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HEADER TRANSFERASE 26-JUL-12 3VVM
TITLE CRYSTAL STRUCTURE OF G52A-P55G MUTANT OF L-SERINE-O-ACETYLTRANSFERASE
TITLE 2 FOUND IN D-CYCLOSERINE BIOSYNTHETIC PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HOMOSERINE O-TRANS-ACETYLASE;
COMPND 5 EC: 2.3.1.31;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LAVENDULAE SUBSP. LAVENDULAE;
SOURCE 3 ORGANISM_TAXID: 58340;
SOURCE 4 STRAIN: ATCC11924;
SOURCE 5 GENE: DCSE, METX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A(+)
KEYWDS D-CYCLOSERINE, ALPHA/BETA HYDROLASE DOMAIN, L-SERINE-O-
KEYWDS 2 ACETYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ODA,Y.MATOBA,T.KUMAGAI,M.NODA,M.SUGIYAMA
REVDAT 1 20-MAR-13 3VVM 0
JRNL AUTH K.ODA,Y.MATOBA,T.KUMAGAI,M.NODA,M.SUGIYAMA
JRNL TITL CRYSTALLOGRAPHIC STUDY TO DETERMINE THE SUBSTRATE
JRNL TITL 2 SPECIFICITY ON AN L-SERINE-ACETYLATING ENZYME FOUND IN THE
JRNL TITL 3 D-CYCLOSERINE BIOSYNTHETIC PATHWAY
JRNL REF J.BACTERIOL. 2013
JRNL REFN ESSN 1098-5530
JRNL PMID 23396912
JRNL DOI 10.1128/JB.02085-12
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2345468.360
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 77226
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) : 0.192
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3893
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11891
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 645
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5574
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 414
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.03000
REMARK 3 B22 (A**2) : 1.52000
REMARK 3 B33 (A**2) : -6.55000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.850 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 45.63
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: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3VVM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB095555.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-10
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 : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : FIXED EXIT DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78450
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 38.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.22700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.400
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: 2B61
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, TRIS, AMMONIUM ACETATE, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.28000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.28000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.16500
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: 4110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 ARG A 244
REMARK 465 ARG A 245
REMARK 465 ALA A 246
REMARK 465 ASP A 247
REMARK 465 GLN A 248
REMARK 465 GLY A 249
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 ARG B 244
REMARK 465 ARG B 245
REMARK 465 ALA B 246
REMARK 465 ASP B 247
REMARK 465 GLN B 248
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 ASP A 65 78.57 -170.87
REMARK 500 SER A 96 -165.19 -79.55
REMARK 500 CYS A 97 26.31 -140.11
REMARK 500 ARG A 115 -135.14 58.21
REMARK 500 SER A 149 -123.24 56.84
