HEADER TRANSFERASE 28-JUL-06 2DV7
TITLE CRYSTAL STRUCTURE OF LYS187 TO ARG MUTANT OF DIPHTHINE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPHTHINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPHTHAMIDE BIOSYNTHESIS METHYLTRANSFERASE;
COMPND 5 EC: 2.1.1.98;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: OT3;
SOURCE 5 GENE: DPHB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS TRANSFERASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MIZUTANI,Y.MATSUURA,K.SARABOJI,S.M.MALATHY SONY,M.N.PONNUSWAMY,
AUTHOR 2 T.S.KUMAREVEL,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 3 INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 2DV7 1 REMARK
REVDAT 4 10-NOV-21 2DV7 1 REMARK SEQADV
REVDAT 3 13-JUL-11 2DV7 1 VERSN
REVDAT 2 24-FEB-09 2DV7 1 VERSN
REVDAT 1 28-JAN-07 2DV7 0
JRNL AUTH H.MIZUTANI,Y.MATSUURA,K.SARABOJI,S.M.MALATHY SONY,
JRNL AUTH 2 M.N.PONNUSWAMY,T.S.KUMAREVEL,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF DIPHTHINE SYNTHASE FROM PYROCOCCUS
JRNL TITL 2 HORIKOSHII OT3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2179249.510
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 35505
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) : 0.215
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1767
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5491
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 308
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 313
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.21000
REMARK 3 B22 (A**2) : 2.21000
REMARK 3 B33 (A**2) : -4.41000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.31
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 1.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.320 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 46.51
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 : GOL.PARAM
REMARK 3 PARAMETER FILE 5 : SAH.PARAM
REMARK 3 PARAMETER FILE 6 : MES.PARAM
REMARK 3 PARAMETER FILE 7 : 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 : GOL.TOP
REMARK 3 TOPOLOGY FILE 5 : SAH.TOP
REMARK 3 TOPOLOGY FILE 6 : MES.TOP
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000025883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : BENDING MAGNET
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 : 35614
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.60
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
REMARK 200 R SYM FOR SHELL (I) : 0.34800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1WNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 0.1M MES, 0.01M
