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HEADER HYDROLASE 10-MAR-16 5IQ0
TITLE CRYSTAL STRUCTURE OF ESTERASE MUTANT - F72G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, EST25, HORMONE-SENSITIVE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-H.SEOK,M.-D.SEO,J.KIM,Y.RYU
REVDAT 1 22-MAR-17 5IQ0 0
JRNL AUTH S.-H.SEOK,M.-D.SEO,J.KIM,Y.RYU
JRNL TITL CRYSTAL STRUCTURE OF ESTERASE MUTANT - F72G
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 167868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.190
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 36.1743 - 4.3338 0.94 11434 138 0.1629 0.1875
REMARK 3 2 4.3338 - 3.4408 0.99 11893 143 0.1460 0.1664
REMARK 3 3 3.4408 - 3.0061 1.00 11915 144 0.1687 0.1844
REMARK 3 4 3.0061 - 2.7313 1.00 11960 144 0.1930 0.2164
REMARK 3 5 2.7313 - 2.5356 1.00 11907 144 0.1888 0.2348
REMARK 3 6 2.5356 - 2.3861 1.00 11903 144 0.1892 0.1974
REMARK 3 7 2.3861 - 2.2667 1.00 11887 142 0.1783 0.1996
REMARK 3 8 2.2667 - 2.1680 1.00 11895 144 0.1839 0.1998
REMARK 3 9 2.1680 - 2.0846 1.00 11899 143 0.1864 0.2101
REMARK 3 10 2.0846 - 2.0126 1.00 11857 143 0.1946 0.1950
REMARK 3 11 2.0126 - 1.9497 1.00 11846 143 0.1969 0.2304
REMARK 3 12 1.9497 - 1.8940 1.00 11930 145 0.2010 0.2268
REMARK 3 13 1.8940 - 1.8441 1.00 11860 143 0.2122 0.2101
REMARK 3 14 1.8441 - 1.7991 0.98 11682 140 0.2238 0.2640
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.320
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 10817
REMARK 3 ANGLE : 1.023 14767
REMARK 3 CHIRALITY : 0.060 1656
REMARK 3 PLANARITY : 0.007 1958
REMARK 3 DIHEDRAL : 12.320 6443
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 5IQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218756.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 167878
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.799
REMARK 200 RESOLUTION RANGE LOW (A) : 36.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 44.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 1JKM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE (PH 7.0),
REMARK 280 MICROBATCH, TEMPERATURE 299K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 98.12400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.81850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 98.12400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.81850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 LEU B 6
REMARK 465 ASN B 7
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ASN C 3
REMARK 465 ALA C 4
REMARK 465 THR C 5
REMARK 465 LEU C 6
REMARK 465 ASN C 7
REMARK 465 GLN C 8
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ASN D 3
REMARK 465 ALA D 4
REMARK 465 THR D 5
REMARK 465 LEU D 6
REMARK 465 ASN D 7
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN D 8 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 SD MET A 74 CE MET D 74 4455 1.54
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 LYS A 318 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 LYS A 318 CB - CG - CD ANGL. DEV. = 20.0 DEGREES
REMARK 500 LYS A 318 CG - CD - CE ANGL. DEV. = -18.9 DEGREES
REMARK 500 LYS A 318 CD - CE - NZ ANGL. DEV. = 15.4 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 4 -167.21 -113.94
REMARK 500 LEU A 131 158.62 81.66
REMARK 500 SER A 201 -118.98 63.33
REMARK 500 CYS A 230 61.03 25.11
REMARK 500 PHE A 254 -50.78 75.79
REMARK 500 LEU A 302 42.63 -99.74
REMARK 500 ALA A 334 18.54 59.09
REMARK 500 SER A 338 -41.63 -136.50
REMARK 500 LEU B 131 159.55 81.66
REMARK 500 SER B 201 -120.31 62.08
REMARK 500 CYS B 230 60.96 24.01
REMARK 500 PHE B 254 -50.12 70.71
REMARK 500 LEU B 302 40.33 -101.01
REMARK 500 SER B 338 -41.86 -136.37
REMARK 500 LEU C 131 158.63 80.26
REMARK 500 SER C 201 -121.37 62.67
REMARK 500 CYS C 230 60.92 24.15
REMARK 500 LYS C 240 71.12 48.81
REMARK 500 PHE C 254 -52.16 77.05
REMARK 500 LEU C 302 42.71 -100.74
REMARK 500 SER C 338 -40.25 -138.25
REMARK 500 LEU D 131 158.34 80.39
REMARK 500 SER D 201 -119.77 61.72
REMARK 500 CYS D 230 61.02 24.28
REMARK 500 PHE D 254 -56.28 76.56
REMARK 500 LEU D 302 42.88 -100.56
REMARK 500 SER D 338 -40.95 -137.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLN C 78 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IQ2 RELATED DB: PDB
REMARK 900 RELATED ID: 5IQ3 RELATED DB: PDB
DBREF 5IQ0 A 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
DBREF 5IQ0 B 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
DBREF 5IQ0 C 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
