE C 136 8 HET MSE D 1 8 HET MSE D 77 8 HET MSE D 136 8 HET CSF 1001 42 HET CSF 2001 42 HET CSF 3001 42 HET CSF 4001 42 HET MPD 401 8 HETNAM MSE SELENOMETHIONINE HETNAM CSF CYTIDINE-5'-MONOPHOSPHATE-3-FLUORO-N-ACETYL- HETNAM 2 CSF NEURAMINIC ACID HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL HETSYN CSF CMP-3FNEUAC FORMUL 1 MSE 12(C5 H11 N O2 SE) FORMUL 5 CSF 4(C20 H30 F N4 O16 P) FORMUL 6 MPD C6 H14 O2 FORMUL 7 HOH *330(H2 O) HELIX 1 1 GLY A 10 GLU A 15 5 6 HELIX 2 2 GLN A 32 GLU A 36 5 5 HELIX 3 3 ASN A 51 SER A 53 5 3 HELIX 4 4 LEU A 54 ASN A 68 1 15 HELIX 5 5 ASN A 88 THR A 94 1 7 HELIX 6 6 THR A 94 PHE A 99 1 6 HELIX 7 7 GLY A 105 LYS A 110 1 6 HELIX 8 8 LEU A 112 ASN A 127 1 16 HELIX 9 9 THR A 131 GLY A 144 1 14 HELIX 10 10 GLN A 168 ALA A 175 1 8 HELIX 11 11 PRO A 176 ASN A 180 5 5 HELIX 12 12 SER A 189 LYS A 205 1 17 HELIX 13 13 SER A 215 PHE A 220 5 6 HELIX 14 14 SER A 247 SER A 255 1 9 HELIX 15 15 LYS A 256 ILE A 258 5 3 HELIX 16 16 GLY B 10 ILE B 16 5 7 HELIX 17 17 ASP B 17 LEU B 21 5 5 HELIX 18 18 GLN B 32 GLU B 36 5 5 HELIX 19 19 ASN B 51 SER B 53 5 3 HELIX 20 20 LEU B 54 ASN B 68 1 15 HELIX 21 21 ASN B 88 PHE B 99 1 12 HELIX 22 22 GLY B 105 LYS B 110 1 6 HELIX 23 23 LEU B 112 ASN B 127 1 16 HELIX 24 24 THR B 131 LEU B 143 1 13 HELIX 25 25 GLN B 168 ALA B 175 1 8 HELIX 26 26 SER B 189 TYR B 204 1 16 HELIX 27 27 SER B 215 PHE B 220 5 6 HELIX 28 28 SER B 247 SER B 255 1 9 HELIX 29 29 LYS B 256 ILE B 258 5 3 HELIX 30 30 GLY C 10 ILE C 16 5 7 HELIX 31 31 ASP C 17 LEU C 21 5 5 HELIX 32 32 GLN C 32 GLU C 36 5 5 HELIX 33 33 ASN C 51 SER C 53 5 3 HELIX 34 34 LEU C 54 ASN C 68 1 15 HELIX 35 35 ASN C 88 PHE C 99 1 12 HELIX 36 36 GLY C 105 LYS C 110 1 6 HELIX 37 37 LEU C 112 ASN C 127 1 16 HELIX 38 38 THR C 131 LEU C 143 1 13 HELIX 39 39 GLN C 168 ALA C 175 1 8 HELIX 40 40 SER C 189 LYS C 205 1 17 HELIX 41 41 SER C 215 PHE C 220 5 6 HELIX 42 42 SER C 247 SER C 255 1 9 HELIX 43 43 GLY D 10 ILE D 16 5 7 HELIX 44 44 ASP D 17 LEU D 21 5 5 HELIX 45 45 GLN D 32 GLU D 36 5 5 HELIX 46 46 ASN D 51 SER D 53 5 3 HELIX 47 47 LEU D 54 ASN D 68 1 15 HELIX 48 48 ASN D 88 PHE D 99 1 12 HELIX 49 49 GLY D 105 LYS D 110 1 6 HELIX 50 50 LEU D 112 ASN