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HEADER HYDROLASE 08-AUG-16 5SWN
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -
TITLE 2 ASP110ASN/FLUOROACETATE - COCRYSTALLIZED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98
SOURCE 3 / CGA009);
SOURCE 4 ORGANISM_TAXID: 258594;
SOURCE 5 STRAIN: ATCC BAA-98 / CGA009;
SOURCE 6 GENE: RPA1163;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HOMODIMER, HYDROLASE, DEHALOGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MEHRABI,T.H.KIM,S.R.PROSSER,E.F.PAI
REVDAT 1 01-FEB-17 5SWN 0
JRNL AUTH T.H.KIM,P.MEHRABI,Z.REN,A.SLJOKA,C.ING,A.BEZGINOV,L.YE,
JRNL AUTH 2 R.POMES,R.S.PROSSER,E.F.PAI
JRNL TITL THE ROLE OF DIMER ASYMMETRY AND PROTOMER DYNAMICS IN ENZYME
JRNL TITL 2 CATALYSIS.
JRNL REF SCIENCE V. 355 2017
JRNL REFN ESSN 1095-9203
JRNL PMID 28104837
JRNL DOI 10.1126/SCIENCE.AAG2355
REMARK 2
REMARK 2 RESOLUTION. 1.54 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) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 78560
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 : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 3896
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 40.7909 - 4.6770 0.96 2644 133 0.1553 0.1689
REMARK 3 2 4.6770 - 3.7131 0.99 2708 145 0.1284 0.1183
REMARK 3 3 3.7131 - 3.2440 1.00 2730 126 0.1505 0.1766
REMARK 3 4 3.2440 - 2.9474 1.00 2698 144 0.1666 0.1702
REMARK 3 5 2.9474 - 2.7362 1.00 2708 141 0.1757 0.1926
REMARK 3 6 2.7362 - 2.5749 1.00 2700 133 0.1718 0.2147
REMARK 3 7 2.5749 - 2.4460 1.00 2664 146 0.1644 0.1935
REMARK 3 8 2.4460 - 2.3395 1.00 2686 146 0.1620 0.1769
REMARK 3 9 2.3395 - 2.2495 1.00 2712 131 0.1672 0.2017
REMARK 3 10 2.2495 - 2.1719 1.00 2690 140 0.1615 0.1820
REMARK 3 11 2.1719 - 2.1040 1.00 2671 146 0.1687 0.1852
REMARK 3 12 2.1040 - 2.0438 1.00 2709 147 0.1748 0.2104
REMARK 3 13 2.0438 - 1.9900 1.00 2643 137 0.1716 0.1834
REMARK 3 14 1.9900 - 1.9415 1.00 2706 133 0.1716 0.2089
REMARK 3 15 1.9415 - 1.8973 1.00 2657 148 0.1778 0.2108
REMARK 3 16 1.8973 - 1.8570 1.00 2722 133 0.1790 0.2395
REMARK 3 17 1.8570 - 1.8198 1.00 2641 140 0.1776 0.2232
REMARK 3 18 1.8198 - 1.7855 1.00 2728 139 0.1816 0.1945
REMARK 3 19 1.7855 - 1.7536 1.00 2645 142 0.1782 0.2404
REMARK 3 20 1.7536 - 1.7239 1.00 2684 143 0.1833 0.2047
REMARK 3 21 1.7239 - 1.6960 1.00 2704 135 0.1794 0.2544
REMARK 3 22 1.6960 - 1.6699 1.00 2664 143 0.1920 0.2182
REMARK 3 23 1.6699 - 1.6454 1.00 2695 136 0.1897 0.2424
REMARK 3 24 1.6454 - 1.6222 1.00 2647 147 0.1954 0.2307
REMARK 3 25 1.6222 - 1.6003 1.00 2652 158 0.2031 0.2439
REMARK 3 26 1.6003 - 1.5795 1.00 2716 144 0.2132 0.2807
REMARK 3 27 1.5795 - 1.5598 0.96 2493 134 0.2785 0.3057
REMARK 3 28 1.5598 - 1.5410 0.87 2347 106 0.2985 0.3450
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) : 19.440
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 4845
REMARK 3 ANGLE : 0.961 6595
REMARK 3 CHIRALITY : 0.055 678
REMARK 3 PLANARITY : 0.006 863
REMARK 3 DIHEDRAL : 22.897 2840
