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HEADER HYDROLASE 28-JUN-12 4FTW
TITLE CRYSTAL STRUCTURE OF A CARBOXYL ESTERASE N110C/L145H AT 2.3 ANGSTROM
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE/CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 272943;
SOURCE 4 STRAIN: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
SOURCE 5 GENE: CGMCC1.1737, RHOS4_13150, RSP_2728;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-30A
KEYWDS ALPHA/BETA HYDROLASE SUPERFAMILY, ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.WU,J.MA,J.ZHOU,H.YU
REVDAT 1 03-OCT-12 4FTW 0
JRNL AUTH J.MA,L.WU,F.GUO,J.GU,X.TANG,L.JIANG,J.LIU,J.ZHOU,H.YU
JRNL TITL ENHANCED ENANTIOSELECTIVITY OF A CARBOXYL ESTERASE FROM
JRNL TITL 2 RHODOBACTER SPHAEROIDES BY DIRECTED EVOLUTION.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2012
JRNL REFN ESSN 1432-0614
JRNL PMID 22987200
JRNL DOI 10.1007/S00253-012-4396-2
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 15208
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 757
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.6737 - 3.9312 0.89 2746 121 0.2367 0.2784
REMARK 3 2 3.9312 - 3.1205 0.98 2930 146 0.2211 0.3225
REMARK 3 3 3.1205 - 2.7261 1.00 2936 173 0.2506 0.2926
REMARK 3 4 2.7261 - 2.4768 1.00 2947 151 0.2666 0.3259
REMARK 3 5 2.4768 - 2.3000 1.00 2892 166 0.2851 0.3260
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.49
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 72.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.89100
REMARK 3 B22 (A**2) : -7.89100
REMARK 3 B33 (A**2) : 15.78210
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1699
REMARK 3 ANGLE : 1.219 2314
REMARK 3 CHIRALITY : 0.077 255
REMARK 3 PLANARITY : 0.004 302
REMARK 3 DIHEDRAL : 18.158 672
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 2012
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15208
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08800
REMARK 200 FOR THE DATA SET : 20.5380
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 : 10.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER MR
REMARK 200 STARTING MODEL: PDB ENTRY 4FHZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M NA-TARTRATE, 34.5MM CYMAL-3, 0.1M
REMARK 280 PIPES , PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 15.85633
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.71267
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.71267
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 15.85633
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: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 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 MET A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 VAL A 12
REMARK 465 PRO A 13
REMARK 465 ARG A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 GLY A 17
REMARK 465 MET A 18
REMARK 465 LYS A 19
REMARK 465 GLU A 20
REMARK 465 THR A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 LYS A 25
REMARK 465 PHE A 26
REMARK 465 GLU A 27
REMARK 465 ARG A 28
REMARK 465 GLN A 29
REMARK 465 HIS A 30
REMARK 465 MET A 31
REMARK 465 ASP A 32
REMARK 465 SER A 33
REMARK 465 PRO A 34
REMARK 465 ASP A 35
REMARK 465 LEU A 36
REMARK 465 GLY A 37
REMARK 465 THR A 38
REMARK 465 ASP A 39
REMARK 465 ASP A 40
REMARK 465 ASP A 41
REMARK 465 ASP A 42
REMARK 465 LYS A 43
REMARK 465 ALA A 44
REMARK 465 MET A 45
REMARK 465 ALA A 46
REMARK 465 ASP A 47
REMARK 465 ASP A 268
REMARK 465 ALA A 269
REMARK 465 CYS A 270
REMARK 465 GLY A 271
REMARK 465 ARG A 272
REMARK 465 THR A 273
REMARK 465 ARG A 274
REMARK 465 ALA A 275
REMARK 465 PRO A 276
REMARK 465 PRO A 277
REMARK 465 PRO A 278
REMARK 465 PRO A 279
REMARK 465 PRO A 280
REMARK 465 LEU A 281
REMARK 465 ARG A 282
REMARK 465 SER A 283
REMARK 465 GLY A 284
REMARK 465 CYS A 285
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 107 CB CYS A 107 SG -0.097
REMARK 500 CYS A 110 CB CYS A 110 SG -0.151