REMARK 280 CO CHLORIDE, PH 6.5, MICROBATCH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 69.07800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.91850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.91850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.53900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.91850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.91850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 103.61700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.91850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.91850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.53900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.91850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.91850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 103.61700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.07800
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: 7410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 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 TYR A 11 -56.45 -122.36
REMARK 500 ARG A 258 -8.83 -50.41
REMARK 500 TYR B 11 -53.69 -128.90
REMARK 500 MET B 39 79.47 -115.25
REMARK 500 LEU B 89 -0.95 71.42
REMARK 500 THR B 146 10.94 -140.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WNG RELATED DB: PDB
REMARK 900 RELATED ID: 2DV3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(L65R)
REMARK 900 RELATED ID: 2DV4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(L65Q)
REMARK 900 RELATED ID: 2DV5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(L65A)
REMARK 900 RELATED ID: PHO001000725.12 RELATED DB: TARGETDB
DBREF 2DV7 A 1 265 UNP O58456 DPHB_PYRHO 1 265
DBREF 2DV7 B 1 265 UNP O58456 DPHB_PYRHO 1 265
SEQADV 2DV7 ARG A 187 UNP O58456 LYS 187 ENGINEERED MUTATION
SEQADV 2DV7 ARG B 187 UNP O58456 LYS 187 ENGINEERED MUTATION
SEQRES 1 A 265 MET VAL LEU TYR PHE ILE GLY LEU GLY LEU TYR ASP GLU
SEQRES 2 A 265 ARG ASP ILE THR VAL LYS GLY LEU GLU ILE ALA LYS LYS
SEQRES 3 A 265 CYS ASP TYR VAL PHE ALA GLU PHE TYR THR SER LEU MET
SEQRES 4 A 265 ALA GLY THR THR LEU GLY ARG ILE GLN LYS LEU ILE GLY
SEQRES 5 A 265 LYS GLU ILE ARG VAL LEU SER ARG GLU ASP VAL GLU LEU
SEQRES 6 A 265 ASN PHE GLU ASN ILE VAL LEU PRO LEU ALA LYS GLU ASN
SEQRES 7 A 265 ASP VAL ALA PHE LEU THR PRO GLY ASP PRO LEU VAL ALA
SEQRES 8 A 265 THR THR HIS ALA GLU LEU ARG ILE ARG ALA LYS ARG ALA
SEQRES 9 A 265 GLY VAL GLU SER TYR VAL ILE HIS ALA PRO SER ILE TYR
SEQRES 10 A 265 SER ALA VAL GLY ILE THR GLY LEU HIS ILE TYR LYS PHE
SEQRES 11 A 265 GLY LYS SER ALA THR VAL ALA TYR PRO GLU GLY ASN TRP
SEQRES 12 A 265 PHE PRO THR SER TYR TYR ASP VAL ILE LYS GLU ASN ALA
SEQRES 13 A 265 GLU ARG GLY LEU HIS THR LEU LEU PHE LEU ASP ILE LYS
SEQRES 14 A 265 ALA GLU LYS ARG MET TYR MET THR ALA ASN GLU ALA MET
SEQRES 15 A 265 GLU LEU LEU LEU ARG VAL GLU ASP MET LYS LYS GLY GLY
SEQRES 16 A 265 VAL PHE THR ASP ASP THR LEU VAL VAL VAL LEU ALA ARG
SEQRES 17 A 265 ALA GLY SER LEU ASN PRO THR ILE ARG ALA GLY TYR VAL