DBREF 5IQ0 D 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
SEQADV 5IQ0 GLY A 72 UNP Q4TZQ3 PHE 72 ENGINEERED MUTATION
SEQADV 5IQ0 GLY B 72 UNP Q4TZQ3 PHE 72 ENGINEERED MUTATION
SEQADV 5IQ0 GLY C 72 UNP Q4TZQ3 PHE 72 ENGINEERED MUTATION
SEQADV 5IQ0 GLY D 72 UNP Q4TZQ3 PHE 72 ENGINEERED MUTATION
SEQRES 1 A 362 MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU
SEQRES 2 A 362 GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR
SEQRES 3 A 362 ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU
SEQRES 4 A 362 ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER
SEQRES 5 A 362 GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU
SEQRES 6 A 362 GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN
SEQRES 7 A 362 GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR
SEQRES 8 A 362 ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE
SEQRES 9 A 362 HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU
SEQRES 10 A 362 PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE
SEQRES 11 A 362 LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER
SEQRES 12 A 362 GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU
SEQRES 13 A 362 PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE
SEQRES 14 A 362 PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP
SEQRES 15 A 362 VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU
SEQRES 16 A 362 ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU
SEQRES 17 A 362 ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU
SEQRES 18 A 362 GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER
SEQRES 19 A 362 GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU
SEQRES 20 A 362 LEU GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET
SEQRES 21 A 362 GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN
SEQRES 22 A 362 ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU
SEQRES 23 A 362 GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL
SEQRES 24 A 362 ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS
SEQRES 25 A 362 TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY
SEQRES 26 A 362 ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER
SEQRES 27 A 362 PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL
SEQRES 28 A 362 ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA
SEQRES 1 B 362 MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU
SEQRES 2 B 362 GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR
SEQRES 3 B 362 ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU
SEQRES 4 B 362 ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER
SEQRES 5 B 362 GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU
SEQRES 6 B 362 GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN
SEQRES 7 B 362 GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR
SEQRES 8 B 362 ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE
SEQRES 9 B 362 HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU
SEQRES 10 B 362 PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE
SEQRES 11 B 362 LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER
SEQRES 12 B 362 GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU
SEQRES 13 B 362 PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE
SEQRES 14 B 362 PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP
SEQRES 15 B 362 VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU
SEQRES 16 B 362 ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU
SEQRES 17 B 362 ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU
SEQRES 18 B 362 GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER
SEQRES 19 B 362 GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU
SEQRES 20 B 362 LEU GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET
SEQRES 21 B 362 GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN
SEQRES 22 B 362 ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU
SEQRES 23 B 362 GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL
SEQRES 24 B 362 ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS
SEQRES 25 B 362 TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY
SEQRES 26 B 362 ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER
SEQRES 27 B 362 PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL
SEQRES 28 B 362 ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA
SEQRES 1 C 362 MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU
SEQRES 2 C 362 GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR