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 5SWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 FR-D
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78560
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 40.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03400
REMARK 200 FOR THE DATA SET : 30.7000
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: PHASER
REMARK 200 STARTING MODEL: 3R3U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL PH 8.5 AND 200 MM
REMARK 280 CACL2 AND 19-22% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 39.43500
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: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 ALA A 257
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 GLU A 78 CG CD OE1 OE2
REMARK 470 GLU B 78 CG CD OE1 OE2
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 OH TYR B 149 O HOH B 501 2.09
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 PRO A 41 62.48 -101.07
REMARK 500 ASN A 110 -133.54 59.95
REMARK 500 ASP A 173 65.74 -152.64
REMARK 500 TYR A 224 -97.87 -121.92
REMARK 500 PRO B 41 63.64 -100.95
REMARK 500 ASN B 110 -130.44 56.86
REMARK 500 ILE B 153 53.03 -113.20
REMARK 500 TYR B 224 -92.79 -123.70
REMARK 500 GLU B 277 92.43 -66.43
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 FAH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
DBREF 5SWN A 4 300 UNP Q6NAM1 DEHA_RHOPA 4 300
DBREF 5SWN B 4 300 UNP Q6NAM1 DEHA_RHOPA 4 300
SEQADV 5SWN ASN A 110 UNP Q6NAM1 ASP 110 ENGINEERED MUTATION
SEQADV 5SWN ASN B 110 UNP Q6NAM1 ASP 110 ENGINEERED MUTATION
SEQRES 1 A 297 LEU ALA ASP LEU PHE PRO GLY PHE GLY SER GLU TRP ILE
SEQRES 2 A 297 ASN THR SER SER GLY ARG ILE PHE ALA ARG VAL GLY GLY
SEQRES 3 A 297 ASP GLY PRO PRO LEU LEU LEU LEU HIS GLY PHE PRO GLN
SEQRES 4 A 297 THR HIS VAL MET TRP HIS ARG VAL ALA PRO LYS LEU ALA
SEQRES 5 A 297 GLU ARG PHE LYS VAL ILE VAL ALA ASP LEU PRO GLY TYR
SEQRES 6 A 297 GLY TRP SER ASP MET PRO GLU SER ASP GLU GLN HIS THR
SEQRES 7 A 297 PRO TYR THR LYS ARG ALA MET ALA LYS GLN LEU ILE GLU
SEQRES 8 A 297 ALA MET GLU GLN LEU GLY HIS VAL HIS PHE ALA LEU ALA
SEQRES 9 A 297 GLY HIS ASN ARG GLY ALA ARG VAL SER TYR ARG LEU ALA
SEQRES 10 A 297 LEU ASP SER PRO GLY ARG LEU SER LYS LEU ALA VAL LEU
SEQRES 11 A 297 ASP ILE LEU PRO THR TYR GLU TYR TRP GLN ARG MET ASN
SEQRES 12 A 297 ARG ALA TYR ALA LEU LYS ILE TYR HIS TRP SER PHE LEU
SEQRES 13 A 297 ALA GLN PRO ALA PRO LEU PRO GLU ASN LEU LEU GLY GLY
SEQRES 14 A 297 ASP PRO ASP PHE TYR VAL LYS ALA LYS LEU ALA SER TRP
SEQRES 15 A 297 THR ARG ALA GLY ASP LEU SER ALA PHE ASP PRO ARG ALA
SEQRES 16 A 297 VAL GLU HIS TYR ARG ILE ALA PHE ALA ASP PRO MET ARG
SEQRES 17 A 297 ARG HIS VAL MET CYS GLU ASP TYR ARG ALA GLY ALA TYR
SEQRES 18 A 297 ALA ASP PHE GLU HIS ASP LYS ILE ASP VAL GLU ALA GLY
SEQRES 19 A 297 ASN LYS ILE PRO VAL PRO MET LEU ALA LEU TRP GLY ALA
SEQRES 20 A 297 SER GLY ILE ALA GLN SER ALA ALA THR PRO LEU ASP VAL
SEQRES 21 A 297 TRP ARG LYS TRP ALA SER ASP VAL GLN GLY ALA PRO ILE
SEQRES 22 A 297 GLU SER GLY HIS PHE LEU PRO GLU GLU ALA PRO ASP GLN
