HEADER OXIDOREDUCTASE 21-FEB-07 2EF7
TITLE CRYSTAL STRUCTURE OF ST2348, A HYPOTHETICAL PROTEIN WITH CBS DOMAINS
TITLE 2 FROM SULFOLOBUS TOKODAII STRAIN7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN ST2348;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;
SOURCE 3 ORGANISM_TAXID: 273063;
SOURCE 4 STRAIN: STRAIN 7;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL-X;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21A
KEYWDS CBS-DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.AGARI,P.KARTHE,T.KUMAREVEL,S.YOKOYAMA,S.KURAMITSU,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 13-JUL-11 2EF7 1 VERSN
REVDAT 3 21-APR-10 2EF7 1 JRNL
REVDAT 2 24-FEB-09 2EF7 1 VERSN
REVDAT 1 21-AUG-07 2EF7 0
JRNL AUTH P.RAGUNATHAN,T.KUMAREVEL,Y.AGARI,A.SHINKAI,S.KURAMITSU,
JRNL AUTH 2 S.YOKOYAMA,K.PONNURAJ
JRNL TITL CRYSTAL STRUCTURE OF ST2348, A CBS DOMAIN PROTEIN, FROM
JRNL TITL 2 HYPERTHERMOPHILIC ARCHAEON SULFOLOBUS TOKODAII
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 375 124 2008
JRNL REFN ISSN 0006-291X
JRNL PMID 18691556
JRNL DOI 10.1016/J.BBRC.2008.07.140
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) : 39.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1397823.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 17453
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) : 0.216
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1734
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) (%) : 98.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2516
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 290
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 134
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -10.60000
REMARK 3 B33 (A**2) : 10.77000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
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) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.290 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.260 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 50.18
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB026590.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97897, 0.9, 0.97929
REMARK 200 MONOCHROMATOR : SI DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17492
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.5000
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 (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.25100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 160MM AMMONIUM CHLORIDE, 16%(W/V)
REMARK 280 POLYETHYLENE GLYCOL 3350, PH 6.3, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-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 25.71000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.63600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.71000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.63600
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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
