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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 08-DEC-04 1Y7H
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, C, D, E, F, G, H;
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, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 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 28-DEC-04 1Y7H 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. 2.52 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) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 277179.930
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 130389
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) : 0.227
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 12883
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 14373
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1624
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.75000
REMARK 3 B22 (A**2) : -0.30000
REMARK 3 B33 (A**2) : 1.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.28000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
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 : 0.31
REMARK 3 BSOL : 15.03
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 1Y7H COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-2004.
REMARK 100 THE RCSB ID CODE IS RCSB031212.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-2003
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) : 0.9791
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 : 138444
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 28.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.440
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : 0.12500
REMARK 200 FOR THE DATA SET : 12.1800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.27600
REMARK 200 R SYM FOR SHELL (I) : 0.30900
REMARK 200 FOR SHELL : 4.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB THEN SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M SODIUM
REMARK 280 THIOCYANATE, 5 MM SPERMINE, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
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 68.86800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 8 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: E, F
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 350 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 TYR A 259
REMARK 465 ASN A 260
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 LEU B 261
REMARK 465 GLU B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 MET C 1
REMARK 465 TYR C 259
REMARK 465 ASN C 260
REMARK 465 LEU C 261
REMARK 465 GLU C 262
REMARK 465 HIS C 263
REMARK 465 HIS C 264
REMARK 465 HIS C 265
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 MET D 1
REMARK 465 LEU D 261
REMARK 465 GLU D 262
REMARK 465 HIS D 263
REMARK 465 HIS D 264
REMARK 465 HIS D 265
REMARK 465 HIS D 266
REMARK 465 HIS D 267
REMARK 465 HIS D 268
REMARK 465 MET E 1
REMARK 465 ASN E 260
REMARK 465 LEU E 261
REMARK 465 GLU E 262
REMARK 465 HIS E 263
REMARK 465 HIS E 264
REMARK 465 HIS E 265
REMARK 465 HIS E 266
REMARK 465 HIS E 267
REMARK 465 HIS E 268
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 LEU F 261
REMARK 465 GLU F 262
REMARK 465 HIS F 263
REMARK 465 HIS F 264
REMARK 465 HIS F 265
REMARK 465 HIS F 266
REMARK 465 HIS F 267
REMARK 465 HIS F 268
REMARK 465 MET G 1
REMARK 465 TYR G 259
REMARK 465 ASN G 260
REMARK 465 LEU G 261
REMARK 465 GLU G 262
REMARK 465 HIS G 263
REMARK 465 HIS G 264
REMARK 465 HIS G 265
REMARK 465 HIS G 266
REMARK 465 HIS G 267
REMARK 465 HIS G 268
REMARK 465 MET H 1
REMARK 465 LEU H 261
REMARK 465 GLU H 262
REMARK 465 HIS H 263
REMARK 465 HIS H 264
REMARK 465 HIS H 265
REMARK 465 HIS H 266
REMARK 465 HIS H 267
REMARK 465 HIS H 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 CYS A 207 CB CYS A 207 SG 0.049
REMARK 500 PRO B 25 CB PRO B 25 CG 0.051
REMARK 500 GLU B 167 CB GLU B 167 CG 0.047
REMARK 500 GLN D 96 CB GLN D 96 CG 0.048
REMARK 500 CYS F 164 CB CYS F 164 SG 0.061
REMARK 500 LEU G 9 CG LEU G 9 CD2 0.047
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 VAL A 8 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 PHE A 107 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 THR A 208 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 TYR B 21 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 PHE B 136 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 ILE B 213 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 ILE C 213 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 PRO D 61 C - N - CA ANGL. DEV. = -7.5 DEGREES
REMARK 500 PHE D 107 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 LEU D 175 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 ILE D 213 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 PHE E 107 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 CYS E 207 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 ILE E 213 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASP F 38 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 PRO F 178 C - N - CA ANGL. DEV. = -8.0 DEGREES
REMARK 500 ILE G 213 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 VAL H 8 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 PHE H 107 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ILE H 213 N - CA - C ANGL. DEV. = -9.3 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 LEU A 132 -118.65 57.10
REMARK 500 SER B 81 -105.83 67.67
