HEADER TRANSFERASE 28-DEC-05 2DC5
TITLE CRYSTAL STRUCTURE OF MOUSE GLUTATHIONE S-TRANSFERASE, MU7
TITLE 2 (GSTM7) AT 1.6 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE, MU 7;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PX050309-01;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, GLUTATHIONE S-TRANSFERASE, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA,
KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 4 ANALYSES
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KAMO,S.KISHISHITA,K.MURAYAMA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2DC5 1 VERSN
REVDAT 1 28-JUN-06 2DC5 0
JRNL AUTH S.KAMO,S.KISHISHITA,K.MURAYAMA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF MOUSE GLUTATHIONE
JRNL TITL 2 S-TRANSFERASE, MU7 (GSTM7) AT 1.6 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 245598.630
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 113517
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) : 0.188
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5559
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 17342
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 915
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 : 3618
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.75000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : -1.30000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.09
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) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
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) : 1.960 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.710 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.140 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 45.39
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 4
REMARK 4 2DC5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JAN-06.
REMARK 100 THE RCSB ID CODE IS RCSB025239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.9790
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : MIRRORS
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113517
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.626
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0419
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.15300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.902
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2GTU
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M NA HEPES
REMARK 280 PH 7.5, 28% PEG 3350, 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 43.19250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.19250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.30500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 GLY A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 SER A 226
REMARK 465 GLY A 227
REMARK 465 PRO A 228
REMARK 465 SER A 229
REMARK 465 SER A 230
REMARK 465 GLY A 231
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 SER B 226
REMARK 465 GLY B 227
REMARK 465 PRO B 228
REMARK 465 SER B 229
REMARK 465 SER B 230
REMARK 465 GLY B 231
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 ALA A 45 167.63 -47.63
REMARK 500 PRO A 46 -3.38 -56.35
REMARK 500 PRO A 65 118.14 -39.02
REMARK 500 GLN A 79 114.48 78.08
REMARK 500 GLU B 56 -17.80 -140.87
REMARK 500 PRO B 65 124.33 -38.96
REMARK 500 GLN B 79 113.24 78.15
REMARK 500 LYS B 180 -1.03 73.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007000002.1 RELATED DB: TARGETDB
DBREF 2DC5 A 8 225 GB 30354091 AAH51924 1 218
DBREF 2DC5 B 8 225 GB 30354091 AAH51924 1 218
SEQADV 2DC5 GLY A 1 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER A 2 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER A 3 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY A 4 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER A 5 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER A 6 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY A 7 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 MSE A 8 GB 30354091 MET 1 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 10 GB 30354091 MET 3 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 42 GB 30354091 MET 35 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 112 GB 30354091 MET 105 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 116 GB 30354091 MET 109 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 141 GB 30354091 MET 134 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 142 GB 30354091 MET 135 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 205 GB 30354091 MET 198 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 215 GB 30354091 MET 208 MODIFIED RESIDUE