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER A 165 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 SER A 189 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 77 -156.55 -100.36
REMARK 500 SER A 165 -98.26 80.48
REMARK 500 SER A 189 54.58 39.90
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 PIN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3CM A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FHZ RELATED DB: PDB
DBREF 4FTW A 49 268 UNP Q3J2V1 Q3J2V1_RHOS4 1 220
SEQADV 4FTW MET A 1 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 2 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 3 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 4 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 5 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 6 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 7 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW SER A 8 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW SER A 9 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLY A 10 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW LEU A 11 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW VAL A 12 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 13 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ARG A 14 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLY A 15 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW SER A 16 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLY A 17 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW MET A 18 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW LYS A 19 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLU A 20 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW THR A 21 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ALA A 22 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ALA A 23 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ALA A 24 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW LYS A 25 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PHE A 26 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLU A 27 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ARG A 28 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLN A 29 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW HIS A 30 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW MET A 31 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 32 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW SER A 33 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 34 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 35 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW LEU A 36 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLY A 37 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW THR A 38 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 39 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 40 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 41 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 42 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW LYS A 43 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ALA A 44 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW MET A 45 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ALA A 46 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ASP A 47 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ILE A 48 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW CYS A 110 UNP Q3J2V1 ASN 62 ENGINEERED MUTATION
SEQADV 4FTW HIS A 145 UNP Q3J2V1 LEU 97 ENGINEERED MUTATION
SEQADV 4FTW ALA A 269 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW CYS A 270 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLY A 271 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ARG A 272 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW THR A 273 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ARG A 274 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ALA A 275 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 276 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 277 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 278 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 279 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW PRO A 280 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW LEU A 281 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW ARG A 282 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW SER A 283 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW GLY A 284 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FTW CYS A 285 UNP Q3J2V1 EXPRESSION TAG