REMARK 500 GLU A 208 -75.00 33.81
REMARK 500 GLU A 254 -27.32 -142.06
REMARK 500 PHE A 322 79.13 -118.74
REMARK 500 ASP A 358 57.76 -119.88
REMARK 500 ARG B 2 -3.71 65.57
REMARK 500 ASP B 16 -132.68 47.24
REMARK 500 ASP B 65 76.81 -165.36
REMARK 500 CYS B 97 28.95 -141.64
REMARK 500 ARG B 115 -136.79 58.75
REMARK 500 SER B 149 -123.24 56.95
REMARK 500 ASP B 205 -119.84 46.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VVL RELATED DB: PDB
DBREF 3VVM A 1 374 UNP D2Z028 D2Z028_STRLA 1 374
DBREF 3VVM B 1 374 UNP D2Z028 D2Z028_STRLA 1 374
SEQADV 3VVM MET A -19 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM GLY A -18 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER A -17 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER A -16 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A -15 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A -14 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A -13 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A -12 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A -11 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A -10 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER A -9 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER A -8 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM GLY A -7 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM LEU A -6 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM VAL A -5 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM PRO A -4 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM ARG A -3 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM GLY A -2 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER A -1 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS A 0 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM ALA A 52 UNP D2Z028 GLY 52 ENGINEERED MUTATION
SEQADV 3VVM GLY A 55 UNP D2Z028 PRO 55 ENGINEERED MUTATION
SEQADV 3VVM MET B -19 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM GLY B -18 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER B -17 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER B -16 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B -15 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B -14 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B -13 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B -12 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B -11 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B -10 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER B -9 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER B -8 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM GLY B -7 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM LEU B -6 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM VAL B -5 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM PRO B -4 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM ARG B -3 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM GLY B -2 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM SER B -1 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM HIS B 0 UNP D2Z028 EXPRESSION TAG
SEQADV 3VVM ALA B 52 UNP D2Z028 GLY 52 ENGINEERED MUTATION
SEQADV 3VVM GLY B 55 UNP D2Z028 PRO 55 ENGINEERED MUTATION
SEQRES 1 A 394 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 394 LEU VAL PRO ARG GLY SER HIS MET ARG GLU PHE ILE PRO
