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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 08-DEC-04 1Y7I
TITLE STRUCTURAL AND BIOCHEMICAL STUDIES IDENTIFY TOBACCO SABP2
TITLE 2 AS A METHYLSALICYLATE ESTERASE AND FURTHER IMPLICATE IT IN
TITLE 3 PLANT INNATE IMMUNITY, NORTHEAST STRUCTURAL GENOMICS
TITLE 4 TARGET AR2241
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SALICYLIC ACID-BINDING PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SABP2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NICOTIANA TABACUM;
SOURCE 3 ORGANISM_COMMON: COMMON TOBACCO;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, NESG
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,Y.YANG,D.KUMAR,Y.CHEN,E.FRIDMAN,S.W.PARK,
AUTHOR 2 Y.CHIANG,T.B.ACTON,G.T.MONTELIONE,E.PICHERSKY,D.F.KLESSIG,
AUTHOR 3 L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 1 21-DEC-04 1Y7I 0
JRNL AUTH F.FOROUHAR,Y.YANG,D.KUMAR,Y.CHEN,E.FRIDMAN,
JRNL AUTH 2 S.W.PARK,Y.CHIANG,T.B.ACTON,G.T.MONTELIONE,
JRNL AUTH 3 E.PICHERSKY,D.F.KLESSIG,L.TONG
JRNL TITL STRUCTURAL AND BIOCHEMICAL STUDIES IDENTIFY
JRNL TITL 2 TOBACCO SABP2 AS A METHYLSALICYLATE ESTERASE AND
JRNL TITL 3 FURTHER IMPLICATE IT IN PLANT INNATE IMMUNITY,
JRNL TITL 4 NORTHEAST STRUCTURAL GENOMICS TARGET AR2241
JRNL REF TO BE PUBLISHED
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 353462.510
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 31540
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) : 0.197
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3152
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3842
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 458
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 : 4121
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 461
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.54000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : 3.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.90000
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
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) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.71
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 : 0.33
REMARK 3 BSOL : 45.82
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y7I COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-2004.
REMARK 100 THE RCSB ID CODE IS RCSB031213.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97904
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 34275
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.05700
REMARK 200 FOR THE DATA SET : 15.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
REMARK 200 R SYM FOR SHELL (I) : 0.26100
REMARK 200 FOR SHELL : 3.470
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COMO
REMARK 200 STARTING MODEL: PDB ENTRY 1Y7H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 10 MM SA, 0.2 M
REMARK 280 CALCIUM ACETATE, 10 MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 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 70.61050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.01200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.61050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.01200
REMARK 290 SMTRY3 4 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 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, 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 1
REMARK 465 LYS A 2
REMARK 465 LEU A 261
REMARK 465 GLU A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
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 VAL B 8 CA VAL B 8 CB 0.036
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 ASP A 38 N - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 PHE A 107 N - CA - C ANGL. DEV. =-12.6 DEGREES
REMARK 500 LEU A 160 N - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 CYS A 207 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 THR A 208 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 ILE A 213 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ASN A 224 N - CA - C ANGL. DEV. = 7.0 DEGREES
REMARK 500 ILE A 233 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 VAL B 8 N - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 THR B 35 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP B 38 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ILE B 76 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 PHE B 107 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 CYS B 207 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 THR B 208 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ILE B 213 N - CA - C ANGL. DEV. = -7.5 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 81 -111.83 41.65
REMARK 500 SER B 81 -112.60 44.18
REMARK 500 LEU B 132 -113.03 53.86
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XKL RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH SALICYLIC ACID AND
REMARK 900 ISOTHIOCYANATE
REMARK 900 RELATED ID: 1Y7H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES IDENTIFY TOBACCO
REMARK 900 SALICYLIC ACID BINDING PROTEIN 2 (SABP2) AS A
REMARK 900 METHYLSALICYLATE ESTERASE AND FURTHER IMPLICATE IT IN PLANT
REMARK 900 DEFENSE
REMARK 900 RELATED ID: AR2241 RELATED DB: TARGETDB
DBREF 1Y7I A 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7I B 1 260 GB 40549303 AAR87711 1 260
SEQADV 1Y7I MSE A 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7I MSE A 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7I LEU A 261 GB 40549303 HIS TAG
SEQADV 1Y7I GLU A 262 GB 40549303 HIS TAG
SEQADV 1Y7I HIS A 263 GB 40549303 HIS TAG
SEQADV 1Y7I HIS A 264 GB 40549303 HIS TAG
SEQADV 1Y7I HIS A 265 GB 40549303 HIS TAG
SEQADV 1Y7I HIS A 266 GB 40549303 HIS TAG
SEQADV 1Y7I HIS A 267 GB 40549303 HIS TAG
SEQADV 1Y7I HIS A 268 GB 40549303 HIS TAG
SEQADV 1Y7I MSE B 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7I MSE B 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7I LEU B 261 GB 40549303 HIS TAG
SEQADV 1Y7I GLU B 262 GB 40549303 HIS TAG
SEQADV 1Y7I HIS B 263 GB 40549303 HIS TAG
SEQADV 1Y7I HIS B 264 GB 40549303 HIS TAG
