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HEADER HYDROLASE 30-JAN-19 6QKW
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -
TITLE 2 TYR219PHE - FLUOROACETATE SOAKED 2HR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 1076;
SOURCE 4 GENE: D1920_22720;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASER, SUBSTRATE INHIBITION, ALLOSTERY, DYNAMICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MEHRABI,T.H.KIM,R.S.PROSSER,E.F.PAI
REVDAT 1 26-JUN-19 6QKW 0
JRNL AUTH P.MEHRABI,C.DI PIETRANTONIO,T.H.KIM,A.SLJOKA,K.TAVERNER,
JRNL AUTH 2 C.ING,N.KRUGLYAK,R.POMES,E.F.PAI,R.S.PROSSER
JRNL TITL SUBSTRATE-BASED ALLOSTERIC REGULATION OF A HOMODIMERIC
JRNL TITL 2 ENZYME.
JRNL REF J.AM.CHEM.SOC. 2019
JRNL REFN ESSN 1520-5126
JRNL PMID 31188575
JRNL DOI 10.1021/JACS.9B03703
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 81991
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4072
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 28.6586 - 4.6391 1.00 2817 149 0.1531 0.1588
REMARK 3 2 4.6391 - 3.6846 1.00 2821 144 0.1289 0.1332
REMARK 3 3 3.6846 - 3.2196 1.00 2750 142 0.1529 0.1858
REMARK 3 4 3.2196 - 2.9255 1.00 2780 151 0.1665 0.1709
REMARK 3 5 2.9255 - 2.7160 1.00 2767 149 0.1741 0.1810
REMARK 3 6 2.7160 - 2.5560 0.99 2724 144 0.1703 0.2336
REMARK 3 7 2.5560 - 2.4281 0.99 2727 142 0.1763 0.2101
REMARK 3 8 2.4281 - 2.3224 0.99 2721 145 0.1684 0.2098
REMARK 3 9 2.3224 - 2.2330 0.97 2686 165 0.1767 0.1955
REMARK 3 10 2.2330 - 2.1560 0.98 2737 143 0.1662 0.2162
REMARK 3 11 2.1560 - 2.0886 0.99 2675 128 0.1709 0.2193
REMARK 3 12 2.0886 - 2.0289 0.98 2723 153 0.1783 0.1970
REMARK 3 13 2.0289 - 1.9755 0.99 2715 146 0.1689 0.1851
REMARK 3 14 1.9755 - 1.9273 0.98 2728 142 0.1732 0.2174
REMARK 3 15 1.9273 - 1.8835 0.98 2676 144 0.1741 0.2012
REMARK 3 16 1.8835 - 1.8435 0.98 2743 122 0.1761 0.1819
REMARK 3 17 1.8435 - 1.8066 0.98 2689 144 0.1737 0.1968
REMARK 3 18 1.8066 - 1.7725 0.98 2718 131 0.1777 0.2087
REMARK 3 19 1.7725 - 1.7409 0.98 2697 145 0.1832 0.2167
REMARK 3 20 1.7409 - 1.7113 0.98 2698 147 0.1814 0.2295
REMARK 3 21 1.7113 - 1.6837 0.99 2685 156 0.1798 0.2054
REMARK 3 22 1.6837 - 1.6578 0.98 2718 133 0.1812 0.2436
REMARK 3 23 1.6578 - 1.6335 0.98 2724 140 0.1877 0.2203
REMARK 3 24 1.6335 - 1.6105 0.98 2653 152 0.1895 0.2609
REMARK 3 25 1.6105 - 1.5887 0.98 2726 135 0.1967 0.2312
REMARK 3 26 1.5887 - 1.5681 0.97 2706 125 0.1997 0.2382
REMARK 3 27 1.5681 - 1.5485 0.97 2622 136 0.2022 0.2341
REMARK 3 28 1.5485 - 1.5298 0.95 2636 139 0.2139 0.2566
REMARK 3 29 1.5298 - 1.5120 0.67 1857 80 0.2114 0.2462
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.590
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 : 0.010 4938
REMARK 3 ANGLE : 1.137 6735
REMARK 3 CHIRALITY : 0.079 685
REMARK 3 PLANARITY : 0.008 889
REMARK 3 DIHEDRAL : 15.785 3948
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 6QKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
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 FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81991
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.512
REMARK 200 RESOLUTION RANGE LOW (A) : 28.653
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG3350, 200 MM CACL2, AND 100
REMARK 280 MM TRIS-HCL PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 39.68500
REMARK 290 SMTRY3 2 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: 2660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 300
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 B 79 CG CD OE1 NE2
REMARK 470 ILE B 153 CG1 CG2 CD1
REMARK 470 ARG B 187 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 277 CG CD OE1 OE2
REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 635 O HOH A 713 2.08
