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HEADER HYDROLASE 07-JAN-13 4IO0
TITLE CRYSTAL STRUCTURE OF F128A MUTANT OF AN EPOXIDE HYDROLASE FROM
TITLE 2 BACILLUS MEGATERIUM COMPLEXED WITH ITS PRODUCT (R)-3-[1]NAPHTHYLOXY-
TITLE 3 PROPANE-1,2-DIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.2.2.10;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 STRAIN: ECU1001;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS A/B HYDROLASE FOLD, EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.D.KONG,J.H.ZHOU,J.H.XU
REVDAT 1 12-FEB-14 4IO0 0
JRNL AUTH X.D.KONG,J.H.ZHOU,J.H.XU
JRNL TITL CRYSTAL STRUCTURE OF F128A MUTANT OF AN EPOXIDE HYDROLASE
JRNL TITL 2 FROM BACILLUS MEGATERIUM COMPLEXED WITH ITS PRODUCT
JRNL TITL 3 (R)-3-[1]NAPHTHYLOXY-PROPANE-1,2-DIOL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_637)
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 15898
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 804
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 45.2559 - 5.2676 0.99 2752 122 0.1733 0.2174
REMARK 3 2 5.2676 - 4.1820 0.99 2580 136 0.1165 0.1785
REMARK 3 3 4.1820 - 3.6537 0.98 2524 132 0.1235 0.1939
REMARK 3 4 3.6537 - 3.3197 0.97 2489 131 0.1606 0.2581
REMARK 3 5 3.3197 - 3.0818 0.95 2442 129 0.2022 0.2986
REMARK 3 6 3.0818 - 2.9002 0.92 2307 154 0.2171 0.3205
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 22.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.520
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) : -0.33440
REMARK 3 B22 (A**2) : -0.33440
REMARK 3 B33 (A**2) : 0.66880
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 : 0.008 4912
REMARK 3 ANGLE : 1.117 6666
REMARK 3 CHIRALITY : 0.075 681
REMARK 3 PLANARITY : 0.004 870
REMARK 3 DIHEDRAL : 16.365 1810
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 4IO0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB076991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121961
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.22100
REMARK 200 R SYM (I) : 0.22100
REMARK 200 FOR THE DATA SET : 8.3370
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.79000
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: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4G00
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 2.0 M (NH4)2SO4, 0.2 M
REMARK 280 LI2SO4, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 58.74800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.82000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.37400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.82000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.82000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 88.12200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.82000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.82000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.37400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.82000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.82000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 88.12200
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 58.74800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 MET A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
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 PRO A 31 50.75 -105.50
REMARK 500 ASP A 32 -150.89 -100.33
REMARK 500 SER A 34 -35.41 -34.06
REMARK 500 ASN A 59 -115.65 43.85
REMARK 500 GLU A 62 152.10 -45.25
REMARK 500 ASP A 97 -132.64 59.75
REMARK 500 TYR A 110 51.15 -141.49
REMARK 500 PHE A 148 -4.09 -59.26
REMARK 500 LYS A 207 68.54 -100.93
REMARK 500 ASN A 256 20.59 82.39
REMARK 500 SER A 266 -136.84 -111.87
REMARK 500 ALA A 268 67.88 -114.22
REMARK 500 ASN B 9 35.65 36.52
REMARK 500 LYS B 18 114.05 -173.82
REMARK 500 PRO B 31 53.18 -101.65
REMARK 500 ASP B 32 -146.00 -101.06
REMARK 500 PHE B 33 -173.44 178.72
REMARK 500 ASN B 59 -124.59 58.43
REMARK 500 LYS B 63 66.03 -113.94
REMARK 500 ASP B 97 -120.17 59.12
REMARK 500 ASP B 160 65.49 61.65
REMARK 500 LYS B 207 76.12 -103.63
REMARK 500 SER B 266 -118.40 -122.10
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 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RN1 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RN1 B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G00 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WILD TYPE ENZYME