REMARK 500 LEU B 132 -111.66 41.01
REMARK 500 SER C 81 -118.40 48.90
REMARK 500 LEU C 132 -110.40 49.93
REMARK 500 SER D 81 -111.78 40.51
REMARK 500 LEU D 132 -111.46 33.60
REMARK 500 SER F 81 -106.15 47.42
REMARK 500 LEU G 132 -109.94 58.67
REMARK 500 SER H 81 -110.67 53.37
REMARK 500 LEU H 132 -115.99 38.30
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: 1Y7I 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
REMARK 900 RELATED ID: AR2241 RELATED DB: TARGETDB
DBREF 1Y7H A 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H B 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H C 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H D 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H E 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H F 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H G 1 260 GB 40549303 AAR87711 1 260
DBREF 1Y7H H 1 260 GB 40549303 AAR87711 1 260
SEQADV 1Y7H MSE A 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE A 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU A 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU A 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS A 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS A 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS A 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS A 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS A 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS A 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE B 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE B 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU B 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU B 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS B 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS B 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS B 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS B 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS B 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS B 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE C 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE C 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU C 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU C 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS C 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS C 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS C 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS C 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS C 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS C 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE D 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE D 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU D 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU D 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS D 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS D 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS D 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS D 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS D 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS D 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE E 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE E 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU E 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU E 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS E 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS E 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS E 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS E 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS E 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS E 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE F 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE F 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU F 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU F 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS F 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS F 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS F 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS F 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS F 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS F 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE G 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE G 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU G 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU G 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS G 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS G 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS G 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS G 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS G 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS G 268 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H MSE H 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1Y7H MSE H 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1Y7H LEU H 261 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H GLU H 262 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS H 263 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS H 264 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS H 265 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS H 266 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS H 267 GB 40549303 CLONING ARTIFACT