SEQADV 2DC5 MSE A 219 GB 30354091 MET 212 MODIFIED RESIDUE
SEQADV 2DC5 SER A 226 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY A 227 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 PRO A 228 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER A 229 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER A 230 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY A 231 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY B 1 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER B 2 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER B 3 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY B 4 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER B 5 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER B 6 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY B 7 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 MSE B 8 GB 30354091 MET 1 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 10 GB 30354091 MET 3 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 42 GB 30354091 MET 35 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 112 GB 30354091 MET 105 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 116 GB 30354091 MET 109 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 141 GB 30354091 MET 134 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 142 GB 30354091 MET 135 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 205 GB 30354091 MET 198 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 215 GB 30354091 MET 208 MODIFIED RESIDUE
SEQADV 2DC5 MSE B 219 GB 30354091 MET 212 MODIFIED RESIDUE
SEQADV 2DC5 SER B 226 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY B 227 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 PRO B 228 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER B 229 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 SER B 230 GB 30354091 CLONING ARTIFACT
SEQADV 2DC5 GLY B 231 GB 30354091 CLONING ARTIFACT
SEQRES 1 A 231 GLY SER SER GLY SER SER GLY MSE PRO MSE THR LEU GLY
SEQRES 2 A 231 TYR TRP ASP ILE ARG GLY LEU ALA HIS ALA ILE ARG LEU
SEQRES 3 A 231 PHE LEU GLU TYR THR ASP SER SER TYR GLU GLU LYS ARG
SEQRES 4 A 231 TYR THR MSE GLY ASP ALA PRO ASP TYR ASP GLN SER GLN
SEQRES 5 A 231 TRP LEU ASN GLU LYS PHE LYS LEU GLY LEU ASP PHE PRO
SEQRES 6 A 231 ASN LEU PRO TYR LEU ILE ASP GLY SER HIS LYS ILE THR
SEQRES 7 A 231 GLN SER ASN ALA ILE LEU ARG TYR LEU GLY ARG LYS HIS
SEQRES 8 A 231 ASN LEU CYS GLY GLU THR GLU GLU GLU ARG ILE ARG VAL
SEQRES 9 A 231 ASP ILE LEU GLU ASN GLN LEU MSE ASP ASN ARG MSE VAL
SEQRES 10 A 231 LEU ALA ARG LEU CYS TYR ASN ALA ASP PHE GLU LYS LEU
SEQRES 11 A 231 LYS PRO GLY TYR LEU GLU GLN LEU PRO GLY MSE MSE ARG
SEQRES 12 A 231 LEU TYR SER GLU PHE LEU GLY LYS ARG PRO TRP PHE ALA
SEQRES 13 A 231 GLY ASP LYS ILE THR PHE VAL ASP PHE ILE ALA TYR ASP
SEQRES 14 A 231 VAL LEU GLU ARG ASN GLN VAL PHE GLU ALA LYS CYS LEU
SEQRES 15 A 231 ASP ALA PHE PRO ASN LEU LYS ASP PHE ILE ALA ARG PHE
SEQRES 16 A 231 GLU GLY LEU LYS LYS ILE SER ASP TYR MSE LYS THR SER
SEQRES 17 A 231 ARG PHE LEU PRO ARG PRO MSE PHE THR LYS MSE ALA THR
SEQRES 18 A 231 TRP GLY SER ASN SER GLY PRO SER SER GLY
SEQRES 1 B 231 GLY SER SER GLY SER SER GLY MSE PRO MSE THR LEU GLY
SEQRES 2 B 231 TYR TRP ASP ILE ARG GLY LEU ALA HIS ALA ILE ARG LEU
SEQRES 3 B 231 PHE LEU GLU TYR THR ASP SER SER TYR GLU GLU LYS ARG
SEQRES 4 B 231 TYR THR MSE GLY ASP ALA PRO ASP TYR ASP GLN SER GLN
SEQRES 5 B 231 TRP LEU ASN GLU LYS PHE LYS LEU GLY LEU ASP PHE PRO
SEQRES 6 B 231 ASN LEU PRO TYR LEU ILE ASP GLY SER HIS LYS ILE THR
SEQRES 7 B 231 GLN SER ASN ALA ILE LEU ARG TYR LEU GLY ARG LYS HIS
SEQRES 8 B 231 ASN LEU CYS GLY GLU THR GLU GLU GLU ARG ILE ARG VAL
SEQRES 9 B 231 ASP ILE LEU GLU ASN GLN LEU MSE ASP ASN ARG MSE VAL
SEQRES 10 B 231 LEU ALA ARG LEU CYS TYR ASN ALA ASP PHE GLU LYS LEU
SEQRES 11 B 231 LYS PRO GLY TYR LEU GLU GLN LEU PRO GLY MSE MSE ARG
SEQRES 12 B 231 LEU TYR SER GLU PHE LEU GLY LYS ARG PRO TRP PHE ALA
SEQRES 13 B 231 GLY ASP LYS ILE THR PHE VAL ASP PHE ILE ALA TYR ASP
SEQRES 14 B 231 VAL LEU GLU ARG ASN GLN VAL PHE GLU ALA LYS CYS LEU
SEQRES 15 B 231 ASP ALA PHE PRO ASN LEU LYS ASP PHE ILE ALA ARG PHE
SEQRES 16 B 231 GLU GLY LEU LYS LYS ILE SER ASP TYR MSE LYS THR SER
SEQRES 17 B 231 ARG PHE LEU PRO ARG PRO MSE PHE THR LYS MSE ALA THR
SEQRES 18 B 231 TRP GLY SER ASN SER GLY PRO SER SER GLY
MODRES 2DC5 MSE A 8 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 10 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 42 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 112 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 116 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 141 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 142 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 205 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 215 MET SELENOMETHIONINE
