| content |
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-SEP-04 1XKL
TITLE CRYSTAL STRUCTURE OF SALICYLIC ACID-BINDING PROTEIN 2
TITLE 2 (SABP2) FROM NICOTIANA TABACUM, NESG TARGET AR2241
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SALICYLIC ACID-BINDING PROTEIN 2;
COMPND 3 CHAIN: A, B, C, D;
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 GENE: AAR87711;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET21;
SOURCE 10 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.CHEN,Y.CHIANG,T.B.ACTON,G.T.MONTELIONE,
AUTHOR 2 J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 1 30-NOV-04 1XKL 0
JRNL AUTH F.FOROUHAR,Y.CHEN,Y.CHIANG,T.B.ACTON,
JRNL AUTH 2 G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF SALICYLIC ACID-BINDING
JRNL TITL 2 PROTEIN 2 (SABP2) FROM NICOTIANA TABACUM, NESG
JRNL TITL 3 TARGET AR2241
JRNL REF TO BE PUBLISHED
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 347566.890
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.2
REMARK 3 NUMBER OF REFLECTIONS : 113140
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 11074
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12533
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1295
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8131
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 926
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.02000
REMARK 3 B22 (A**2) : -1.09000
REMARK 3 B33 (A**2) : 4.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
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) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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 : 41.46
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 1XKL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-2004.
REMARK 100 THE RCSB ID CODE IS RCSB030460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-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) : 0.97935
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 : 131338
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.06800
REMARK 200 FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : 0.27800
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB THEN SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES-NAOH, 20% PEG3350, 5
REMARK 280 MM SA, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 68.22850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.88650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.22850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.88650
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 878 LIES ON A SPECIAL POSITION.
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 MET A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 ASP A 264
REMARK 465 PRO A 265
REMARK 465 LEU A 266
REMARK 465 GLU A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 TYR B 259
REMARK 465 ASN B 260
REMARK 465 MET B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 ASP B 264
REMARK 465 PRO B 265
REMARK 465 LEU B 266
REMARK 465 GLU B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 HIS B 273
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 ASN C 260
REMARK 465 MET C 261
REMARK 465 ALA C 262
REMARK 465 GLY C 263
REMARK 465 ASP C 264
REMARK 465 PRO C 265
REMARK 465 LEU C 266
REMARK 465 GLU C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 HIS C 273
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 LYS D 190
REMARK 465 MET D 261
REMARK 465 ALA D 262
REMARK 465 GLY D 263
REMARK 465 ASP D 264
REMARK 465 PRO D 265
REMARK 465 LEU D 266
REMARK 465 GLU D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 HIS D 272
REMARK 465 HIS D 273
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 917 O HOH 917 2665 1.30
REMARK 500 O HOH 918 O HOH 918 2665 1.51
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 SER A 81 N SER A 81 CA -0.106
REMARK 500 SER B 81 N SER B 81 CA -0.111
REMARK 500 SER C 81 N SER C 81 CA -0.116
REMARK 500 SER D 81 N SER D 81 CA -0.113
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 72 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 SER A 81 CA - CB - OG ANGL. DEV. = 17.2 DEGREES