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 VAL A 234 CG1 - CB - CG2 ANGL. DEV. = 10.2 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 ASP A 110 -129.34 56.91
REMARK 500 ASP A 173 67.41 -155.27
REMARK 500 TYR A 224 -100.62 -123.03
REMARK 500 GLN A 255 -75.44 -63.21
REMARK 500 SER A 256 -91.05 50.47
REMARK 500 ALA A 258 116.65 178.55
REMARK 500 ASP B 110 -131.60 57.28
REMARK 500 ILE B 153 40.77 -106.31
REMARK 500 ASP B 173 68.07 -154.06
REMARK 500 TYR B 224 -92.34 -120.87
REMARK 500 SER B 256 -144.97 -158.80
REMARK 500 ALA B 257 -110.59 -49.19
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAH B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAH B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOA B 403
DBREF1 6QKW A 1 302 UNP A0A397K2D3_RHOPL
DBREF2 6QKW A A0A397K2D3 1 302
DBREF1 6QKW B 1 302 UNP A0A397K2D3_RHOPL
DBREF2 6QKW B A0A397K2D3 1 302
SEQADV 6QKW GLY A -1 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW HIS A 0 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW LYS A 90 UNP A0A397K2D GLN 90 CONFLICT
SEQADV 6QKW ILE A 204 UNP A0A397K2D LEU 204 CONFLICT
SEQADV 6QKW PHE A 219 UNP A0A397K2D TYR 219 ENGINEERED MUTATION
SEQADV 6QKW ILE A 232 UNP A0A397K2D VAL 232 CONFLICT
SEQADV 6QKW THR A 290 UNP A0A397K2D ILE 290 CONFLICT
SEQADV 6QKW ARG A 296 UNP A0A397K2D LYS 296 CONFLICT
SEQADV 6QKW ALA A 300 UNP A0A397K2D VAL 300 CONFLICT
SEQADV 6QKW GLY A 303 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW SER A 304 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW GLY B -1 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW HIS B 0 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW LYS B 90 UNP A0A397K2D GLN 90 CONFLICT
SEQADV 6QKW ILE B 204 UNP A0A397K2D LEU 204 CONFLICT
SEQADV 6QKW PHE B 219 UNP A0A397K2D TYR 219 ENGINEERED MUTATION
SEQADV 6QKW ILE B 232 UNP A0A397K2D VAL 232 CONFLICT
SEQADV 6QKW THR B 290 UNP A0A397K2D ILE 290 CONFLICT
SEQADV 6QKW ARG B 296 UNP A0A397K2D LYS 296 CONFLICT
SEQADV 6QKW ALA B 300 UNP A0A397K2D VAL 300 CONFLICT
SEQADV 6QKW GLY B 303 UNP A0A397K2D EXPRESSION TAG
SEQADV 6QKW SER B 304 UNP A0A397K2D EXPRESSION TAG
SEQRES 1 A 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 A 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 A 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 A 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 A 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 A 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 A 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 A 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 A 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 A 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 A 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 A 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 A 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 A 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 A 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 A 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP PHE
SEQRES 18 A 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 A 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 A 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 A 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 A 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 A 306 PHE SER ALA ALA PRO GLY SER
SEQRES 1 B 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 B 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 B 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 B 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 B 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 B 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 B 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 B 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 B 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 B 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 B 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 B 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 B 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 B 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 B 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 B 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP PHE