SEQADV 1Y7H HIS H 268 GB 40549303 CLONING ARTIFACT
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
SEQRES 1 C 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 C 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 C 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 C 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 C 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 C 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 C 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 C 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 C 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 C 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 C 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 C 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 C 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 C 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 C 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 C 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 C 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 C 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 C 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 C 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 C 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 D 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 D 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 D 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 D 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 D 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 D 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 D 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 D 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 D 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 D 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 D 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 D 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 D 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 D 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 D 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 D 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 D 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 D 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 D 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 D 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 E 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 E 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 E 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 E 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 E 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 E 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 E 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 E 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 E 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 E 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 E 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 E 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 E 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 E 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 E 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 E 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 E 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 E 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 E 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 E 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 F 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 F 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 F 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 F 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 F 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 F 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 F 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 F 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 F 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 F 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 F 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 F 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 F 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 F 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 F 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 F 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 F 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 F 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 F 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 F 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 G 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 G 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 G 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 G 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 G 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 G 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 G 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 G 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 G 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 G 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 G 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 G 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 G 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 G 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 G 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 G 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 G 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 G 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 G 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 G 268 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 H 268 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 H 268 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 H 268 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 H 268 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 H 268 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 H 268 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 H 268 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 H 268 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 H 268 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 H 268 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 H 268 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 H 268 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 H 268 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 H 268 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 H 268 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 H 268 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 H 268 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 H 268 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 H 268 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 H 268 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 H 268 LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 1Y7H MSE A 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE A 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE B 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE C 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE D 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE E 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE F 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE G 241 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 63 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 66 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 85 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 91 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 108 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 149 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 183 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 239 MET SELENOMETHIONINE
MODRES 1Y7H MSE H 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 MSE C 63 8
HET MSE C 66 8
HET MSE C 85 8
HET MSE C 91 8
HET MSE C 108 8
HET MSE C 149 8
HET MSE C 183 8
HET MSE C 239 8
HET MSE C 241 8
HET MSE D 63 8
HET MSE D 66 8
HET MSE D 85 8
HET MSE D 91 8
HET MSE D 108 8
HET MSE D 149 8
HET MSE D 183 8
HET MSE D 239 8
HET MSE D 241 8
HET MSE E 63 8
HET MSE E 66 8
HET MSE E 85 8
HET MSE E 91 8
HET MSE E 108 8
HET MSE E 149 8
HET MSE E 183 8
HET MSE E 239 8
HET MSE E 241 8
HET MSE F 63 8
HET MSE F 66 8
HET MSE F 85 8
HET MSE F 91 8
HET MSE F 108 8
HET MSE F 149 8
HET MSE F 183 8
HET MSE F 239 8
HET MSE F 241 8
HET MSE G 63 8
HET MSE G 66 8
HET MSE G 85 8
HET MSE G 91 8
HET MSE G 108 8
HET MSE G 149 8
HET MSE G 183 8
HET MSE G 239 8
HET MSE G 241 8
HET MSE H 63 8
HET MSE H 66 8
HET MSE H 85 8
HET MSE H 91 8
HET MSE H 108 8
HET MSE H 149 8
HET MSE H 183 8
HET MSE H 239 8
HET MSE H 241 8
HET SCN 291 3
HET SCN 292 3
HET SCN 293 3
HET SCN 294 3
HET SCN 295 3
HET SCN 296 3
HET SCN 297 3
HET SCN 298 3
HETNAM MSE SELENOMETHIONINE
HETNAM SCN THIOCYANATE ION
FORMUL 1 MSE 72(C5 H11 N1 O2 SE1)
FORMUL 9 SCN 8(C1 N1 S1 1-)
FORMUL 17 HOH *224(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 GLU A 67 1 14
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 ALA A 128 LEU A 132 5 5
HELIX 8 8 GLY A 152 LEU A 160 1 9
HELIX 9 9 SER A 165 SER A 174 1 10
HELIX 10 10 PHE A 182 LYS A 188 1 7
HELIX 11 11 ARG A 196 VAL A 200 5 5
HELIX 12 12 PRO A 214 ILE A 225 1 12
HELIX 13 13 MSE A 239 GLU A 244 1 6
HELIX 14 14 GLU A 244 HIS A 257 1 14
HELIX 15 15 GLY B 16 TYR B 21 5 6
HELIX 16 16 LEU B 23 ALA B 30 1 8
HELIX 17 17 LYS B 48 LEU B 52 5 5
HELIX 18 18 THR B 54 THR B 59 1 6
HELIX 19 19 THR B 59 SER B 68 1 10
HELIX 20 20 LEU B 82 TYR B 94 1 13
HELIX 21 21 PRO B 95 ILE B 98 5 4
HELIX 22 22 SER B 116 THR B 126 1 11
HELIX 23 23 GLY B 152 LYS B 159 1 8
HELIX 24 24 SER B 165 VAL B 176 1 12
HELIX 25 25 PHE B 182 SER B 187 1 6
HELIX 26 26 ARG B 196 VAL B 200 5 5
HELIX 27 27 PRO B 214 ILE B 225 1 12
HELIX 28 28 MSE B 239 GLU B 244 1 6
HELIX 29 29 GLU B 244 TYR B 259 1 16
HELIX 30 30 GLY C 16 TYR C 21 5 6
HELIX 31 31 LYS C 22 ALA C 30 1 9
HELIX 32 32 LYS C 48 LEU C 52 5 5
HELIX 33 33 THR C 54 LEU C 69 1 16
HELIX 34 34 LEU C 82 TYR C 94 1 13
HELIX 35 35 SER C 116 THR C 126 1 11
HELIX 36 36 ALA C 128 LEU C 132 5 5
HELIX 37 37 GLY C 152 LEU C 160 1 9
HELIX 38 38 SER C 165 SER C 174 1 10
HELIX 39 39 PHE C 182 LYS C 188 1 7
HELIX 40 40 ARG C 196 VAL C 200 5 5
HELIX 41 41 PRO C 214 ILE C 225 1 12
HELIX 42 42 MSE C 239 GLU C 244 1 6
HELIX 43 43 GLU C 244 ALA C 256 1 13
HELIX 44 44 GLY D 16 TYR D 21 5 6
HELIX 45 45 LYS D 22 ALA D 30 1 9
HELIX 46 46 LYS D 48 LEU D 52 5 5
HELIX 47 47 THR D 54 LEU D 69 1 16
HELIX 48 48 LEU D 82 TYR D 94 1 13
HELIX 49 49 SER D 116 ARG D 125 1 10
HELIX 50 50 GLY D 152 LEU D 160 1 9
HELIX 51 51 SER D 165 SER D 174 1 10
HELIX 52 52 PHE D 182 SER D 187 1 6
HELIX 53 53 ARG D 196 VAL D 200 5 5
HELIX 54 54 PRO D 214 GLY D 226 1 13