D 127 1 16 HELIX 51 51 THR D 131 GLY D 144 1 14 HELIX 52 52 GLN D 168 ALA D 175 1 8 HELIX 53 53 SER D 189 LYS D 205 1 17 HELIX 54 54 SER D 215 PHE D 220 5 6 HELIX 55 55 SER D 247 SER D 255 1 9 HELIX 56 56 LYS D 256 ILE D 258 5 3 SHEET 1 A 7 HIS A 103 LEU A 104 0 SHEET 2 A 7 GLU A 72 CYS A 78 1 N ILE A 76 O HIS A 103 SHEET 3 A 7 LYS A 44 TYR A 50 1 N VAL A 48 O MSE A 77 SHEET 4 A 7 PHE A 25 CYS A 30 1 N VAL A 27 O LYS A 46 SHEET 5 A 7 LYS A 3 ALA A 7 1 N ILE A 5 O ASP A 26 SHEET 6 A 7 GLU A 147 SER A 151 1 O TYR A 149 N VAL A 4 SHEET 7 A 7 LYS A 207 CYS A 210 1 O TYR A 209 N LEU A 150 SHEET 1 B 2 LYS A 38 TYR A 39 0 SHEET 2 B 2 GLN A 234 GLU A 235 -1 O GLN A 234 N TYR A 39 SHEET 1 C 7 HIS B 103 LEU B 104 0 SHEET 2 C 7 GLU B 72 CYS B 78 1 N ILE B 76 O HIS B 103 SHEET 3 C 7 LYS B 44 TYR B 50 1 N VAL B 48 O MSE B 77 SHEET 4 C 7 PHE B 25 CYS B 30 1 N VAL B 27 O LYS B 46 SHEET 5 C 7 LYS B 3 ALA B 7 1 N ILE B 5 O ASP B 26 SHEET 6 C 7 GLU B 147 SER B 151 1 O TYR B 149 N VAL B 4 SHEET 7 C 7 LYS B 207 CYS B 210 1 O TYR B 209 N LEU B 150 SHEET 1 D 7 HIS C 103 LEU C 104 0 SHEET 2 D 7 GLU C 72 CYS C 78 1 N ILE C 76 O HIS C 103 SHEET 3 D 7 LYS C 44 TYR C 50 1 N VAL C 48 O MSE C 77 SHEET 4 D 7 PHE C 25 CYS C 30 1 N VAL C 27 O LYS C 46 SHEET 5 D 7 LYS C 3 ALA C 7 1 N ILE C 5 O ASP C 26 SHEET 6 D 7 GLU C 147 SER C 151 1 O TYR C 149 N ILE C 6 SHEET 7 D 7 LYS C 207 CYS C 210 1 O TYR C 209 N LEU C 150 SHEET 1 E 2 LYS C 38 TYR C 39 0 SHEET 2 E 2 GLN C 234 GLU C 235 -1 O GLN C 234 N TYR C 39 SHEET 1 F 7 HIS D 103 LEU D 104 0 SHEET 2 F 7 GLU D 72 CYS D 78 1 N ILE D 76 O HIS D 103 SHEET 3 F 7 LYS D 44 TYR D 50 1 N CYS D 45 O GLU D 72 SHEET 4 F 7 ASP D 26 CYS D 30 1 N VAL D 27 O LYS D 46 SHEET 5 F 7 LYS D 3 ALA D 7 1 N ILE D 5 O ASP D 26 SHEET 6 F 7 GLU D 147 SER D 151 1 O TYR D 149 N VAL D 4 SHEET 7 F 7 LYS D 207 CYS D 210 1 O TYR D 209 N LEU D 150 SHEET 1 G 2 LYS D 38 TYR D 39 0 SHEET 2 G 2 GLN D 234 GLU D 235 -1 O GLN D 234 N TYR D 39 CRYST1 83.660 66.031 99.172 90.00 94.42 90.00 P 1 21 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 0.011953 0.000000 0.000924 0.00000 SCALE2 0.000000 0.015144 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010114 0.00000