SEQRES 3 C 362 ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU
SEQRES 4 C 362 ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER
SEQRES 5 C 362 GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU
SEQRES 6 C 362 GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN
SEQRES 7 C 362 GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR
SEQRES 8 C 362 ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE
SEQRES 9 C 362 HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU
SEQRES 10 C 362 PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE
SEQRES 11 C 362 LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER
SEQRES 12 C 362 GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU
SEQRES 13 C 362 PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE
SEQRES 14 C 362 PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP
SEQRES 15 C 362 VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU
SEQRES 16 C 362 ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU
SEQRES 17 C 362 ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU
SEQRES 18 C 362 GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER
SEQRES 19 C 362 GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU
SEQRES 20 C 362 LEU GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET
SEQRES 21 C 362 GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN
SEQRES 22 C 362 ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU
SEQRES 23 C 362 GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL
SEQRES 24 C 362 ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS
SEQRES 25 C 362 TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY
SEQRES 26 C 362 ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER
SEQRES 27 C 362 PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL
SEQRES 28 C 362 ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA
SEQRES 1 D 362 MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU
SEQRES 2 D 362 GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR
SEQRES 3 D 362 ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU
SEQRES 4 D 362 ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER
SEQRES 5 D 362 GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU
SEQRES 6 D 362 GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN
SEQRES 7 D 362 GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR
SEQRES 8 D 362 ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE
SEQRES 9 D 362 HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU
SEQRES 10 D 362 PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE
SEQRES 11 D 362 LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER
SEQRES 12 D 362 GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU
SEQRES 13 D 362 PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE
SEQRES 14 D 362 PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP
SEQRES 15 D 362 VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU
SEQRES 16 D 362 ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU
SEQRES 17 D 362 ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU
SEQRES 18 D 362 GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER
SEQRES 19 D 362 GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU
SEQRES 20 D 362 LEU GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET
SEQRES 21 D 362 GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN
SEQRES 22 D 362 ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU
SEQRES 23 D 362 GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL
SEQRES 24 D 362 ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS
SEQRES 25 D 362 TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY
SEQRES 26 D 362 ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER
SEQRES 27 D 362 PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL
SEQRES 28 D 362 ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA
FORMUL 5 HOH *946(H2 O)
HELIX 1 AA1 PRO A 10 ASP A 15 1 6
HELIX 2 AA2 ASP A 27 LEU A 37 1 11
HELIX 3 AA3 GLU A 53 SER A 77 1 25
HELIX 4 AA4 ASP A 135 THR A 148 1 14
HELIX 5 AA5 ALA A 161 GLY A 165 5 5
HELIX 6 AA6 PRO A 170 SER A 185 1 16
HELIX 7 AA7 ASN A 186 GLY A 191 1 6
HELIX 8 AA8 SER A 201 GLY A 218 1 18
HELIX 9 AA9 TRP A 219 ILE A 223 5 5
HELIX 10 AB1 PRO A 245 ASN A 250 1 6
HELIX 11 AB2 ASP A 256 ASP A 268 1 13
HELIX 12 AB3 TRP A 280 ALA A 284 5 5
HELIX 13 AB4 SER A 285 ALA A 290 1 6
HELIX 14 AB5 LEU A 305 ALA A 319 1 15