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 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 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 GLU A 128
REMARK 465 THR A 129
REMARK 465 MSE A 130
REMARK 465 GLY A 131
REMARK 465 GLU A 132
REMARK 465 TYR A 133
REMARK 465 MSE B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 PHE B 127
REMARK 465 GLU B 128
REMARK 465 THR B 129
REMARK 465 TYR B 133
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 44 -8.44 75.55
REMARK 500 GLN B 13 117.54 -171.02
REMARK 500 ASP B 42 47.12 -97.09
REMARK 500 SER B 76 134.45 -171.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 164 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 193 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B 174 DISTANCE = 5.96 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: STO001002348.1 RELATED DB: TARGETDB
DBREF 2EF7 A 1 133 UNP Q96Y20 Q96Y20_SULTO 1 133
DBREF 2EF7 B 1 133 UNP Q96Y20 Q96Y20_SULTO 1 133
SEQRES 1 A 133 MSE GLU GLU GLU ILE VAL LYS GLU TYR MSE LYS THR GLN
SEQRES 2 A 133 VAL ILE SER VAL THR LYS ASP ALA LYS LEU ASN ASP ILE
SEQRES 3 A 133 ALA LYS VAL MSE THR GLU LYS ASN ILE GLY SER VAL ILE
SEQRES 4 A 133 VAL VAL ASP GLY ASN LYS PRO VAL GLY ILE ILE THR GLU
SEQRES 5 A 133 ARG ASP ILE VAL LYS ALA ILE GLY LYS GLY LYS SER LEU
SEQRES 6 A 133 GLU THR LYS ALA GLU GLU PHE MSE THR ALA SER LEU ILE
SEQRES 7 A 133 THR ILE ARG GLU ASP SER PRO ILE THR GLY ALA LEU ALA
SEQRES 8 A 133 LEU MSE ARG GLN PHE ASN ILE ARG HIS LEU PRO VAL VAL
SEQRES 9 A 133 ASP ASP LYS GLY ASN LEU LYS GLY ILE ILE SER ILE ARG
SEQRES 10 A 133 ASP ILE THR ARG ALA ILE ASP ASP MSE PHE GLU THR MSE
SEQRES 11 A 133 GLY GLU TYR
SEQRES 1 B 133 MSE GLU GLU GLU ILE VAL LYS GLU TYR MSE LYS THR GLN
SEQRES 2 B 133 VAL ILE SER VAL THR LYS ASP ALA LYS LEU ASN ASP ILE
SEQRES 3 B 133 ALA LYS VAL MSE THR GLU LYS ASN ILE GLY SER VAL ILE
SEQRES 4 B 133 VAL VAL ASP GLY ASN LYS PRO VAL GLY ILE ILE THR GLU
SEQRES 5 B 133 ARG ASP ILE VAL LYS ALA ILE GLY LYS GLY LYS SER LEU
SEQRES 6 B 133 GLU THR LYS ALA GLU GLU PHE MSE THR ALA SER LEU ILE
SEQRES 7 B 133 THR ILE ARG GLU ASP SER PRO ILE THR GLY ALA LEU ALA
SEQRES 8 B 133 LEU MSE ARG GLN PHE ASN ILE ARG HIS LEU PRO VAL VAL
SEQRES 9 B 133 ASP ASP LYS GLY ASN LEU LYS GLY ILE ILE SER ILE ARG
SEQRES 10 B 133 ASP ILE THR ARG ALA ILE ASP ASP MSE PHE GLU THR MSE
SEQRES 11 B 133 GLY GLU TYR
MODRES 2EF7 MSE A 1 MET SELENOMETHIONINE
MODRES 2EF7 MSE A 10 MET SELENOMETHIONINE
MODRES 2EF7 MSE A 30 MET SELENOMETHIONINE
MODRES 2EF7 MSE A 73 MET SELENOMETHIONINE
MODRES 2EF7 MSE A 93 MET SELENOMETHIONINE
MODRES 2EF7 MSE A 126 MET SELENOMETHIONINE
MODRES 2EF7 MSE B 10 MET SELENOMETHIONINE
MODRES 2EF7 MSE B 30 MET SELENOMETHIONINE
MODRES 2EF7 MSE B 73 MET SELENOMETHIONINE
MODRES 2EF7 MSE B 93 MET SELENOMETHIONINE
MODRES 2EF7 MSE B 126 MET SELENOMETHIONINE
MODRES 2EF7 MSE B 130 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 10 8
HET MSE A 30 8