SEQRES 23 A 297 THR ALA GLU ALA LEU VAL ARG PHE PHE SER ALA
SEQRES 1 B 297 LEU ALA ASP LEU PHE PRO GLY PHE GLY SER GLU TRP ILE
SEQRES 2 B 297 ASN THR SER SER GLY ARG ILE PHE ALA ARG VAL GLY GLY
SEQRES 3 B 297 ASP GLY PRO PRO LEU LEU LEU LEU HIS GLY PHE PRO GLN
SEQRES 4 B 297 THR HIS VAL MET TRP HIS ARG VAL ALA PRO LYS LEU ALA
SEQRES 5 B 297 GLU ARG PHE LYS VAL ILE VAL ALA ASP LEU PRO GLY TYR
SEQRES 6 B 297 GLY TRP SER ASP MET PRO GLU SER ASP GLU GLN HIS THR
SEQRES 7 B 297 PRO TYR THR LYS ARG ALA MET ALA LYS GLN LEU ILE GLU
SEQRES 8 B 297 ALA MET GLU GLN LEU GLY HIS VAL HIS PHE ALA LEU ALA
SEQRES 9 B 297 GLY HIS ASN ARG GLY ALA ARG VAL SER TYR ARG LEU ALA
SEQRES 10 B 297 LEU ASP SER PRO GLY ARG LEU SER LYS LEU ALA VAL LEU
SEQRES 11 B 297 ASP ILE LEU PRO THR TYR GLU TYR TRP GLN ARG MET ASN
SEQRES 12 B 297 ARG ALA TYR ALA LEU LYS ILE TYR HIS TRP SER PHE LEU
SEQRES 13 B 297 ALA GLN PRO ALA PRO LEU PRO GLU ASN LEU LEU GLY GLY
SEQRES 14 B 297 ASP PRO ASP PHE TYR VAL LYS ALA LYS LEU ALA SER TRP
SEQRES 15 B 297 THR ARG ALA GLY ASP LEU SER ALA PHE ASP PRO ARG ALA
SEQRES 16 B 297 VAL GLU HIS TYR ARG ILE ALA PHE ALA ASP PRO MET ARG
SEQRES 17 B 297 ARG HIS VAL MET CYS GLU ASP TYR ARG ALA GLY ALA TYR
SEQRES 18 B 297 ALA ASP PHE GLU HIS ASP LYS ILE ASP VAL GLU ALA GLY
SEQRES 19 B 297 ASN LYS ILE PRO VAL PRO MET LEU ALA LEU TRP GLY ALA
SEQRES 20 B 297 SER GLY ILE ALA GLN SER ALA ALA THR PRO LEU ASP VAL
SEQRES 21 B 297 TRP ARG LYS TRP ALA SER ASP VAL GLN GLY ALA PRO ILE
SEQRES 22 B 297 GLU SER GLY HIS PHE LEU PRO GLU GLU ALA PRO ASP GLN
SEQRES 23 B 297 THR ALA GLU ALA LEU VAL ARG PHE PHE SER ALA
HET FAH A 401 5
HET CL A 402 1
HET CL B 401 1
HETNAM FAH FLUOROACETIC ACID
HETNAM CL CHLORIDE ION
FORMUL 3 FAH C2 H3 F O2
FORMUL 4 CL 2(CL 1-)
FORMUL 6 HOH *530(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 ASN 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 ALA B 55 1 6
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 ASN 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 TRP B 185 1 13
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 ALA B 300 1 15
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 LYS A 59
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 245 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 60 N GLY B 28
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 LEU B 130
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 -2.05
CISPEP 2 ALA A 163 PRO A 164 0 3.15
CISPEP 3 PHE B 40 PRO B 41 0 -1.82
CISPEP 4 ALA B 163 PRO B 164 0 4.84
SITE 1 AC1 6 ASN A 110 ARG A 111 ARG A 114 HIS A 155
SITE 2 AC1 6 TRP A 156 TYR A 219
SITE 1 AC2 4 ARG A 114 LEU A 136 HOH A 536 HOH A 616
SITE 1 AC3 3 ASN B 110 ARG B 114 HOH B 622
CRYST1 41.880 78.870 84.900 90.00 103.18 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 0.023878 0.000000 0.005592 0.00000
SCALE2 0.000000 0.012679 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012097 0.00000
TER 2340 ALA A 300
TER 4691 ALA B 300
MASTER 277 0 3 32 16 0 4 6 5220 2 5 46
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