SEQRES 3 A 394 PRO ALA SER ARG PHE ILE GLU LEU PRO ASP GLY PHE ALA
SEQRES 4 A 394 MET ARG ARG GLY GLY ALA LEU TYR GLY ALA ARG ILE ALA
SEQRES 5 A 394 TYR GLU THR PHE GLY SER LEU ASN ALA ALA ARG ASP ASN
SEQRES 6 A 394 ALA VAL LEU VAL LEU THR ALA LEU SER GLY ASP ALA HIS
SEQRES 7 A 394 ALA ALA SER ARG PRO ASP ASP PRO THR PRO GLY TRP TRP
SEQRES 8 A 394 GLU ALA MET VAL GLY PRO GLY LYS PRO VAL ASP THR ASP
SEQRES 9 A 394 LEU TRP HIS VAL ILE CYS VAL ASN SER LEU GLY SER CYS
SEQRES 10 A 394 LYS GLY SER THR GLY PRO ALA SER THR ASP PRO ARG THR
SEQRES 11 A 394 GLY GLU PRO TYR ARG LEU SER PHE PRO GLU LEU SER ILE
SEQRES 12 A 394 GLU ASP ILE ALA ASP ALA ALA ALA HIS THR VAL ARG ALA
SEQRES 13 A 394 LEU GLY ILE SER ARG LEU ALA CYS VAL VAL GLY ALA SER
SEQRES 14 A 394 MET GLY GLY MET SER ALA LEU ALA LEU LEU ALA ARG HIS
SEQRES 15 A 394 PRO GLU LEU ALA ARG THR HIS ILE SER LEU SER GLY ALA
SEQRES 16 A 394 VAL HIS ALA LEU PRO PHE SER ILE ALA VAL ARG SER LEU
SEQRES 17 A 394 GLN ARG GLU ALA ILE ARG SER ASP PRO GLY TRP LEU GLN
SEQRES 18 A 394 GLY HIS TYR ASP GLU GLY GLU GLY PRO ARG ARG GLY MET
SEQRES 19 A 394 LEU THR ALA ARG LYS LEU GLY MET MET THR TYR ARG SER
SEQRES 20 A 394 ALA GLN GLU TRP ASP CYS ARG PHE GLY ARG THR ARG ILE
SEQRES 21 A 394 GLY GLU ARG ARG ARG ALA ASP GLN GLY ARG PHE GLY PRO
SEQRES 22 A 394 GLU PHE GLU VAL GLU SER TYR LEU ASP PHE HIS ALA GLN
SEQRES 23 A 394 ARG PHE ALA ASP ARG PHE ASP PRO ASN SER TYR LEU TYR
SEQRES 24 A 394 LEU SER HIS ALA MET ASP GLN PHE ASP LEU GLY ASP GLY
SEQRES 25 A 394 GLY GLY GLY GLY GLY GLY ALA PRO GLY ALA LEU SER ARG
SEQRES 26 A 394 MET ARG VAL GLU ARG ALA LEU VAL MET GLY ALA ARG THR
SEQRES 27 A 394 ASP ILE LEU PHE PRO LEU SER GLN GLN GLN GLU ILE ALA
SEQRES 28 A 394 ASP GLY LEU SER ALA GLY GLY ALA ASP VAL SER PHE LEU
SEQRES 29 A 394 PRO VAL ASP THR PRO ALA GLY HIS ASP ALA PHE LEU VAL
SEQRES 30 A 394 ASP ILE GLU ARG PHE GLY PRO PRO VAL ALA LYS PHE LEU
SEQRES 31 A 394 ALA ILE VAL ALA
SEQRES 1 B 394 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 394 LEU VAL PRO ARG GLY SER HIS MET ARG GLU PHE ILE PRO
SEQRES 3 B 394 PRO ALA SER ARG PHE ILE GLU LEU PRO ASP GLY PHE ALA
SEQRES 4 B 394 MET ARG ARG GLY GLY ALA LEU TYR GLY ALA ARG ILE ALA
SEQRES 5 B 394 TYR GLU THR PHE GLY SER LEU ASN ALA ALA ARG ASP ASN
SEQRES 6 B 394 ALA VAL LEU VAL LEU THR ALA LEU SER GLY ASP ALA HIS
SEQRES 7 B 394 ALA ALA SER ARG PRO ASP ASP PRO THR PRO GLY TRP TRP
SEQRES 8 B 394 GLU ALA MET VAL GLY PRO GLY LYS PRO VAL ASP THR ASP
SEQRES 9 B 394 LEU TRP HIS VAL ILE CYS VAL ASN SER LEU GLY SER CYS
SEQRES 10 B 394 LYS GLY SER THR GLY PRO ALA SER THR ASP PRO ARG THR
SEQRES 11 B 394 GLY GLU PRO TYR ARG LEU SER PHE PRO GLU LEU SER ILE
SEQRES 12 B 394 GLU ASP ILE ALA ASP ALA ALA ALA HIS THR VAL ARG ALA
SEQRES 13 B 394 LEU GLY ILE SER ARG LEU ALA CYS VAL VAL GLY ALA SER
SEQRES 14 B 394 MET GLY GLY MET SER ALA LEU ALA LEU LEU ALA ARG HIS
SEQRES 15 B 394 PRO GLU LEU ALA ARG THR HIS ILE SER LEU SER GLY ALA
SEQRES 16 B 394 VAL HIS ALA LEU PRO PHE SER ILE ALA VAL ARG SER LEU
SEQRES 17 B 394 GLN ARG GLU ALA ILE ARG SER ASP PRO GLY TRP LEU GLN
SEQRES 18 B 394 GLY HIS TYR ASP GLU GLY GLU GLY PRO ARG ARG GLY MET
SEQRES 19 B 394 LEU THR ALA ARG LYS LEU GLY MET MET THR TYR ARG SER