REMARK 500 PHE A 107 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 TYR A 191 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ILE A 213 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 SER B 81 CA - CB - OG ANGL. DEV. = 17.0 DEGREES
REMARK 500 PHE B 107 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 LYS B 159 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 LEU B 175 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 THR B 208 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ILE B 213 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 ASP C 38 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 LEU C 39 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 ILE C 76 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 SER C 81 CA - CB - OG ANGL. DEV. = 17.0 DEGREES
REMARK 500 PHE C 107 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 CYS C 207 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 THR C 208 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 ILE C 213 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 SER D 81 CA - CB - OG ANGL. DEV. = 16.8 DEGREES
REMARK 500 PHE D 107 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ILE D 213 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 71 -30.93 76.68
REMARK 500 LEU B 132 -116.11 54.58
REMARK 500 LEU C 132 -119.87 51.71
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 583 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH 621 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH 705 DISTANCE = 6.15 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: AR2241 RELATED DB: TARGETDB
DBREF 1XKL A 1 260 GB 40549303 AAR87711 1 260
DBREF 1XKL B 1 260 GB 40549303 AAR87711 1 260
DBREF 1XKL C 1 260 GB 40549303 AAR87711 1 260
DBREF 1XKL D 1 260 GB 40549303 AAR87711 1 260
SEQADV 1XKL MSE A 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1XKL MSE A 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1XKL MSE A 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1XKL MSE A 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1XKL MSE A 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1XKL MSE A 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1XKL MSE A 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1XKL MSE A 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1XKL MSE A 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1XKL MET A 261 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ALA A 262 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLY A 263 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ASP A 264 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL PRO A 265 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL LEU A 266 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLU A 267 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL HIS A 268 GB 40549303 HIS TAG
SEQADV 1XKL HIS A 269 GB 40549303 HIS TAG
SEQADV 1XKL HIS A 270 GB 40549303 HIS TAG
SEQADV 1XKL HIS A 271 GB 40549303 HIS TAG
SEQADV 1XKL HIS A 272 GB 40549303 HIS TAG
SEQADV 1XKL HIS A 273 GB 40549303 HIS TAG
SEQADV 1XKL MSE B 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1XKL MSE B 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1XKL MSE B 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1XKL MSE B 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1XKL MSE B 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1XKL MSE B 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1XKL MSE B 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1XKL MSE B 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1XKL MSE B 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1XKL MET B 261 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ALA B 262 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLY B 263 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ASP B 264 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL PRO B 265 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL LEU B 266 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLU B 267 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL HIS B 268 GB 40549303 HIS TAG
SEQADV 1XKL HIS B 269 GB 40549303 HIS TAG
SEQADV 1XKL HIS B 270 GB 40549303 HIS TAG
SEQADV 1XKL HIS B 271 GB 40549303 HIS TAG
SEQADV 1XKL HIS B 272 GB 40549303 HIS TAG