SEQRES 18 A 265 LYS ASP LEU ILE ARG GLU ASP PHE GLY ASP PRO PRO HIS
SEQRES 19 A 265 ILE LEU ILE VAL PRO GLY LYS LEU HIS ILE VAL GLU ALA
SEQRES 20 A 265 GLU TYR LEU VAL GLU ILE ALA GLY ALA PRO ARG GLU ILE
SEQRES 21 A 265 LEU ARG VAL ASN VAL
SEQRES 1 B 265 MET VAL LEU TYR PHE ILE GLY LEU GLY LEU TYR ASP GLU
SEQRES 2 B 265 ARG ASP ILE THR VAL LYS GLY LEU GLU ILE ALA LYS LYS
SEQRES 3 B 265 CYS ASP TYR VAL PHE ALA GLU PHE TYR THR SER LEU MET
SEQRES 4 B 265 ALA GLY THR THR LEU GLY ARG ILE GLN LYS LEU ILE GLY
SEQRES 5 B 265 LYS GLU ILE ARG VAL LEU SER ARG GLU ASP VAL GLU LEU
SEQRES 6 B 265 ASN PHE GLU ASN ILE VAL LEU PRO LEU ALA LYS GLU ASN
SEQRES 7 B 265 ASP VAL ALA PHE LEU THR PRO GLY ASP PRO LEU VAL ALA
SEQRES 8 B 265 THR THR HIS ALA GLU LEU ARG ILE ARG ALA LYS ARG ALA
SEQRES 9 B 265 GLY VAL GLU SER TYR VAL ILE HIS ALA PRO SER ILE TYR
SEQRES 10 B 265 SER ALA VAL GLY ILE THR GLY LEU HIS ILE TYR LYS PHE
SEQRES 11 B 265 GLY LYS SER ALA THR VAL ALA TYR PRO GLU GLY ASN TRP
SEQRES 12 B 265 PHE PRO THR SER TYR TYR ASP VAL ILE LYS GLU ASN ALA
SEQRES 13 B 265 GLU ARG GLY LEU HIS THR LEU LEU PHE LEU ASP ILE LYS
SEQRES 14 B 265 ALA GLU LYS ARG MET TYR MET THR ALA ASN GLU ALA MET
SEQRES 15 B 265 GLU LEU LEU LEU ARG VAL GLU ASP MET LYS LYS GLY GLY
SEQRES 16 B 265 VAL PHE THR ASP ASP THR LEU VAL VAL VAL LEU ALA ARG
SEQRES 17 B 265 ALA GLY SER LEU ASN PRO THR ILE ARG ALA GLY TYR VAL
SEQRES 18 B 265 LYS ASP LEU ILE ARG GLU ASP PHE GLY ASP PRO PRO HIS
SEQRES 19 B 265 ILE LEU ILE VAL PRO GLY LYS LEU HIS ILE VAL GLU ALA
SEQRES 20 B 265 GLU TYR LEU VAL GLU ILE ALA GLY ALA PRO ARG GLU ILE
SEQRES 21 B 265 LEU ARG VAL ASN VAL
HET SO4 A1302 5
HET SO4 A1303 5
HET SAH A1300 26
HET MES A1501 12
HET GOL A1402 6
HET GOL A1403 6
HET SO4 B1301 5
HET SO4 B1304 5
HET SO4 B1305 5
HET MES B1502 12
HET MES B1503 12
HET GOL B1401 6
HETNAM SO4 SULFATE ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 5 SAH C14 H20 N6 O5 S
FORMUL 6 MES 3(C6 H13 N O4 S)
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 15 HOH *313(H2 O)
HELIX 1 1 ASP A 12 ILE A 16 5 5
HELIX 2 2 THR A 17 LYS A 26 1 10
HELIX 3 3 THR A 43 GLY A 52 1 10
HELIX 4 4 SER A 59 VAL A 71 1 13
HELIX 5 5 VAL A 71 LYS A 76 1 6
HELIX 6 6 HIS A 94 ALA A 104 1 11
HELIX 7 7 SER A 115 VAL A 120 1 6
HELIX 8 8 GLY A 121 GLY A 124 5 4
HELIX 9 9 HIS A 126 TYR A 128 5 3
HELIX 10 10 THR A 146 ARG A 158 1 13
HELIX 11 11 ALA A 170 ARG A 173 5 4
HELIX 12 12 THR A 177 LYS A 193 1 17
HELIX 13 13 VAL A 221 ILE A 225 1 5
HELIX 14 14 HIS A 243 ALA A 254 1 12
HELIX 15 15 PRO A 257 ARG A 262 5 6
HELIX 16 16 ASP B 12 ILE B 16 5 5
HELIX 17 17 THR B 17 LYS B 26 1 10
HELIX 18 18 THR B 43 GLY B 52 1 10
HELIX 19 19 SER B 59 VAL B 71 1 13
HELIX 20 20 VAL B 71 LYS B 76 1 6
HELIX 21 21 ALA B 95 ALA B 104 1 10
