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HEADER HYDROLASE 18-NOV-18 6ISQ
TITLE STRUCTURE OF LIPASE MUTANT WITH OXIDED CYS-HIS-ASP CATALYTIC TRIAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 84753;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CALB, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.X.CEN,J.H.ZHOU,Q.WU
REVDAT 1 24-JUL-19 6ISQ 0
JRNL AUTH M.T.REETZ,J.H.ZHOU,T.S.MOODY,M.L.HUANG,Q.WU,Y.X.CEN,W.SINGH,
JRNL AUTH 2 M.ARKIN
JRNL TITL ARTIFICIAL CYSTEINE-LIPASES WITH HIGH ACTIVITY AND ALTERED
JRNL TITL 2 CATALYTIC MECHANISM CREATED BY LABORATORY EVOLUTION.
JRNL REF NAT COMMUN 2019
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-019-11155-3
REMARK 2
REMARK 2 RESOLUTION. 1.86 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 50329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2554
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 37.0457 - 4.8567 0.99 2770 127 0.1442 0.1693
REMARK 3 2 4.8567 - 3.8562 1.00 2735 132 0.1426 0.1423
REMARK 3 3 3.8562 - 3.3692 1.00 2707 152 0.1456 0.1726
REMARK 3 4 3.3692 - 3.0613 1.00 2727 126 0.1633 0.1922
REMARK 3 5 3.0613 - 2.8419 1.00 2703 161 0.1668 0.1801
REMARK 3 6 2.8419 - 2.6744 1.00 2713 145 0.1649 0.1956
REMARK 3 7 2.6744 - 2.5405 1.00 2700 143 0.1650 0.1712
REMARK 3 8 2.5405 - 2.4300 0.99 2713 153 0.1598 0.2182
REMARK 3 9 2.4300 - 2.3364 1.00 2662 146 0.1635 0.1856
REMARK 3 10 2.3364 - 2.2558 1.00 2731 131 0.1580 0.1716
REMARK 3 11 2.2558 - 2.1853 1.00 2705 139 0.1607 0.2249
REMARK 3 12 2.1853 - 2.1228 1.00 2699 131 0.1609 0.2298
REMARK 3 13 2.1228 - 2.0670 1.00 2716 183 0.1646 0.1968
REMARK 3 14 2.0670 - 2.0165 0.98 2549 151 0.1726 0.2204
REMARK 3 15 2.0165 - 1.9707 0.98 2655 156 0.1976 0.2588
REMARK 3 16 1.9707 - 1.9288 0.95 2619 116 0.1993 0.2442
REMARK 3 17 1.9288 - 1.8902 0.92 2491 145 0.2060 0.2549
REMARK 3 18 1.8902 - 1.8545 0.81 2180 117 0.2165 0.2430
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.750
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 : 0.018 4968
REMARK 3 ANGLE : 1.456 6815
REMARK 3 CHIRALITY : 0.096 780
REMARK 3 PLANARITY : 0.010 901
REMARK 3 DIHEDRAL : 16.098 1794
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 55.3872 0.1516 52.6137
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.1202
REMARK 3 T33: 0.1245 T12: 0.0096
REMARK 3 T13: 0.0160 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.3830 L22: 0.1867
REMARK 3 L33: 0.3420 L12: 0.0895
REMARK 3 L13: 0.1875 L23: 0.0991
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: -0.0069 S13: 0.0051
REMARK 3 S21: 0.0075 S22: -0.0025 S23: 0.0086
REMARK 3 S31: -0.0098 S32: -0.0028 S33: 0.0070
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 6ISQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1300009453.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51204
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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: 1TCA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, PH 6.0 25%
REMARK 280 PEG4000 8% ISOPROPANOL 0.5% N,N-DIMETHYLDODECYLAMINE OXIDE(DDAO),
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 66.18750
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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
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 TOTAL BURIED SURFACE AREA: 240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
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 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 ILE A 285 CG1 CG2 CD1
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 ARG A 302 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 302 NE - CZ - NH2 ANGL. DEV. = -4.5 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 ASN A 51 -92.47 -149.42
REMARK 500 ASP A 75 118.92 -36.16
REMARK 500 CSD A 105 -127.99 51.64
REMARK 500 ASP A 134 67.64 -112.52
REMARK 500 SER A 150 157.54 -39.63
REMARK 500 SER B 29 87.07 -158.22
REMARK 500 ASN B 51 -91.32 -149.68
REMARK 500 ASP B 75 118.47 -37.27
REMARK 500 CSD B 105 -123.57 49.72
REMARK 500 ASP B 134 67.64 -111.53
REMARK 500 PRO B 143 -177.55 -63.74
REMARK 500 ALA B 148 119.90 -29.39