HELIX 55 55 MSE D 239 GLU D 244 1 6
HELIX 56 56 GLU D 244 TYR D 259 1 16
HELIX 57 57 GLY E 16 TYR E 21 5 6
HELIX 58 58 LYS E 22 ALA E 29 1 8
HELIX 59 59 LYS E 48 LEU E 52 5 5
HELIX 60 60 THR E 54 LEU E 69 1 16
HELIX 61 61 LEU E 82 TYR E 94 1 13
HELIX 62 62 SER E 116 THR E 126 1 11
HELIX 63 63 PRO E 127 LEU E 132 5 6
HELIX 64 64 GLY E 152 LEU E 160 1 9
HELIX 65 65 SER E 165 SER E 174 1 10
HELIX 66 66 PHE E 182 LYS E 188 1 7
HELIX 67 67 ARG E 196 VAL E 200 5 5
HELIX 68 68 PRO E 214 GLY E 226 1 13
HELIX 69 69 MSE E 239 GLU E 244 1 6
HELIX 70 70 GLU E 244 TYR E 259 1 16
HELIX 71 71 GLY F 16 TYR F 21 5 6
HELIX 72 72 LEU F 23 ALA F 30 1 8
HELIX 73 73 LYS F 48 LEU F 52 5 5
HELIX 74 74 THR F 54 LEU F 69 1 16
HELIX 75 75 LEU F 82 TYR F 94 1 13
HELIX 76 76 SER F 116 ARG F 125 1 10
HELIX 77 77 THR F 126 TRP F 131 5 6
HELIX 78 78 GLY F 152 LEU F 160 1 9
HELIX 79 79 SER F 165 SER F 174 1 10
HELIX 80 80 PHE F 182 SER F 187 1 6
HELIX 81 81 PRO F 214 GLY F 226 1 13
HELIX 82 82 MSE F 239 GLU F 244 1 6
HELIX 83 83 GLU F 244 TYR F 259 1 16
HELIX 84 84 GLY G 16 TYR G 21 5 6
HELIX 85 85 LYS G 22 ALA G 30 1 9
HELIX 86 86 LYS G 48 LEU G 52 5 5
HELIX 87 87 THR G 54 LEU G 69 1 16
HELIX 88 88 LEU G 82 TYR G 94 1 13
HELIX 89 89 SER G 116 ARG G 125 1 10
HELIX 90 90 PRO G 127 LEU G 132 5 6
HELIX 91 91 GLY G 152 LEU G 160 1 9
HELIX 92 92 SER G 165 VAL G 176 1 12
HELIX 93 93 PHE G 182 LYS G 188 1 7
HELIX 94 94 PRO G 214 ILE G 225 1 12
HELIX 95 95 MSE G 239 GLU G 244 1 6
HELIX 96 96 GLU G 244 LYS G 258 1 15
HELIX 97 97 GLY H 16 TYR H 21 5 6
HELIX 98 98 LYS H 22 ALA H 29 1 8
HELIX 99 99 LYS H 48 LEU H 52 5 5
HELIX 100 100 THR H 54 LEU H 69 1 16
HELIX 101 101 LEU H 82 TYR H 94 1 13
HELIX 102 102 SER H 116 ARG H 125 1 10
HELIX 103 103 THR H 126 LEU H 132 5 7
HELIX 104 104 GLY H 152 HIS H 158 1 7
HELIX 105 105 SER H 165 VAL H 176 1 12
HELIX 106 106 PHE H 182 SER H 187 1 6
HELIX 107 107 ARG H 196 VAL H 200 5 5
HELIX 108 108 PRO H 214 ILE H 225 1 12
HELIX 109 109 MSE H 239 GLU H 244 1 6
HELIX 110 110 GLU H 244 TYR H 259 1 16
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 SER A 81 1 O VAL A 78 N VAL A 10
SHEET 4 A 6 ILE A 98 ALA A 106 1 O VAL A 102 N LEU A 77
SHEET 5 A 6 ARG A 202 VAL A 206 1 O VAL A 203 N PHE A 103
SHEET 6 A 6 GLU A 229 GLU A 232 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 ILE B 76 HIS B 80 1 O ILE B 76 N VAL B 8
SHEET 4 C 6 ALA B 100 LEU B 104 1 O VAL B 102 N GLY B 79
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 233 N VAL B 206
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
SHEET 1 E 6 LYS C 33 THR C 35 0
SHEET 2 E 6 HIS C 6 VAL C 10 1 N PHE C 7 O THR C 35
SHEET 3 E 6 VAL C 75 HIS C 80 1 O VAL C 78 N VAL C 10
SHEET 4 E 6 ILE C 98 LEU C 104 1 O TYR C 99 N VAL C 75
SHEET 5 E 6 ARG C 202 CYS C 207 1 O VAL C 203 N PHE C 103
SHEET 6 E 6 GLU C 229 ILE C 233 1 O ILE C 231 N VAL C 206
SHEET 1 F 2 GLN C 135 PRO C 138 0
SHEET 2 F 2 THR C 147 PHE C 150 -1 O SER C 148 N LEU C 137
SHEET 1 G 6 LYS D 33 ALA D 36 0
SHEET 2 G 6 HIS D 6 VAL D 10 1 N PHE D 7 O LYS D 33
SHEET 3 G 6 VAL D 75 SER D 81 1 O HIS D 80 N VAL D 10
SHEET 4 G 6 ILE D 98 ALA D 106 1 O VAL D 102 N LEU D 77
SHEET 5 G 6 ARG D 202 CYS D 207 1 O VAL D 203 N ALA D 101
SHEET 6 G 6 GLU D 229 ILE D 233 1 O ILE D 231 N VAL D 206
SHEET 1 H 2 GLN D 135 PRO D 138 0
SHEET 2 H 2 THR D 147 PHE D 150 -1 O SER D 148 N LEU D 137
SHEET 1 I 6 LYS E 33 LEU E 37 0
SHEET 2 I 6 HIS E 6 VAL E 10 1 N PHE E 7 O LYS E 33
SHEET 3 I 6 VAL E 75 HIS E 80 1 O VAL E 78 N VAL E 10
SHEET 4 I 6 ILE E 98 LEU E 104 1 O VAL E 102 N LEU E 77
SHEET 5 I 6 ARG E 202 CYS E 207 1 O VAL E 203 N PHE E 103
SHEET 6 I 6 GLU E 229 ILE E 233 1 O ILE E 233 N VAL E 206
SHEET 1 J 2 GLN E 135 PRO E 138 0
SHEET 2 J 2 THR E 147 PHE E 150 -1 O SER E 148 N LEU E 137
SHEET 1 K 6 LYS F 33 THR F 35 0
SHEET 2 K 6 HIS F 6 VAL F 10 1 N PHE F 7 O LYS F 33
SHEET 3 K 6 VAL F 75 HIS F 80 1 O VAL F 78 N VAL F 10
SHEET 4 K 6 ILE F 98 LEU F 104 1 O VAL F 102 N LEU F 77
SHEET 5 K 6 ARG F 202 CYS F 207 1 O VAL F 203 N ALA F 101
SHEET 6 K 6 GLU F 229 ILE F 233 1 O ILE F 231 N VAL F 206
SHEET 1 L 2 GLN F 135 PRO F 138 0
SHEET 2 L 2 THR F 147 PHE F 150 -1 O SER F 148 N LEU F 137
SHEET 1 M 6 LYS G 33 ALA G 36 0
SHEET 2 M 6 HIS G 6 VAL G 10 1 N PHE G 7 O LYS G 33
SHEET 3 M 6 VAL G 75 HIS G 80 1 O VAL G 78 N VAL G 10
SHEET 4 M 6 ILE G 98 LEU G 104 1 O VAL G 102 N LEU G 77
SHEET 5 M 6 ARG G 202 CYS G 207 1 O VAL G 203 N PHE G 103
SHEET 6 M 6 GLU G 229 ILE G 233 1 O ILE G 233 N VAL G 206
SHEET 1 N 2 GLN G 135 PRO G 138 0
SHEET 2 N 2 THR G 147 PHE G 150 -1 O SER G 148 N LEU G 137
SHEET 1 O 6 LYS H 33 THR H 35 0
SHEET 2 O 6 HIS H 6 VAL H 10 1 N PHE H 7 O LYS H 33
SHEET 3 O 6 VAL H 75 HIS H 80 1 O VAL H 78 N VAL H 10
SHEET 4 O 6 ILE H 98 LEU H 104 1 O VAL H 102 N GLY H 79
SHEET 5 O 6 ARG H 202 CYS H 207 1 O VAL H 203 N ALA H 101
SHEET 6 O 6 GLU H 229 ILE H 233 1 O ILE H 233 N VAL H 206
SHEET 1 P 2 GLN H 135 PRO H 138 0
SHEET 2 P 2 THR H 147 PHE H 150 -1 O SER H 148 N LEU H 137
CRYST1 45.630 137.736 171.208 90.00 90.10 90.00 P 1 21 1 16
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 0.021915 0.000000 0.000040 0.00000
SCALE2 0.000000 0.007260 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005841 0.00000
TER 2032 LYS A 258
TER 4084 ASN B 260
TER 6116 LYS C 258
TER 8168 ASN D 260
TER 10212 TYR E 259
TER 12255 ASN F 260
TER 14287 LYS G 258
TER 16339 ASN H 260
MASTER 393 0 80 110 64 0 0 616579 8 600 168
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