HELIX 22 22 SER B 115 VAL B 120 1 6
HELIX 23 23 GLY B 121 GLY B 124 5 4
HELIX 24 24 HIS B 126 PHE B 130 5 5
HELIX 25 25 THR B 146 ARG B 158 1 13
HELIX 26 26 THR B 177 LYS B 193 1 17
HELIX 27 27 VAL B 221 ILE B 225 1 5
HELIX 28 28 HIS B 243 GLY B 255 1 13
HELIX 29 29 GLU B 259 ASN B 264 1 6
SHEET 1 A 5 ILE A 55 LEU A 58 0
SHEET 2 A 5 TYR A 29 GLU A 33 1 N VAL A 30 O ARG A 56
SHEET 3 A 5 ASP A 79 THR A 84 1 O ALA A 81 N PHE A 31
SHEET 4 A 5 VAL A 2 GLY A 7 1 N VAL A 2 O VAL A 80
SHEET 5 A 5 SER A 108 ILE A 111 1 O TYR A 109 N PHE A 5
SHEET 1 B 5 PHE A 130 VAL A 136 0
SHEET 2 B 5 HIS A 161 LEU A 166 1 O HIS A 161 N GLY A 131
SHEET 3 B 5 HIS A 234 VAL A 238 -1 O LEU A 236 N LEU A 164
SHEET 4 B 5 LEU A 202 ALA A 207 -1 N VAL A 204 O ILE A 237
SHEET 5 B 5 THR A 215 TYR A 220 -1 O ARG A 217 N VAL A 205
SHEET 1 C 2 ILE A 168 LYS A 169 0
SHEET 2 C 2 MET A 174 TYR A 175 -1 O MET A 174 N LYS A 169
SHEET 1 D 5 ILE B 55 LEU B 58 0
SHEET 2 D 5 TYR B 29 GLU B 33 1 N ALA B 32 O LEU B 58
SHEET 3 D 5 ASP B 79 THR B 84 1 O ALA B 81 N PHE B 31
SHEET 4 D 5 VAL B 2 GLY B 7 1 N TYR B 4 O VAL B 80
SHEET 5 D 5 GLU B 107 ILE B 111 1 O ILE B 111 N PHE B 5
SHEET 1 E 5 ALA B 134 VAL B 136 0
SHEET 2 E 5 THR B 162 LEU B 166 1 O PHE B 165 N ALA B 134
SHEET 3 E 5 HIS B 234 VAL B 238 -1 O LEU B 236 N LEU B 164
SHEET 4 E 5 LEU B 202 ALA B 207 -1 N VAL B 204 O ILE B 237
SHEET 5 E 5 THR B 215 TYR B 220 -1 O ARG B 217 N VAL B 205
SHEET 1 F 2 ILE B 168 LYS B 169 0
SHEET 2 F 2 MET B 174 TYR B 175 -1 O MET B 174 N LYS B 169
CISPEP 1 PRO A 232 PRO A 233 0 -0.05
CISPEP 2 PRO B 232 PRO B 233 0 -0.11
SITE 1 AC1 3 ARG B 46 TYR B 128 HIS B 243
SITE 1 AC2 4 ARG A 60 ALA A 91 HOH A1589 LYS B 49
SITE 1 AC3 4 TYR A 11 SER A 211 LEU A 212 ASN A 213
SITE 1 AC4 3 PRO B 257 ARG B 258 GLU B 259
SITE 1 AC5 6 ARG B 46 LYS B 129 LYS B 241 HIS B 243
SITE 2 AC5 6 HOH B1592 HOH B1619
SITE 1 AC6 18 LEU A 10 THR A 36 SER A 37 GLY A 86
SITE 2 AC6 18 ASP A 87 VAL A 90 SER A 115 ILE A 116
SITE 3 AC6 18 PHE A 165 LEU A 166 LEU A 206 ARG A 208
SITE 4 AC6 18 ALA A 209 PRO A 233 HIS A 234 ILE A 235
SITE 5 AC6 18 HOH A1533 HOH A1544
SITE 1 AC7 5 MET A 39 THR A 42 THR A 43 LEU A 44
SITE 2 AC7 5 VAL A 57
SITE 1 AC8 4 GLY B 86 SER B 115 ILE B 116 HOH B1506
SITE 1 AC9 4 ASP B 200 TYR B 220 LYS B 222 GLU B 259
SITE 1 BC1 6 TRP A 143 LEU B 38 MET B 39 THR B 42
SITE 2 BC1 6 THR B 43 LEU B 44
SITE 1 BC2 6 TYR A 128 LEU A 160 HIS A 243 HOH A1639
SITE 2 BC2 6 ASN B 66 LYS B 132
SITE 1 BC3 2 THR A 43 ARG A 46
CRYST1 105.837 105.837 138.156 90.00 90.00 90.00 P 41 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 0.009448 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009448 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007238 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