REMARK 500 SER B 150 154.03 -31.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 645 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH B 653 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 654 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B 655 DISTANCE = 6.33 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA B 402
DBREF 6ISQ A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6ISQ B 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQADV 6ISQ GLY A -3 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ ALA A -2 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ ALA A 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6ISQ THR A 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6ISQ VAL A 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6ISQ CSD A 105 UNP P41365 SER 130 ENGINEERED MUTATION
SEQADV 6ISQ GLY A 149 UNP P41365 VAL 174 ENGINEERED MUTATION
SEQADV 6ISQ TYR A 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6ISQ TYR A 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQADV 6ISQ GLY B -3 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ ALA B -2 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 6ISQ ALA B 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6ISQ THR B 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6ISQ VAL B 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6ISQ CSD B 105 UNP P41365 SER 130 ENGINEERED MUTATION
SEQADV 6ISQ GLY B 149 UNP P41365 VAL 174 ENGINEERED MUTATION
SEQADV 6ISQ TYR B 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6ISQ TYR B 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQRES 1 A 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 A 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 A 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 A 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 A 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 A 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 A 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 A 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 A 321 VAL LEU THR VAL CSD GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 A 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 A 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 A 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA GLY SER ALA PRO
SEQRES 13 A 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 A 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 A 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN
SEQRES 16 A 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 A 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 A 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 A 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 A 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 A 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 A 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO TYR TYR
SEQRES 23 A 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 A 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 A 321 ARG THR CYS SER GLY ILE VAL THR PRO
SEQRES 1 B 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 B 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 B 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 B 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 B 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 B 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 B 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 B 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 B 321 VAL LEU THR VAL CSD GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 B 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 B 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 B 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA GLY SER ALA PRO
SEQRES 13 B 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 B 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 B 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN
SEQRES 16 B 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 B 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 B 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 B 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 B 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 B 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 B 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO TYR TYR