MODRES 2DC5 MSE A 219 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 8 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 10 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 42 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 112 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 116 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 141 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 142 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 205 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 215 MET SELENOMETHIONINE
MODRES 2DC5 MSE B 219 MET SELENOMETHIONINE
HET MSE A 8 8
HET MSE A 10 8
HET MSE A 42 8
HET MSE A 112 8
HET MSE A 116 8
HET MSE A 141 8
HET MSE A 142 8
HET MSE A 205 8
HET MSE A 215 8
HET MSE A 219 8
HET MSE B 8 8
HET MSE B 10 8
HET MSE B 42 8
HET MSE B 112 8
HET MSE B 116 8
HET MSE B 141 8
HET MSE B 142 8
HET MSE B 205 8
HET MSE B 215 8
HET MSE B 219 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 HOH *563(H2 O)
HELIX 1 1 ARG A 18 LEU A 20 5 3
HELIX 2 2 ALA A 21 THR A 31 1 11
HELIX 3 3 GLN A 50 ASN A 55 1 6
HELIX 4 4 GLN A 79 HIS A 91 1 13
HELIX 5 5 THR A 97 TYR A 123 1 27
HELIX 6 6 ASP A 126 GLY A 150 1 25
HELIX 7 7 THR A 161 GLU A 178 1 18
HELIX 8 8 PHE A 185 LEU A 198 1 14
HELIX 9 9 LEU A 198 LYS A 206 1 9
HELIX 10 10 ALA B 21 THR B 31 1 11
HELIX 11 11 GLN B 50 ASN B 55 1 6
HELIX 12 12 GLN B 79 HIS B 91 1 13
HELIX 13 13 THR B 97 TYR B 123 1 27
HELIX 14 14 ASP B 126 GLY B 150 1 25
HELIX 15 15 PHE B 162 GLU B 178 1 17
HELIX 16 16 PHE B 185 GLY B 197 1 13
HELIX 17 17 LEU B 198 MSE B 205 1 8
SHEET 1 A 4 TYR A 35 TYR A 40 0
SHEET 2 A 4 MSE A 10 TRP A 15 1 N LEU A 12 O LYS A 38
SHEET 3 A 4 TYR A 69 ASP A 72 -1 O TYR A 69 N GLY A 13
SHEET 4 A 4 HIS A 75 THR A 78 -1 O ILE A 77 N LEU A 70
SHEET 1 B 4 TYR B 35 TYR B 40 0
SHEET 2 B 4 MSE B 10 TRP B 15 1 N LEU B 12 O LYS B 38
SHEET 3 B 4 TYR B 69 ASP B 72 -1 O ILE B 71 N THR B 11
SHEET 4 B 4 HIS B 75 THR B 78 -1 O ILE B 77 N LEU B 70
LINK C MSE A 8 N PRO A 9 1555 1555 1.34
LINK C PRO A 9 N MSE A 10 1555 1555 1.33
LINK C MSE A 10 N THR A 11 1555 1555 1.33
LINK C THR A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N GLY A 43 1555 1555 1.33
LINK C LEU A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N ASP A 113 1555 1555 1.33
LINK C ARG A 115 N MSE A 116 1555 1555 1.33
LINK C MSE A 116 N VAL A 117 1555 1555 1.33
LINK C GLY A 140 N MSE A 141 1555 1555 1.33
LINK C MSE A 141 N MSE A 142 1555 1555 1.33
LINK C MSE A 142 N ARG A 143 1555 1555 1.33
LINK C TYR A 204 N MSE A 205 1555 1555 1.33
LINK C MSE A 205 N LYS A 206 1555 1555 1.33
LINK C PRO A 214 N MSE A 215 1555 1555 1.33
LINK C MSE A 215 N PHE A 216 1555 1555 1.33
LINK C LYS A 218 N MSE A 219 1555 1555 1.33
LINK C MSE A 219 N ALA A 220 1555 1555 1.33
LINK C MSE B 8 N PRO B 9 1555 1555 1.34
LINK C PRO B 9 N MSE B 10 1555 1555 1.33
LINK C MSE B 10 N THR B 11 1555 1555 1.33
LINK C THR B 41 N MSE B 42 1555 1555 1.33
LINK C MSE B 42 N GLY B 43 1555 1555 1.33
LINK C LEU B 111 N MSE B 112 1555 1555 1.33
LINK C MSE B 112 N ASP B 113 1555 1555 1.33
LINK C ARG B 115 N MSE B 116 1555 1555 1.33
LINK C MSE B 116 N VAL B 117 1555 1555 1.33
LINK C GLY B 140 N MSE B 141 1555 1555 1.33
LINK C MSE B 141 N MSE B 142 1555 1555 1.33
LINK C MSE B 142 N ARG B 143 1555 1555 1.33
LINK C TYR B 204 N MSE B 205 1555 1555 1.33
LINK C MSE B 205 N LYS B 206 1555 1555 1.33
LINK C PRO B 214 N MSE B 215 1555 1555 1.33
LINK C MSE B 215 N PHE B 216 1555 1555 1.33
LINK C LYS B 218 N MSE B 219 1555 1555 1.33
LINK C MSE B 219 N ALA B 220 1555 1555 1.33
CISPEP 1 MSE A 8 PRO A 9 0 0.01
CISPEP 2 LEU A 67 PRO A 68 0 0.35
CISPEP 3 ARG A 213 PRO A 214 0 -0.21
CISPEP 4 ALA B 45 PRO B 46 0 -0.06
CISPEP 5 LEU B 67 PRO B 68 0 0.29
CISPEP 6 ARG B 213 PRO B 214 0 -0.20
CRYST1 86.385 94.610 57.761 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 0.011576 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010570 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017313 0.00000
HETATM 1 N MSE A 8 42.694 11.477 43.799 1.00 42.59 N
HETATM 2 CA MSE A 8 44.026 10.974 43.353 1.00 38.51 C
HETATM 3 C MSE A 8 44.279 11.340 41.895 1.00 32.29 C
HETATM 4 O MSE A 8 43.381 11.828 41.206 1.00 38.78 O
HETATM 5 CB MSE A 8 44.095 9.458 43.526 1.00 44.45 C
HETATM 6 CG MSE A 8 43.967 8.992 44.963 1.00 54.74 C
HETATM 7 SE MSE A 8 44.235 7.092 45.126 1.00 78.28 SE
HETATM 8 CE MSE A 8 42.447 6.497 44.690 1.00 62.28 C
(ATOM LINES ARE NOT SHOWN.)
END