REMARK 900 RELATED ID: 4G02 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WILD TYPE ENZYME COMPLEXED WITH A
REMARK 900 SUBSTRATE ANALOGUE
REMARK 900 RELATED ID: 4INZ RELATED DB: PDB
DBREF 4IO0 A 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
DBREF 4IO0 B 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
SEQADV 4IO0 GLY A -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 SER A -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 HIS A -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 MET A -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 ALA A -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 SER A -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 MET A -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 THR A -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY A -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY A -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLN A -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLN A -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 MET A -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY A -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 ARG A -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY A -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 SER A 0 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 ALA A 128 UNP G9BEX6 PHE 128 ENGINEERED MUTATION
SEQADV 4IO0 GLY B -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 SER B -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 HIS B -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 MET B -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 ALA B -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 SER B -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 MET B -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 THR B -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY B -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY B -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLN B -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLN B -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 MET B -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY B -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 ARG B -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 GLY B -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 SER B 0 UNP G9BEX6 EXPRESSION TAG
SEQADV 4IO0 ALA B 128 UNP G9BEX6 PHE 128 ENGINEERED MUTATION
SEQRES 1 A 304 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 A 304 GLY ARG GLY SER MET SER LYS GLN TYR ILE ASN VAL ASN
SEQRES 3 A 304 GLY VAL ASN LEU HIS TYR ILE SER LYS GLY GLN GLY GLU
SEQRES 4 A 304 LEU MET LEU PHE LEU HIS GLY PHE PRO ASP PHE SER HIS
SEQRES 5 A 304 ILE TRP ARG HIS GLN ILE ASP GLU PHE SER ASN ASP PHE
SEQRES 6 A 304 HIS THR VAL ALA LEU ASP LEU ARG GLY TYR ASN LEU SER
SEQRES 7 A 304 GLU LYS PRO SER GLY LEU GLU SER TYR GLU ILE ASP VAL
SEQRES 8 A 304 LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU GLY LEU GLY
SEQRES 9 A 304 TYR SER SER CYS THR LEU VAL VAL HIS ASP TRP GLY ALA
SEQRES 10 A 304 GLY ILE GLY TRP THR PHE ALA TYR ARG TYR PRO GLU TYR
SEQRES 11 A 304 VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO HIS PRO TYR
SEQRES 12 A 304 THR ALA MET ARG GLU LEU ARG THR ASN LYS ASN GLN GLN
SEQRES 13 A 304 LYS ALA SER GLU TYR MET LYS TRP PHE GLN LYS GLN GLU
SEQRES 14 A 304 VAL GLN ASP TYR MET GLU ARG ASP ASN PHE SER GLY LEU
SEQRES 15 A 304 ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS LYS GLY TYR
SEQRES 16 A 304 LEU THR ALA ASP ASP VAL GLN ALA TYR MET ASN SER TRP
SEQRES 17 A 304 GLU ASN GLY SER VAL LEU SER MET LEU SER TYR TYR ARG
SEQRES 18 A 304 ASN LEU LYS ILE PHE THR GLU GLU ASP LEU ARG ARG LYS
SEQRES 19 A 304 SER LEU PHE PRO LEU GLU GLU GLU VAL LEU ASN ILE PRO
SEQRES 20 A 304 VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO THR PHE MET
SEQRES 21 A 304 PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR VAL PRO ASN
SEQRES 22 A 304 ILE SER VAL HIS ARG LEU ALA GLU ALA SER HIS ALA PRO
SEQRES 23 A 304 GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN VAL MET TRP
SEQRES 24 A 304 ASN PHE LEU ASN LYS
SEQRES 1 B 304 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 B 304 GLY ARG GLY SER MET SER LYS GLN TYR ILE ASN VAL ASN
SEQRES 3 B 304 GLY VAL ASN LEU HIS TYR ILE SER LYS GLY GLN GLY GLU
SEQRES 4 B 304 LEU MET LEU PHE LEU HIS GLY PHE PRO ASP PHE SER HIS