SEQRES 23 B 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 B 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 B 321 ARG THR CYS SER GLY ILE VAL THR PRO
MODRES 6ISQ CSD A 105 SER MODIFIED RESIDUE
MODRES 6ISQ CSD B 105 SER MODIFIED RESIDUE
HET CSD A 105 8
HET CSD B 105 8
HET ACT A 401 4
HET IPA A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET PGE A 406 10
HET PGE A 407 10
HET ACT B 401 4
HET IPA B 402 4
HETNAM CSD 3-SULFINOALANINE
HETNAM ACT ACETATE ION
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
HETSYN IPA 2-PROPANOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 IPA 2(C3 H8 O)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 8 PGE 2(C6 H14 O4)
FORMUL 12 HOH *300(H2 O)
HELIX 1 AA1 PRO A 12 GLY A 19 1 8
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 CSD A 105 PHE A 118 1 14
HELIX 6 AA6 PRO A 119 ARG A 122 5 4
HELIX 7 AA7 ALA A 151 GLN A 157 1 7
HELIX 8 AA8 SER A 161 ALA A 170 1 10
HELIX 9 AA9 ALA A 212 GLY A 217 1 6
HELIX 10 AB1 ASP A 223 SER A 230 1 8
HELIX 11 AB2 SER A 230 SER A 243 1 14
HELIX 12 AB3 ARG A 249 TYR A 253 5 5
HELIX 13 AB4 GLY A 254 CYS A 258 5 5
HELIX 14 AB5 THR A 267 ALA A 276 1 10
HELIX 15 AB6 LEU A 278 ILE A 285 5 8
HELIX 16 AB7 ALA A 301 ALA A 305 5 5
HELIX 17 AB8 PRO B 12 GLY B 19 1 8
HELIX 18 AB9 THR B 43 ASP B 49 1 7
HELIX 19 AC1 ASN B 51 LEU B 59 1 9
HELIX 20 AC2 ASP B 75 SER B 94 1 20
HELIX 21 AC3 CSD B 105 PHE B 118 1 14
HELIX 22 AC4 PRO B 119 ARG B 122 5 4
HELIX 23 AC5 PRO B 143 LEU B 147 5 5
HELIX 24 AC6 ALA B 151 GLN B 157 1 7
HELIX 25 AC7 SER B 161 ALA B 170 1 10
HELIX 26 AC8 ALA B 212 GLY B 217 1 6
HELIX 27 AC9 ASP B 223 SER B 230 1 8
HELIX 28 AD1 SER B 230 SER B 243 1 14
HELIX 29 AD2 ARG B 249 TYR B 253 5 5
HELIX 30 AD3 GLY B 254 CYS B 258 5 5
HELIX 31 AD4 THR B 267 ALA B 276 1 10
HELIX 32 AD5 LEU B 278 ILE B 285 5 8
HELIX 33 AD6 ALA B 301 ALA B 305 5 5
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 AA1 7 LEU A 99 VAL A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA3 7 LEU B 20 CYS B 22 0
SHEET 2 AA3 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA3 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 AA3 7 LEU B 99 VAL B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA3 7 VAL B 125 PHE B 131 1 O PHE B 131 N THR B 103
SHEET 6 AA3 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 AA3 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA4 2 ARG B 309 THR B 310 0
SHEET 2 AA4 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.08
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.05
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.12
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.07
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.05
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.11
LINK C VAL A 104 N CSD A 105 1555 1555 1.32
LINK C CSD A 105 N GLN A 106 1555 1555 1.31
LINK C VAL B 104 N CSD B 105 1555 1555 1.32
LINK C CSD B 105 N GLN B 106 1555 1555 1.32
CISPEP 1 PRO A 69 PRO A 70 0 -11.86
CISPEP 2 GLY A 142 PRO A 143 0 16.01
CISPEP 3 GLN A 191 PRO A 192 0 1.54
CISPEP 4 PRO B 69 PRO B 70 0 -12.00
CISPEP 5 GLY B 142 PRO B 143 0 5.31
CISPEP 6 GLN B 191 PRO B 192 0 2.74
SITE 1 AC1 5 THR A 40 CSD A 105 GLN A 157 ILE A 189
SITE 2 AC1 5 IPA A 402
SITE 1 AC2 6 GLY A 39 THR A 40 CSD A 105 HIS A 224
SITE 2 AC2 6 PRO A 280 ACT A 401
SITE 1 AC3 6 LYS A 136 ARG A 168 HOH A 504 HOH A 511
SITE 2 AC3 6 HOH A 621 ASP B 296
SITE 1 AC4 8 MET A -1 THR A 174 GLN A 175 ASN A 206
SITE 2 AC4 8 HOH A 560 ALA B 92 GLY B 95 ASN B 96
SITE 1 AC5 3 ASP A 252 THR A 256 ASP A 257
SITE 1 AC6 2 GLU A 188 ASP A 223
SITE 1 AC7 5 THR B 40 CSD B 105 GLN B 157 ILE B 189
SITE 2 AC7 5 IPA B 402
SITE 1 AC8 8 GLY B 39 THR B 40 VAL B 104 CSD B 105
SITE 2 AC8 8 HIS B 224 PRO B 280 ACT B 401 HOH B 561
CRYST1 44.691 132.375 52.422 90.00 90.04 90.00 P 1 21 1 4
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 0.022376 0.000000 0.000014 0.00000
SCALE2 0.000000 0.007554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019076 0.00000
TER 2403 PRO A 317
TER 4798 PRO B 317
MASTER 335 0 11 33 18 0 14 6 5049 2 80 50
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