SEQRES 20 B 394 ALA GLN GLU TRP ASP CYS ARG PHE GLY ARG THR ARG ILE
SEQRES 21 B 394 GLY GLU ARG ARG ARG ALA ASP GLN GLY ARG PHE GLY PRO
SEQRES 22 B 394 GLU PHE GLU VAL GLU SER TYR LEU ASP PHE HIS ALA GLN
SEQRES 23 B 394 ARG PHE ALA ASP ARG PHE ASP PRO ASN SER TYR LEU TYR
SEQRES 24 B 394 LEU SER HIS ALA MET ASP GLN PHE ASP LEU GLY ASP GLY
SEQRES 25 B 394 GLY GLY GLY GLY GLY GLY ALA PRO GLY ALA LEU SER ARG
SEQRES 26 B 394 MET ARG VAL GLU ARG ALA LEU VAL MET GLY ALA ARG THR
SEQRES 27 B 394 ASP ILE LEU PHE PRO LEU SER GLN GLN GLN GLU ILE ALA
SEQRES 28 B 394 ASP GLY LEU SER ALA GLY GLY ALA ASP VAL SER PHE LEU
SEQRES 29 B 394 PRO VAL ASP THR PRO ALA GLY HIS ASP ALA PHE LEU VAL
SEQRES 30 B 394 ASP ILE GLU ARG PHE GLY PRO PRO VAL ALA LYS PHE LEU
SEQRES 31 B 394 ALA ILE VAL ALA
FORMUL 3 HOH *414(H2 O)
HELIX 1 1 TYR A 114 PHE A 118 5 5
HELIX 2 2 SER A 122 LEU A 137 1 16
HELIX 3 3 SER A 149 HIS A 162 1 14
HELIX 4 4 LEU A 179 SER A 195 1 17
HELIX 5 5 TRP A 199 HIS A 203 5 5
HELIX 6 6 PRO A 210 ARG A 226 1 17
HELIX 7 7 SER A 227 GLY A 236 1 10
HELIX 8 8 PHE A 255 ASP A 270 1 16
HELIX 9 9 ASP A 273 PHE A 287 1 15
HELIX 10 10 ASP A 288 GLY A 296 5 9
HELIX 11 11 GLY A 297 MET A 306 1 10
HELIX 12 12 PRO A 323 GLY A 337 1 15
HELIX 13 13 ALA A 350 HIS A 352 5 3
HELIX 14 14 ASP A 353 ASP A 358 1 6
HELIX 15 15 ASP A 358 ALA A 374 1 17
HELIX 16 16 TYR B 114 PHE B 118 5 5
HELIX 17 17 SER B 122 LEU B 137 1 16
HELIX 18 18 SER B 149 HIS B 162 1 14
HELIX 19 19 LEU B 179 SER B 195 1 17
HELIX 20 20 ASP B 196 HIS B 203 5 8
HELIX 21 21 PRO B 210 ARG B 226 1 17
HELIX 22 22 SER B 227 GLY B 236 1 10
HELIX 23 23 PHE B 255 ARG B 271 1 17
HELIX 24 24 ASP B 273 PHE B 287 1 15
HELIX 25 25 GLY B 297 MET B 306 1 10
HELIX 26 26 PRO B 323 GLY B 337 1 15
HELIX 27 27 ALA B 350 HIS B 352 5 3
HELIX 28 28 ASP B 353 ASP B 358 1 6
HELIX 29 29 ASP B 358 ALA B 374 1 17
SHEET 1 A 8 ARG A 10 GLU A 13 0
SHEET 2 A 8 ARG A 30 PHE A 36 -1 O ILE A 31 N ILE A 12
SHEET 3 A 8 HIS A 87 VAL A 91 -1 O VAL A 88 N PHE A 36
SHEET 4 A 8 ALA A 46 LEU A 50 1 N VAL A 47 O ILE A 89
SHEET 5 A 8 CYS A 144 ALA A 148 1 O VAL A 146 N LEU A 48
SHEET 6 A 8 THR A 168 LEU A 172 1 O LEU A 172 N GLY A 147
SHEET 7 A 8 ARG A 310 ALA A 316 1 O LEU A 312 N SER A 171
SHEET 8 A 8 ASP A 340 VAL A 346 1 O VAL A 346 N GLY A 315
SHEET 1 B 2 PHE A 18 ALA A 19 0
SHEET 2 B 2 ALA A 25 LEU A 26 -1 O LEU A 26 N PHE A 18
SHEET 1 C 2 VAL A 75 GLY A 76 0
SHEET 2 C 2 VAL A 81 ASP A 82 1 O VAL A 81 N GLY A 76
SHEET 1 D 8 ARG B 10 GLU B 13 0
SHEET 2 D 8 ARG B 30 PHE B 36 -1 O TYR B 33 N ARG B 10
SHEET 3 D 8 HIS B 87 VAL B 91 -1 O VAL B 88 N PHE B 36
SHEET 4 D 8 ALA B 46 LEU B 50 1 N VAL B 47 O ILE B 89
SHEET 5 D 8 LEU B 142 ALA B 148 1 O VAL B 146 N LEU B 48
SHEET 6 D 8 ALA B 166 LEU B 172 1 O LEU B 172 N GLY B 147
SHEET 7 D 8 ARG B 310 ALA B 316 1 O LEU B 312 N SER B 171
SHEET 8 D 8 ASP B 340 VAL B 346 1 O VAL B 346 N GLY B 315
SHEET 1 E 2 PHE B 18 ALA B 19 0
SHEET 2 E 2 ALA B 25 LEU B 26 -1 O LEU B 26 N PHE B 18
SHEET 1 F 2 VAL B 75 GLY B 76 0
SHEET 2 F 2 VAL B 81 ASP B 82 1 O VAL B 81 N GLY B 76
CRYST1 46.560 102.330 147.300 90.00 90.00 90.00 P 21 21 21 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 0.021478 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006789 0.00000
TER 2786 ALA A 374
TER 5576 ALA B 374
MASTER 314 0 0 29 24 0 0 6 5988 2 0 62
END |