SEQRES 18 B 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 B 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 B 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 B 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 B 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 B 306 PHE SER ALA ALA PRO GLY SER
HET CL A 401 1
HET FAH B 401 5
HET FAH B 402 5
HET GOA B 403 5
HETNAM CL CHLORIDE ION
HETNAM FAH FLUOROACETIC ACID
HETNAM GOA GLYCOLIC ACID
HETSYN GOA HYDROXYACETIC ACID; HYDROXYETHANOIC ACID
FORMUL 3 CL CL 1-
FORMUL 4 FAH 2(C2 H3 F O2)
FORMUL 6 GOA C2 H4 O3
FORMUL 7 HOH *652(H2 O)
HELIX 1 AA1 THR A 43 HIS A 48 5 6
HELIX 2 AA2 VAL A 50 GLU A 56 1 7
HELIX 3 AA3 HIS A 80 TYR A 83 5 4
HELIX 4 AA4 THR A 84 LEU A 99 1 16
HELIX 5 AA5 ASP A 110 SER A 123 1 14
HELIX 6 AA6 PRO A 137 ARG A 144 1 8
HELIX 7 AA7 ASN A 146 ILE A 153 1 8
HELIX 8 AA8 TYR A 154 LEU A 159 1 6
HELIX 9 AA9 PRO A 164 GLY A 171 1 8
HELIX 10 AB1 ASP A 173 TRP A 185 1 13
HELIX 11 AB2 ASP A 195 ALA A 207 1 13
HELIX 12 AB3 ASP A 208 TYR A 224 1 17
HELIX 13 AB4 TYR A 224 GLY A 237 1 14
HELIX 14 AB5 THR A 259 LYS A 266 1 8
HELIX 15 AB6 PHE A 281 ALA A 286 1 6
HELIX 16 AB7 ALA A 286 ALA A 300 1 15
HELIX 17 AB8 THR B 43 HIS B 48 5 6
HELIX 18 AB9 VAL B 50 GLU B 56 1 7
HELIX 19 AC1 HIS B 80 TYR B 83 5 4
HELIX 20 AC2 THR B 84 LEU B 99 1 16
HELIX 21 AC3 ASP B 110 SER B 123 1 14
HELIX 22 AC4 PRO B 137 ARG B 144 1 8
HELIX 23 AC5 ASN B 146 ILE B 153 1 8
HELIX 24 AC6 TYR B 154 LEU B 159 1 6
HELIX 25 AC7 PRO B 164 GLY B 171 1 8
HELIX 26 AC8 ASP B 173 SER B 184 1 12
HELIX 27 AC9 ASP B 195 ALA B 207 1 13
HELIX 28 AD1 ASP B 208 TYR B 224 1 17
HELIX 29 AD2 TYR B 224 GLY B 237 1 14
HELIX 30 AD3 THR B 259 LYS B 266 1 8
HELIX 31 AD4 PHE B 281 ALA B 286 1 6
HELIX 32 AD5 ALA B 286 SER B 299 1 14
SHEET 1 AA1 8 GLY A 12 ILE A 16 0
SHEET 2 AA1 8 ILE A 23 GLY A 29 -1 O ILE A 23 N ILE A 16
SHEET 3 AA1 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N LEU A 34 O ILE A 61
SHEET 5 AA1 8 PHE A 104 HIS A 109 1 O ALA A 105 N LEU A 35
SHEET 6 AA1 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 AA1 8 MET A 244 GLY A 249 1 O LEU A 247 N VAL A 132
SHEET 8 AA1 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
SHEET 1 AA2 8 GLY B 12 ILE B 16 0
SHEET 2 AA2 8 ILE B 23 GLY B 29 -1 O VAL B 27 N GLY B 12
SHEET 3 AA2 8 LYS B 59 ALA B 63 -1 O VAL B 62 N ARG B 26
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N LEU B 34 O LYS B 59
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
SHEET 6 AA2 8 LEU B 127 LEU B 133 1 O ALA B 131 N LEU B 106
SHEET 7 AA2 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O ILE B 276 N TRP B 248
CISPEP 1 PHE A 40 PRO A 41 0 -2.94
CISPEP 2 ALA A 163 PRO A 164 0 4.10
CISPEP 3 PHE B 40 PRO B 41 0 -5.52
CISPEP 4 ALA B 163 PRO B 164 0 7.02
SITE 1 AC1 5 ASP A 110 ARG A 111 ARG A 114 HOH A 713
SITE 2 AC1 5 HOH A 723
SITE 1 AC2 6 ASP B 110 ARG B 111 ARG B 114 TRP B 156
SITE 2 AC2 6 TRP B 185 GOA B 403
SITE 1 AC3 8 ASP B 134 TYR B 141 LYS B 152 TRP B 185
SITE 2 AC3 8 GLY B 252 ILE B 253 HIS B 280 HOH B 600
SITE 1 AC4 7 ASP B 110 ARG B 111 ARG B 114 ILE B 135
SITE 2 AC4 7 TRP B 156 HIS B 280 FAH B 401
CRYST1 41.750 79.370 85.010 90.00 103.01 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 0.023952 0.000000 0.005533 0.00000
SCALE2 0.000000 0.012599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012073 0.00000
TER 2409 ALA A 300
TER 4763 SER B 299
MASTER 323 0 4 32 16 0 8 6 5350 2 15 48
END |