SEQADV 1Y7I HIS B 265 GB 40549303 HIS TAG
SEQADV 1Y7I HIS B 266 GB 40549303 HIS TAG
SEQADV 1Y7I HIS B 267 GB 40549303 HIS TAG
SEQADV 1Y7I HIS B 268 GB 40549303 HIS TAG
SEQRES 1 A 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 A 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 A 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 A 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 A 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 A 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 A 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 A 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 A 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 A 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 A 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 A 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 A 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 A 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 A 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 A 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 A 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 A 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 A 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 A 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 A 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 B 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 B 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 B 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 B 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 B 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 B 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 B 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 B 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 B 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 B 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 B 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 B 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 B 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 B 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 B 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 B 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 B 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 B 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 B 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 B 268 LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 1Y7I MSE A 63 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 66 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 85 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 91 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 108 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 149 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 183 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 239 MET SELENOMETHIONINE
MODRES 1Y7I MSE A 241 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 63 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 66 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 85 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 91 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 108 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 149 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 183 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 239 MET SELENOMETHIONINE
MODRES 1Y7I MSE B 241 MET SELENOMETHIONINE
HET MSE A 63 8
HET MSE A 66 8
HET MSE A 85 8
HET MSE A 91 8
HET MSE A 108 8
HET MSE A 149 8
HET MSE A 183 8
HET MSE A 239 8
HET MSE A 241 8
HET MSE B 63 8
HET MSE B 66 8
HET MSE B 85 8
HET MSE B 91 8
HET MSE B 108 8
HET MSE B 149 8
HET MSE B 183 8
HET MSE B 239 8
HET MSE B 241 8
HET SAL 501 10
HET SAL 502 10
HET SAL 503 10
HETNAM MSE SELENOMETHIONINE
HETNAM SAL 2-HYDROXYBENZOIC ACID
HETSYN SAL SALICYLIC ACID
FORMUL 1 MSE 18(C5 H11 N1 O2 SE1)
FORMUL 3 SAL 3(C7 H6 O3)
FORMUL 6 HOH *461(H2 O1)
HELIX 1 1 GLY A 16 TYR A 21 5 6
HELIX 2 2 LYS A 22 ALA A 30 1 9
HELIX 3 3 LYS A 48 LEU A 52 5 5
HELIX 4 4 THR A 54 LEU A 69 1 16
HELIX 5 5 LEU A 82 TYR A 94 1 13
HELIX 6 6 SER A 116 THR A 126 1 11
HELIX 7 7 PRO A 127 LEU A 132 5 6
HELIX 8 8 GLY A 152 LEU A 160 1 9
HELIX 9 9 SER A 165 VAL A 176 1 12
HELIX 10 10 PHE A 182 SER A 187 1 6
HELIX 11 11 ARG A 196 VAL A 200 5 5
HELIX 12 12 PRO A 214 GLY A 226 1 13
HELIX 13 13 MSE A 239 GLU A 244 1 6
HELIX 14 14 GLU A 244 TYR A 259 1 16
HELIX 15 15 GLY B 16 TYR B 21 5 6
HELIX 16 16 LYS B 22 ALA B 30 1 9
HELIX 17 17 LYS B 48 LEU B 52 5 5
HELIX 18 18 THR B 54 LEU B 69 1 16
HELIX 19 19 LEU B 82 TYR B 94 1 13
HELIX 20 20 SER B 116 ARG B 125 1 10
HELIX 21 21 PRO B 127 LEU B 132 5 6
HELIX 22 22 GLY B 152 LEU B 160 1 9
HELIX 23 23 SER B 165 VAL B 176 1 12
HELIX 24 24 PHE B 182 LYS B 188 1 7
HELIX 25 25 ARG B 196 VAL B 200 5 5
HELIX 26 26 PRO B 214 ILE B 225 1 12
HELIX 27 27 MSE B 239 GLU B 244 1 6
HELIX 28 28 GLU B 244 HIS B 263 1 20
SHEET 1 A 6 LYS A 33 LEU A 37 0
SHEET 2 A 6 HIS A 6 VAL A 10 1 N PHE A 7 O LYS A 33
SHEET 3 A 6 VAL A 75 HIS A 80 1 O VAL A 78 N VAL A 10
SHEET 4 A 6 ILE A 98 LEU A 104 1 O VAL A 102 N LEU A 77
SHEET 5 A 6 ARG A 202 CYS A 207 1 O VAL A 203 N PHE A 103
SHEET 6 A 6 GLU A 229 ILE A 233 1 O ILE A 231 N VAL A 206
SHEET 1 B 2 GLN A 135 PRO A 138 0
SHEET 2 B 2 THR A 147 PHE A 150 -1 O SER A 148 N LEU A 137
SHEET 1 C 6 LYS B 33 ALA B 36 0
SHEET 2 C 6 HIS B 6 VAL B 10 1 N PHE B 7 O LYS B 33
SHEET 3 C 6 VAL B 75 HIS B 80 1 O VAL B 78 N VAL B 10
SHEET 4 C 6 ILE B 98 LEU B 104 1 O VAL B 102 N LEU B 77
SHEET 5 C 6 ARG B 202 CYS B 207 1 O VAL B 203 N PHE B 103
SHEET 6 C 6 GLU B 229 ILE B 233 1 O ILE B 231 N TYR B 204
SHEET 1 D 2 GLN B 135 PRO B 138 0
SHEET 2 D 2 THR B 147 PHE B 150 -1 O SER B 148 N LEU B 137
CRYST1 141.221 48.024 92.590 90.00 110.63 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 0.007081 0.000000 0.002666 0.00000
SCALE2 0.000000 0.020823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011540 0.00000
TER 2043 ASN A 260
TER 4123 HIS B 264
MASTER 304 0 21 28 16 0 0 6 4612 2 174 42
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