SEQRES 1 A 285 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 285 ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES 3 A 285 GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES 4 A 285 ASP ASP ASP LYS ALA MET ALA ASP ILE MET THR ARG LYS
SEQRES 5 A 285 LEU THR PHE GLY ARG ARG GLY ALA ALA PRO GLY GLU ALA
SEQRES 6 A 285 THR SER LEU VAL VAL PHE LEU HIS GLY TYR GLY ALA ASP
SEQRES 7 A 285 GLY ALA ASP LEU LEU GLY LEU ALA GLU PRO LEU ALA PRO
SEQRES 8 A 285 HIS LEU PRO GLY THR ALA PHE VAL ALA PRO ASP ALA PRO
SEQRES 9 A 285 GLU PRO CYS ARG ALA CYS GLY PHE GLY PHE GLN TRP PHE
SEQRES 10 A 285 PRO ILE PRO TRP LEU ASP GLY SER SER GLU THR ALA ALA
SEQRES 11 A 285 ALA GLU GLY MET ALA ALA ALA ALA ARG ASP LEU ASP ALA
SEQRES 12 A 285 PHE HIS ASP GLU ARG LEU ALA GLU GLU GLY LEU PRO PRO
SEQRES 13 A 285 GLU ALA LEU ALA LEU VAL GLY PHE SER GLN GLY THR MET
SEQRES 14 A 285 MET ALA LEU HIS VAL ALA PRO ARG ARG ALA GLU GLU ILE
SEQRES 15 A 285 ALA GLY ILE VAL GLY PHE SER GLY ARG LEU LEU ALA PRO
SEQRES 16 A 285 GLU ARG LEU ALA GLU GLU ALA ARG SER LYS PRO PRO VAL
SEQRES 17 A 285 LEU LEU VAL HIS GLY ASP ALA ASP PRO VAL VAL PRO PHE
SEQRES 18 A 285 ALA ASP MET SER LEU ALA GLY GLU ALA LEU ALA GLU ALA
SEQRES 19 A 285 GLY PHE THR THR TYR GLY HIS VAL MET LYS GLY THR GLY
SEQRES 20 A 285 HIS GLY ILE ALA PRO ASP GLY LEU SER VAL ALA LEU ALA
SEQRES 21 A 285 PHE LEU LYS GLU ARG LEU PRO ASP ALA CYS GLY ARG THR
SEQRES 22 A 285 ARG ALA PRO PRO PRO PRO PRO LEU ARG SER GLY CYS
HET PIN A 301 18
HET 3CM A 302 32
HET NA A 303 1
HET CL A 304 1
HETNAM PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)
HETNAM 3CM 3-CYCLOHEXYLPROPYL 4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-
HETNAM 2 3CM GLUCOPYRANOSIDE
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETSYN PIN PIPES; 1,4-PIPERAZINEDIETHANESULFONIC ACID
HETSYN 3CM CYMAL-3
FORMUL 2 PIN C8 H18 N2 O6 S2
FORMUL 3 3CM C21 H38 O11
FORMUL 4 NA NA 1+
FORMUL 5 CL CL 1-
FORMUL 6 HOH *22(H2 O)
HELIX 1 1 ASP A 78 GLY A 84 1 7
HELIX 2 2 LEU A 85 ALA A 90 1 6
HELIX 3 3 PRO A 91 LEU A 93 5 3
HELIX 4 4 ILE A 119 GLY A 124 1 6
HELIX 5 5 SER A 126 GLU A 152 1 27
HELIX 6 6 PRO A 155 GLU A 157 5 3
HELIX 7 7 SER A 165 ALA A 175 1 11
HELIX 8 8 PRO A 176 ARG A 178 5 3
HELIX 9 9 ALA A 194 GLU A 196 5 3
HELIX 10 10 ARG A 197 ALA A 202 1 6
HELIX 11 11 PHE A 221 ALA A 234 1 14
HELIX 12 12 ALA A 251 LEU A 266 1 16
SHEET 1 A 7 PHE A 55 GLY A 59 0
SHEET 2 A 7 THR A 96 PRO A 101 -1 O PHE A 98 N ARG A 58
SHEET 3 A 7 SER A 67 LEU A 72 1 N PHE A 71 O VAL A 99
SHEET 4 A 7 LEU A 159 PHE A 164 1 O VAL A 162 N VAL A 70
SHEET 5 A 7 GLY A 184 PHE A 188 1 O VAL A 186 N LEU A 161
SHEET 6 A 7 VAL A 208 GLY A 213 1 O LEU A 209 N ILE A 185
SHEET 7 A 7 THR A 238 MET A 243 1 O TYR A 239 N VAL A 208
SHEET 1 B 2 GLU A 105 PRO A 106 0
SHEET 2 B 2 PHE A 114 GLN A 115 -1 O GLN A 115 N GLU A 105
SSBOND 1 CYS A 107 CYS A 110 1555 1555 2.28
CISPEP 1 ARG A 58 GLY A 59 0 -14.72
CISPEP 2 SER A 189 GLY A 190 0 25.69
SITE 1 AC1 6 TYR A 75 GLY A 76 PHE A 112 LEU A 122
SITE 2 AC1 6 SER A 256 3CM A 302
SITE 1 AC2 7 ASP A 81 LEU A 122 PHE A 164 VAL A 218
SITE 2 AC2 7 HIS A 248 GLY A 249 PIN A 301
CRYST1 112.382 112.382 47.569 90.00 90.00 120.00 P 31 2 1 6
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 0.008898 0.005137 0.000000 0.00000
SCALE2 0.000000 0.010275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021022 0.00000
TER 1612 PRO A 267
MASTER 352 0 4 12 9 0 4 6 1685 1 52 22
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