SEQADV 1XKL HIS B 273 GB 40549303 HIS TAG
SEQADV 1XKL MSE C 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1XKL MSE C 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1XKL MSE C 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1XKL MSE C 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1XKL MSE C 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1XKL MSE C 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1XKL MSE C 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1XKL MSE C 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1XKL MSE C 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1XKL MET C 261 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ALA C 262 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLY C 263 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ASP C 264 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL PRO C 265 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL LEU C 266 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLU C 267 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL HIS C 268 GB 40549303 HIS TAG
SEQADV 1XKL HIS C 269 GB 40549303 HIS TAG
SEQADV 1XKL HIS C 270 GB 40549303 HIS TAG
SEQADV 1XKL HIS C 271 GB 40549303 HIS TAG
SEQADV 1XKL HIS C 272 GB 40549303 HIS TAG
SEQADV 1XKL HIS C 273 GB 40549303 HIS TAG
SEQADV 1XKL MSE D 63 GB 40549303 MET 63 MODIFIED RESIDUE
SEQADV 1XKL MSE D 66 GB 40549303 MET 66 MODIFIED RESIDUE
SEQADV 1XKL MSE D 85 GB 40549303 MET 85 MODIFIED RESIDUE
SEQADV 1XKL MSE D 91 GB 40549303 MET 91 MODIFIED RESIDUE
SEQADV 1XKL MSE D 108 GB 40549303 MET 108 MODIFIED RESIDUE
SEQADV 1XKL MSE D 149 GB 40549303 MET 149 MODIFIED RESIDUE
SEQADV 1XKL MSE D 183 GB 40549303 MET 183 MODIFIED RESIDUE
SEQADV 1XKL MSE D 239 GB 40549303 MET 239 MODIFIED RESIDUE
SEQADV 1XKL MSE D 241 GB 40549303 MET 241 MODIFIED RESIDUE
SEQADV 1XKL MET D 261 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ALA D 262 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLY D 263 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL ASP D 264 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL PRO D 265 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL LEU D 266 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL GLU D 267 GB 40549303 CLONING ARTIFACT
SEQADV 1XKL HIS D 268 GB 40549303 HIS TAG
SEQADV 1XKL HIS D 269 GB 40549303 HIS TAG
SEQADV 1XKL HIS D 270 GB 40549303 HIS TAG
SEQADV 1XKL HIS D 271 GB 40549303 HIS TAG
SEQADV 1XKL HIS D 272 GB 40549303 HIS TAG
SEQADV 1XKL HIS D 273 GB 40549303 HIS TAG
SEQRES 1 A 273 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 A 273 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 A 273 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 A 273 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 A 273 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 A 273 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 A 273 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 A 273 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 A 273 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 A 273 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 A 273 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 A 273 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 A 273 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 A 273 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 A 273 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 A 273 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 A 273 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 A 273 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 A 273 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 A 273 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 A 273 MET ALA GLY ASP PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 273 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 B 273 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 B 273 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 B 273 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 B 273 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 B 273 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 B 273 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 B 273 