SEQRES 5 B 304 ILE TRP ARG HIS GLN ILE ASP GLU PHE SER ASN ASP PHE
SEQRES 6 B 304 HIS THR VAL ALA LEU ASP LEU ARG GLY TYR ASN LEU SER
SEQRES 7 B 304 GLU LYS PRO SER GLY LEU GLU SER TYR GLU ILE ASP VAL
SEQRES 8 B 304 LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU GLY LEU GLY
SEQRES 9 B 304 TYR SER SER CYS THR LEU VAL VAL HIS ASP TRP GLY ALA
SEQRES 10 B 304 GLY ILE GLY TRP THR PHE ALA TYR ARG TYR PRO GLU TYR
SEQRES 11 B 304 VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO HIS PRO TYR
SEQRES 12 B 304 THR ALA MET ARG GLU LEU ARG THR ASN LYS ASN GLN GLN
SEQRES 13 B 304 LYS ALA SER GLU TYR MET LYS TRP PHE GLN LYS GLN GLU
SEQRES 14 B 304 VAL GLN ASP TYR MET GLU ARG ASP ASN PHE SER GLY LEU
SEQRES 15 B 304 ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS LYS GLY TYR
SEQRES 16 B 304 LEU THR ALA ASP ASP VAL GLN ALA TYR MET ASN SER TRP
SEQRES 17 B 304 GLU ASN GLY SER VAL LEU SER MET LEU SER TYR TYR ARG
SEQRES 18 B 304 ASN LEU LYS ILE PHE THR GLU GLU ASP LEU ARG ARG LYS
SEQRES 19 B 304 SER LEU PHE PRO LEU GLU GLU GLU VAL LEU ASN ILE PRO
SEQRES 20 B 304 VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO THR PHE MET
SEQRES 21 B 304 PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR VAL PRO ASN
SEQRES 22 B 304 ILE SER VAL HIS ARG LEU ALA GLU ALA SER HIS ALA PRO
SEQRES 23 B 304 GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN VAL MET TRP
SEQRES 24 B 304 ASN PHE LEU ASN LYS
HET SO4 A 301 5
HET RN1 A 302 16
HET SO4 B 301 5
HET RN1 B 302 16
HETNAM SO4 SULFATE ION
HETNAM RN1 (2R)-3-(NAPHTHALEN-1-YLOXY)PROPANE-1,2-DIOL
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 RN1 2(C13 H14 O3)
FORMUL 7 HOH *100(H2 O)
HELIX 1 1 PHE A 33 ILE A 36 5 4
HELIX 2 2 TRP A 37 SER A 45 1 9
HELIX 3 3 GLY A 66 TYR A 70 5 5
HELIX 4 4 GLU A 71 LEU A 86 1 16
HELIX 5 5 ASP A 97 TYR A 110 1 14
HELIX 6 6 TYR A 126 ASN A 135 1 10
HELIX 7 7 ASN A 135 PHE A 148 1 14
HELIX 8 8 GLN A 149 GLN A 151 5 3
HELIX 9 9 GLU A 152 LYS A 176 1 25
HELIX 10 10 THR A 180 GLY A 194 1 15
HELIX 11 11 SER A 195 TYR A 202 1 8
HELIX 12 12 TYR A 203 LEU A 206 5 4
HELIX 13 13 THR A 210 ARG A 215 1 6
HELIX 14 14 MET A 243 ASP A 248 5 6
HELIX 15 15 GLY A 249 TYR A 253 5 5
HELIX 16 16 ALA A 268 LYS A 273 1 6
HELIX 17 17 LYS A 273 LYS A 287 1 15
HELIX 18 18 PHE B 33 ILE B 36 5 4
HELIX 19 19 TRP B 37 SER B 45 1 9
HELIX 20 20 GLY B 66 TYR B 70 5 5
HELIX 21 21 GLU B 71 LEU B 86 1 16
HELIX 22 22 ASP B 97 TYR B 110 1 14
HELIX 23 23 TYR B 126 ASN B 135 1 10
HELIX 24 24 ASN B 135 PHE B 148 1 14
HELIX 25 25 LYS B 150 LYS B 176 1 27
HELIX 26 26 THR B 180 GLY B 194 1 15
HELIX 27 27 SER B 195 TYR B 202 1 8
HELIX 28 28 TYR B 203 LEU B 206 5 4
HELIX 29 29 THR B 210 ARG B 215 1 6
HELIX 30 30 MET B 243 ASP B 248 5 6
HELIX 31 31 GLY B 249 TYR B 253 5 5
HELIX 32 32 ALA B 268 LYS B 273 1 6
HELIX 33 33 LYS B 273 LYS B 287 1 15
SHEET 1 A 8 SER A 2 VAL A 8 0
SHEET 2 A 8 VAL A 11 LYS A 18 -1 O SER A 17 N SER A 2
SHEET 3 A 8 HIS A 49 LEU A 53 -1 O ALA A 52 N ILE A 16
SHEET 4 A 8 LEU A 23 LEU A 27 1 N MET A 24 O VAL A 51
SHEET 5 A 8 CYS A 91 VAL A 95 1 O VAL A 94 N LEU A 25
SHEET 6 A 8 VAL A 114 ALA A 119 1 O ILE A 118 N VAL A 95
SHEET 7 A 8 VAL A 231 GLY A 236 1 O GLN A 232 N ALA A 119
SHEET 8 A 8 ILE A 257 LEU A 262 1 O HIS A 260 N ILE A 233
SHEET 1 B 8 TYR B 5 VAL B 8 0
SHEET 2 B 8 VAL B 11 GLY B 19 -1 O LEU B 13 N ILE B 6
SHEET 3 B 8 HIS B 49 LEU B 53 -1 O ALA B 52 N ILE B 16
SHEET 4 B 8 LEU B 23 LEU B 27 1 N PHE B 26 O VAL B 51
SHEET 5 B 8 CYS B 91 VAL B 95 1 O VAL B 94 N LEU B 27
SHEET 6 B 8 VAL B 114 ALA B 119 1 O GLN B 115 N CYS B 91
SHEET 7 B 8 VAL B 231 GLY B 236 1 O GLN B 232 N LEU B 117
SHEET 8 B 8 ILE B 257 LEU B 262 1 O SER B 258 N VAL B 231
CISPEP 1 PHE A 30 PRO A 31 0 -10.04
CISPEP 2 PHE B 30 PRO B 31 0 -5.02
SITE 1 AC1 6 GLU A 272 LYS A 273 PRO A 274 GLN A 275
SITE 2 AC1 6 GLU A 276 ASN B 161
SITE 1 AC2 10 ASP A 97 TRP A 98 ALA A 128 LEU A 132
SITE 2 AC2 10 GLN A 138 SER A 142 TYR A 144 MET A 145
SITE 3 AC2 10 LEU A 206 PHE A 242
SITE 1 AC3 4 LYS B 273 PRO B 274 GLN B 275 GLU B 276
SITE 1 AC4 8 ASP B 97 TRP B 98 ALA B 128 SER B 142
SITE 2 AC4 8 TYR B 144 LEU B 219 PHE B 242 ASN B 246
CRYST1 109.640 109.640 117.496 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 0.009121 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008511 0.00000
TER 2381 LYS A 287
TER 4739 LYS B 287
MASTER 328 0 4 33 16 0 8 6 4861 2 42 48
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