HELIX 15 AB6 ALA A 334 SER A 338 5 5
HELIX 16 AB7 ILE A 343 ALA A 362 1 20
HELIX 17 AB8 PRO B 10 ASP B 15 1 6
HELIX 18 AB9 ASP B 27 LEU B 37 1 11
HELIX 19 AC1 GLU B 53 SER B 77 1 25
HELIX 20 AC2 ASP B 135 THR B 148 1 14
HELIX 21 AC3 ALA B 161 GLY B 165 5 5
HELIX 22 AC4 PRO B 170 SER B 185 1 16
HELIX 23 AC5 ASN B 186 GLY B 191 1 6
HELIX 24 AC6 SER B 201 GLU B 217 1 17
HELIX 25 AC7 TRP B 219 ILE B 223 5 5
HELIX 26 AC8 PRO B 245 ASN B 250 1 6
HELIX 27 AC9 ASP B 256 ASP B 268 1 13
HELIX 28 AD1 TRP B 280 ALA B 284 5 5
HELIX 29 AD2 SER B 285 ALA B 290 1 6
HELIX 30 AD3 LEU B 305 ALA B 319 1 15
HELIX 31 AD4 ALA B 334 SER B 338 5 5
HELIX 32 AD5 ILE B 343 ALA B 362 1 20
HELIX 33 AD6 PRO C 10 GLY C 14 5 5
HELIX 34 AD7 ASP C 27 LEU C 37 1 11
HELIX 35 AD8 GLU C 53 SER C 77 1 25
HELIX 36 AD9 ASP C 135 THR C 148 1 14
HELIX 37 AE1 ALA C 161 GLY C 165 5 5
HELIX 38 AE2 PRO C 170 SER C 185 1 16
HELIX 39 AE3 ASN C 186 GLY C 191 1 6
HELIX 40 AE4 SER C 201 GLU C 217 1 17
HELIX 41 AE5 TRP C 219 ILE C 223 5 5
HELIX 42 AE6 PRO C 245 ASN C 250 1 6
HELIX 43 AE7 ASP C 256 ASP C 268 1 13
HELIX 44 AE8 TRP C 280 ALA C 284 5 5
HELIX 45 AE9 SER C 285 ALA C 290 1 6
HELIX 46 AF1 LEU C 305 ALA C 319 1 15
HELIX 47 AF2 ALA C 334 SER C 338 5 5
HELIX 48 AF3 ILE C 343 ALA C 362 1 20
HELIX 49 AF4 PRO D 10 ASP D 15 1 6
HELIX 50 AF5 ASP D 27 LEU D 37 1 11
HELIX 51 AF6 GLU D 53 SER D 77 1 25
HELIX 52 AF7 ASP D 135 THR D 148 1 14
HELIX 53 AF8 ALA D 161 GLY D 165 5 5
HELIX 54 AF9 PRO D 170 SER D 185 1 16
HELIX 55 AG1 ASN D 186 GLY D 191 1 6
HELIX 56 AG2 SER D 201 GLY D 218 1 18
HELIX 57 AG3 TRP D 219 ILE D 223 5 5
HELIX 58 AG4 PRO D 245 ASN D 250 1 6
HELIX 59 AG5 ASP D 256 ASP D 268 1 13
HELIX 60 AG6 TRP D 280 ALA D 284 5 5
HELIX 61 AG7 SER D 285 ALA D 290 1 6
HELIX 62 AG8 LEU D 305 ALA D 319 1 15
HELIX 63 AG9 ALA D 334 SER D 338 5 5
HELIX 64 AH1 ILE D 343 ALA D 362 1 20
SHEET 1 AA116 VAL A 85 LYS A 93 0
SHEET 2 AA116 GLU A 99 PRO A 107 -1 O ILE A 104 N ARG A 88
SHEET 3 AA116 VAL A 151 GLU A 156 -1 O GLY A 154 N TYR A 103
SHEET 4 AA116 LEU A 117 THR A 123 1 N VAL A 120 O VAL A 153
SHEET 5 AA116 ILE A 192 GLU A 200 1 O ILE A 196 N VAL A 121
SHEET 6 AA116 GLY A 225 GLN A 229 1 O GLN A 229 N GLY A 199
SHEET 7 AA116 HIS A 295 LEU A 302 1 O VAL A 296 N ALA A 228
SHEET 8 AA116 THR A 323 CYS A 332 1 O ARG A 326 N VAL A 299
SHEET 9 AA116 THR B 323 CYS B 332 -1 O GLY B 325 N HIS A 329
SHEET 10 AA116 HIS B 295 LEU B 302 1 N VAL B 299 O VAL B 328
SHEET 11 AA116 GLY B 225 GLN B 229 1 N ALA B 228 O VAL B 296
SHEET 12 AA116 ILE B 192 GLU B 200 1 N GLY B 199 O GLN B 229
SHEET 13 AA116 LEU B 117 THR B 123 1 N VAL B 121 O ILE B 196
SHEET 14 AA116 VAL B 151 GLU B 156 1 O VAL B 153 N VAL B 120
SHEET 15 AA116 GLU B 99 PRO B 107 -1 N TYR B 103 O GLY B 154
SHEET 16 AA116 VAL B 85 LYS B 93 -1 N GLU B 90 O LEU B 102
SHEET 1 AA216 VAL C 85 LYS C 93 0
SHEET 2 AA216 GLU C 99 PRO C 107 -1 O LEU C 102 N GLU C 90
SHEET 3 AA216 VAL C 151 GLU C 156 -1 O GLY C 154 N TYR C 103
SHEET 4 AA216 LEU C 117 THR C 123 1 N VAL C 120 O VAL C 153
SHEET 5 AA216 ILE C 192 GLU C 200 1 O ILE C 196 N VAL C 121
SHEET 6 AA216 GLY C 225 GLN C 229 1 O GLN C 229 N GLY C 199
SHEET 7 AA216 HIS C 295 LEU C 302 1 O VAL C 296 N ALA C 228
SHEET 8 AA216 THR C 323 CYS C 332 1 O ARG C 326 N VAL C 299
SHEET 9 AA216 THR D 323 CYS D 332 -1 O GLY D 325 N HIS C 329
SHEET 10 AA216 HIS D 295 LEU D 302 1 N VAL D 299 O VAL D 328
SHEET 11 AA216 GLY D 225 GLN D 229 1 N ALA D 228 O VAL D 296
SHEET 12 AA216 ILE D 192 GLU D 200 1 N GLY D 199 O GLN D 229
SHEET 13 AA216 LEU D 117 THR D 123 1 N VAL D 121 O ILE D 196
SHEET 14 AA216 VAL D 151 GLU D 156 1 O VAL D 153 N VAL D 120
SHEET 15 AA216 GLU D 99 PRO D 107 -1 N TYR D 103 O GLY D 154
SHEET 16 AA216 VAL D 85 LYS D 93 -1 N GLU D 90 O LEU D 102
SSBOND 1 MET A 74 MET D 74 1555 4455 2.00
LINK CE MET A 74 SD MET D 74 1555 4455 1.90
CISPEP 1 GLY A 165 ASN A 166 0 -0.36
CISPEP 2 PHE A 169 PRO A 170 0 6.80
CISPEP 3 GLY B 165 ASN B 166 0 -0.71
CISPEP 4 PHE B 169 PRO B 170 0 6.48
CISPEP 5 GLY C 165 ASN C 166 0 -0.24
CISPEP 6 PHE C 169 PRO C 170 0 6.43
CISPEP 7 GLY D 165 ASN D 166 0 -0.29
CISPEP 8 PHE D 169 PRO D 170 0 6.58
CRYST1 196.248 95.637 99.135 90.00 95.51 90.00 C 1 2 1 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 0.005096 0.000000 0.000491 0.00000
SCALE2 0.000000 0.010456 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010134 0.00000
TER 2684 ALA A 362
TER 5318 ALA B 362
TER 7943 ALA C 362
TER 10573 ALA D 362
MASTER 358 0 0 64 32 0 0 611515 4 0 112
END |