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 B 273 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 B 273 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 B 273 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 B 273 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 B 273 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 B 273 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 B 273 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 B 273 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 B 273 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 B 273 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 B 273 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 B 273 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 B 273 MET ALA GLY ASP PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 273 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 C 273 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 C 273 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 C 273 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 C 273 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 C 273 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 C 273 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 C 273 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 C 273 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 C 273 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 C 273 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 C 273 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 C 273 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 C 273 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 C 273 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 C 273 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 C 273 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 C 273 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 C 273 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 C 273 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 C 273 MET ALA GLY ASP PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 273 MET LYS GLU GLY LYS HIS PHE VAL LEU VAL HIS GLY ALA
SEQRES 2 D 273 CYS HIS GLY GLY TRP SER TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 D 273 LEU GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU
SEQRES 4 D 273 ALA ALA SER GLY THR ASP LEU ARG LYS ILE GLU GLU LEU
SEQRES 5 D 273 ARG THR LEU TYR ASP TYR THR LEU PRO LEU MSE GLU LEU
SEQRES 6 D 273 MSE GLU SER LEU SER ALA ASP GLU LYS VAL ILE LEU VAL
SEQRES 7 D 273 GLY HIS SER LEU GLY GLY MSE ASN LEU GLY LEU ALA MSE
SEQRES 8 D 273 GLU LYS TYR PRO GLN LYS ILE TYR ALA ALA VAL PHE LEU
SEQRES 9 D 273 ALA ALA PHE MSE PRO ASP SER VAL HIS ASN SER SER PHE
SEQRES 10 D 273 VAL LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN
SEQRES 11 D 273 TRP LEU ASP THR GLN PHE LEU PRO TYR GLY SER PRO GLU
SEQRES 12 D 273 GLU PRO LEU THR SER MSE PHE PHE GLY PRO LYS PHE LEU
SEQRES 13 D 273 ALA HIS LYS LEU TYR GLN LEU CYS SER PRO GLU ASP LEU
SEQRES 14 D 273 ALA LEU ALA SER SER LEU VAL ARG PRO SER SER LEU PHE
SEQRES 15 D 273 MSE GLU ASP LEU SER LYS ALA LYS TYR PHE THR ASP GLU
SEQRES 16 D 273 ARG PHE GLY SER VAL LYS ARG VAL TYR ILE VAL CYS THR
SEQRES 17 D 273 GLU ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN
SEQRES 18 D 273 ILE ASP ASN ILE GLY VAL THR GLU ALA ILE GLU ILE LYS
SEQRES 19 D 273 GLY ALA ASP HIS MSE ALA MSE LEU CYS GLU PRO GLN LYS
SEQRES 20 D 273 LEU CYS ALA SER LEU LEU GLU ILE ALA HIS LYS TYR ASN
SEQRES 21 D 273 MET ALA GLY ASP PRO LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 1XKL MSE A 63 MET SELENOMETHIONINE
MODRES 1XKL MSE A 66 MET SELENOMETHIONINE
MODRES 1XKL MSE A 85 MET SELENOMETHIONINE
MODRES 1XKL MSE A 91 MET SELENOMETHIONINE
MODRES 1XKL MSE A 108 MET SELENOMETHIONINE
MODRES 1XKL MSE A 149 MET SELENOMETHIONINE
MODRES 1XKL MSE A 183 MET SELENOMETHIONINE
MODRES 1XKL MSE A 239 MET SELENOMETHIONINE
MODRES 1XKL MSE A 241 MET SELENOMETHIONINE
MODRES 1XKL MSE B 63 MET SELENOMETHIONINE
MODRES 1XKL MSE B 66 MET SELENOMETHIONINE
MODRES 1XKL MSE B 85 MET SELENOMETHIONINE
MODRES 1XKL MSE B 91 MET SELENOMETHIONINE
MODRES 1XKL MSE B 108 MET SELENOMETHIONINE
MODRES 1XKL MSE B 149 MET SELENOMETHIONINE