HET MSE A 73 8
HET MSE A 93 8
HET MSE A 126 8
HET MSE B 10 8
HET MSE B 30 8
HET MSE B 73 8
HET MSE B 93 8
HET MSE B 126 8
HET MSE B 130 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 HOH *134(H2 O)
HELIX 1 1 ILE A 5 TYR A 9 5 5
HELIX 2 2 LYS A 22 ASN A 34 1 13
HELIX 3 3 GLU A 52 LYS A 61 1 10
HELIX 4 4 LYS A 68 PHE A 72 5 5
HELIX 5 5 PRO A 85 ASN A 97 1 13
HELIX 6 6 ILE A 116 PHE A 127 1 12
HELIX 7 7 ILE B 5 TYR B 9 5 5
HELIX 8 8 LYS B 22 ASN B 34 1 13
HELIX 9 9 GLU B 52 LYS B 61 1 10
HELIX 10 10 LYS B 68 PHE B 72 5 5
HELIX 11 11 PRO B 85 PHE B 96 1 12
HELIX 12 12 ILE B 116 ASP B 125 1 10
SHEET 1 A 4 SER A 16 THR A 18 0
SHEET 2 A 4 SER A 37 ASP A 42 1 O VAL A 41 N VAL A 17
SHEET 3 A 4 LYS A 45 THR A 51 -1 O VAL A 47 N VAL A 40
SHEET 4 A 4 THR A 74 ALA A 75 -1 O THR A 74 N ILE A 49
SHEET 1 B 3 ILE A 80 ARG A 81 0
SHEET 2 B 3 HIS A 100 VAL A 104 1 O VAL A 104 N ILE A 80
SHEET 3 B 3 LEU A 110 SER A 115 -1 O GLY A 112 N VAL A 103
SHEET 1 C 4 LYS B 11 THR B 12 0
SHEET 2 C 4 LEU B 110 SER B 115 -1 O ILE B 113 N LYS B 11
SHEET 3 C 4 HIS B 100 VAL B 104 -1 N VAL B 103 O GLY B 112
SHEET 4 C 4 ILE B 80 ARG B 81 1 N ILE B 80 O VAL B 104
SHEET 1 D 4 SER B 16 THR B 18 0
SHEET 2 D 4 SER B 37 VAL B 41 1 O VAL B 41 N VAL B 17
SHEET 3 D 4 PRO B 46 THR B 51 -1 O VAL B 47 N VAL B 40
SHEET 4 D 4 THR B 74 ALA B 75 -1 O THR B 74 N ILE B 49
LINK C MSE A 1 N GLU A 2 1555 1555 1.33
LINK C TYR A 9 N MSE A 10 1555 1555 1.33
LINK C MSE A 10 N LYS A 11 1555 1555 1.32
LINK C VAL A 29 N MSE A 30 1555 1555 1.33
LINK C MSE A 30 N THR A 31 1555 1555 1.33
LINK C PHE A 72 N MSE A 73 1555 1555 1.33
LINK C MSE A 73 N THR A 74 1555 1555 1.33
LINK C LEU A 92 N MSE A 93 1555 1555 1.33
LINK C MSE A 93 N ARG A 94 1555 1555 1.33
LINK C ASP A 125 N MSE A 126 1555 1555 1.33
LINK C MSE A 126 N PHE A 127 1555 1555 1.33
LINK C TYR B 9 N MSE B 10 1555 1555 1.33
LINK C MSE B 10 N LYS B 11 1555 1555 1.33
LINK C VAL B 29 N MSE B 30 1555 1555 1.33
LINK C MSE B 30 N THR B 31 1555 1555 1.33
LINK C PHE B 72 N MSE B 73 1555 1555 1.33
LINK C MSE B 73 N THR B 74 1555 1555 1.32
LINK C LEU B 92 N MSE B 93 1555 1555 1.33
LINK C MSE B 93 N ARG B 94 1555 1555 1.33
LINK C ASP B 125 N MSE B 126 1555 1555 1.33
LINK C MSE B 130 N GLY B 131 1555 1555 1.33
CRYST1 51.420 135.272 41.234 90.00 90.00 90.00 P 21 21 2 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 0.019448 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007393 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024252 0.00000
HETATM 1 N MSE A 1 22.916 -7.772 2.633 1.00 32.35 N
HETATM 2 CA MSE A 1 22.269 -6.856 1.659 1.00 33.62 C
HETATM 3 C MSE A 1 22.782 -5.436 1.847 1.00 33.16 C
HETATM 4 O MSE A 1 23.241 -5.061 2.929 1.00 35.98 O
HETATM 5 CB MSE A 1 20.762 -6.873 1.869 1.00 37.16 C
HETATM 6 CG MSE A 1 20.156 -8.229 1.708 1.00 50.40 C
HETATM 7 SE MSE A 1 18.349 -8.068 2.252 1.00 68.09 SE
HETATM 8 CE MSE A 1 18.501 -6.498 3.329 1.00 42.28 C
(ATOM LINES ARE NOT SHOWN.)
END