MODRES 1XKL MSE B 183 MET SELENOMETHIONINE
MODRES 1XKL MSE B 239 MET SELENOMETHIONINE
MODRES 1XKL MSE B 241 MET SELENOMETHIONINE
MODRES 1XKL MSE C 63 MET SELENOMETHIONINE
MODRES 1XKL MSE C 66 MET SELENOMETHIONINE
MODRES 1XKL MSE C 85 MET SELENOMETHIONINE
MODRES 1XKL MSE C 91 MET SELENOMETHIONINE
MODRES 1XKL MSE C 108 MET SELENOMETHIONINE
MODRES 1XKL MSE C 149 MET SELENOMETHIONINE
MODRES 1XKL MSE C 183 MET SELENOMETHIONINE
MODRES 1XKL MSE C 239 MET SELENOMETHIONINE
MODRES 1XKL MSE C 241 MET SELENOMETHIONINE
MODRES 1XKL MSE D 63 MET SELENOMETHIONINE
MODRES 1XKL MSE D 66 MET SELENOMETHIONINE
MODRES 1XKL MSE D 85 MET SELENOMETHIONINE
MODRES 1XKL MSE D 91 MET SELENOMETHIONINE
MODRES 1XKL MSE D 108 MET SELENOMETHIONINE
MODRES 1XKL MSE D 149 MET SELENOMETHIONINE
MODRES 1XKL MSE D 183 MET SELENOMETHIONINE
MODRES 1XKL MSE D 239 MET SELENOMETHIONINE
MODRES 1XKL MSE D 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 STH A 297 12
HET STH B 298 12
HET STH C 299 12
HET STH D 300 12
HETNAM MSE SELENOMETHIONINE
HETNAM STH 2-AMINO-4H-1,3-BENZOXATHIIN-4-OL
FORMUL 1 MSE 36(C5 H11 N1 O2 SE1)
FORMUL 5 STH 4(C8 H9 N1 O2 S1)
FORMUL 9 HOH *926(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 SER A 68 1 15
HELIX 5 5 LEU A 82 TYR A 94 1 13
HELIX 6 6 SER A 116 ARG A 125 1 10
HELIX 7 7 GLY A 152 LEU A 160 1 9
HELIX 8 8 SER A 165 VAL A 176 1 12
HELIX 9 9 PHE A 182 ALA A 189 1 8
HELIX 10 10 ARG A 196 VAL A 200 5 5
HELIX 11 11 PRO A 214 GLY A 226 1 13
HELIX 12 12 MSE A 239 GLU A 244 1 6
HELIX 13 13 GLU A 244 TYR A 259 1 16
HELIX 14 14 GLY B 16 TYR B 21 5 6
HELIX 15 15 LYS B 22 ALA B 30 1 9
HELIX 16 16 LYS B 48 LEU B 52 5 5
HELIX 17 17 THR B 54 SER B 68 1 15
HELIX 18 18 LEU B 82 TYR B 94 1 13
HELIX 19 19 SER B 116 THR B 126 1 11
HELIX 20 20 PRO B 127 LEU B 132 5 6
HELIX 21 21 GLY B 152 LEU B 160 1 9
HELIX 22 22 SER B 165 VAL B 176 1 12
HELIX 23 23 PHE B 182 ALA B 189 1 8
HELIX 24 24 ARG B 196 VAL B 200 5 5
HELIX 25 25 PRO B 214 GLY B 226 1 13
HELIX 26 26 MSE B 239 GLU B 244 1 6
HELIX 27 27 GLU B 244 ILE B 255 1 12
HELIX 28 28 GLY C 16 TYR C 21 5 6
HELIX 29 29 LYS C 22 ALA C 30 1 9
HELIX 30 30 LYS C 48 LEU C 52 5 5
HELIX 31 31 THR C 54 LEU C 69 1 16
HELIX 32 32 LEU C 82 TYR C 94 1 13
HELIX 33 33 SER C 116 THR C 126 1 11
HELIX 34 34 PRO C 127 LEU C 132 5 6
HELIX 35 35 GLY C 152 LEU C 160 1 9
HELIX 36 36 SER C 165 VAL C 176 1 12
HELIX 37 37 PHE C 182 LYS C 188 1 7
HELIX 38 38 ARG C 196 VAL C 200 5 5
HELIX 39 39 PRO C 214 GLY C 226 1 13
HELIX 40 40 MSE C 239 GLU C 244 1 6
HELIX 41 41 GLU C 244 ALA C 256 1 13
HELIX 42 42 GLY D 16 TYR D 21 5 6
HELIX 43 43 LEU D 23 ALA D 30 1 8
HELIX 44 44 LYS D 48 LEU D 52 5 5
HELIX 45 45 THR D 54 LEU D 69 1 16
HELIX 46 46 LEU D 82 TYR D 94 1 13
HELIX 47 47 SER D 116 ARG D 125 1 10
HELIX 48 48 PRO D 127 LEU D 132 5 6
HELIX 49 49 GLY D 152 LEU D 160 1 9
HELIX 50 50 SER D 165 VAL D 176 1 12
HELIX 51 51 PHE D 182 SER D 187 1 6
HELIX 52 52 ARG D 196 VAL D 200 5 5
HELIX 53 53 PRO D 214 ILE D 225 1 12
HELIX 54 54 MSE D 239 GLU D 244 1 6
HELIX 55 55 GLU D 244 TYR D 259 1 16
SHEET 1 A 6 LYS A 33 ALA A 36 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 233 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 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 PHE B 150 N GLN B 135
SHEET 1 E 6 LYS C 33 LEU C 37 0
SHEET 2 E 6 HIS C 6 VAL C 10 1 N PHE C 7 O LYS C 33
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 VAL C 102 N LEU C 77
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 233 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 HIS D 80 1 O VAL D 78 N VAL D 10
SHEET 4 G 6 ILE D 98 LEU D 104 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 PHE D 103
SHEET 6 G 6 GLU D 229 ILE D 233 1 O ILE D 233 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
LINK OG SER A 81 C7 STH A 297
LINK OG SER B 81 C7 STH B 298
LINK OG SER C 81 C7 STH C 299
LINK OG SER D 81 C7 STH D 300
CRYST1 136.457 167.773 44.831 90.00 90.00 90.00 P 21 21 2 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 0.007328 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005960 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022306 0.00000
TER 2043 ASN A 260
TER 4066 LYS B 258
TER 6101 TYR C 259
TER 8135 ASN D 260
MASTER 390 0 40 55 32 0 0 6 9105 4 340 84
END |