HEADER TRANSFERASE 19-FEB-13 4JAQ
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PKS11 REVEALS
TITLE 2 INTERMEDIATES IN THE SYNTHESIS OF METHYL-BRANCHED ALKYLPYRONES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-PYRONE SYNTHESIS POLYKETIDE SYNTHASE-LIKE PKS11;
COMPND 3 CHAIN: D, A, C, B;
COMPND 4 SYNONYM: ALPHA-PYRONE SYNTHESIS POLYKETIDE SYNTHASE TYPE III PKS11,
COMPND 5 CHALCONE SYNTHASE-LIKE PROTEIN, CHS-LIKE;
COMPND 6 EC: 2.3.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: PKS11, RV1665, MT1705;
SOURCE 6 EXPRESSION_SYSTEM: MYCOBACTERIUM SMEGMATIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1772;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: DEST17
KEYWDS LIPID BIOSYNTHESIS, STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE,
KEYWDS 2 KETOSYNTHASE ENZYME, ALKYLPYRONE SYNTHESIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.GOKULAN,J.C.SACCHETTINI,MYCOBACTERIUM TUBERCULOSIS STRUCTURAL
AUTHOR 2 PROTEOMICS PROJECT (XMTB)
REVDAT 2 27-NOV-13 4JAQ 1 JRNL
REVDAT 1 24-APR-13 4JAQ 0
JRNL AUTH K.GOKULAN,S.E.O'LEARY,W.K.RUSSELL,D.H.RUSSELL,M.LALGONDAR,
JRNL AUTH 2 T.P.BEGLEY,T.R.IOERGER,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS POLYKETIDE
JRNL TITL 2 SYNTHASE 11 (PKS11) REVEALS INTERMEDIATES IN THE SYNTHESIS
JRNL TITL 3 OF METHYL-BRANCHED ALKYLPYRONES.
JRNL REF J.BIOL.CHEM. V. 288 16484 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23615910
JRNL DOI 10.1074/JBC.M113.468892
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 3 NUMBER OF REFLECTIONS : 125850
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 6346
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 48.1329 - 5.3714 1.00 4679 226 0.1880 0.2156
REMARK 3 2 5.3714 - 4.2643 1.00 4564 226 0.1555 0.1878
REMARK 3 3 4.2643 - 3.7255 1.00 4465 248 0.1545 0.1955
REMARK 3 4 3.7255 - 3.3849 0.99 4485 213 0.1725 0.1917
REMARK 3 5 3.3849 - 3.1424 0.99 4443 250 0.1801 0.1902
REMARK 3 6 3.1424 - 2.9571 0.99 4382 237 0.1839 0.2214
REMARK 3 7 2.9571 - 2.8091 0.98 4350 241 0.1843 0.2313
REMARK 3 8 2.8091 - 2.6868 0.97 4285 250 0.1885 0.2164
REMARK 3 9 2.6868 - 2.5834 0.95 4219 238 0.1829 0.2391
REMARK 3 10 2.5834 - 2.4942 0.95 4241 218 0.1844 0.2303
REMARK 3 11 2.4942 - 2.4162 0.93 4087 234 0.1848 0.2371
REMARK 3 12 2.4162 - 2.3472 0.92 4120 226 0.1737 0.2270
REMARK 3 13 2.3472 - 2.2854 0.91 4029 219 0.1772 0.2330
REMARK 3 14 2.2854 - 2.2296 0.90 3934 207 0.1836 0.2397
REMARK 3 15 2.2296 - 2.1789 0.88 3946 196 0.1784 0.2276
REMARK 3 16 2.1789 - 2.1326 0.87 3882 203 0.1797 0.1985
REMARK 3 17 2.1326 - 2.0899 0.87 3867 187 0.1701 0.2166
REMARK 3 18 2.0899 - 2.0505 0.86 3768 209 0.1744 0.2234
REMARK 3 19 2.0505 - 2.0138 0.85 3787 189 0.1825 0.2108
REMARK 3 20 2.0138 - 1.9797 0.85 3726 214 0.1836 0.2291
REMARK 3 21 1.9797 - 1.9478 0.86 3736 204 0.1905 0.2529
REMARK 3 22 1.9478 - 1.9178 0.83 3719 219 0.1933 0.2502
REMARK 3 23 1.9178 - 1.8896 0.84 3663 196 0.1991 0.2428
REMARK 3 24 1.8896 - 1.8630 0.84 3744 186 0.2052 0.2480
REMARK 3 25 1.8630 - 1.8378 0.83 3628 199 0.2171 0.2592
REMARK 3 26 1.8378 - 1.8139 0.84 3698 180 0.2238 0.2595
REMARK 3 27 1.8139 - 1.7913 0.82 3654 196 0.2402 0.2977
REMARK 3 28 1.7913 - 1.7697 0.82 3614 174 0.2557 0.3108
REMARK 3 29 1.7697 - 1.7491 0.80 3522 203 0.2800 0.3490
REMARK 3 30 1.7491 - 1.7300 0.74 3267 158 0.2947 0.3182
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 35.86
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.010
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) : 0.73260
REMARK 3 B22 (A**2) : 0.08120
REMARK 3 B33 (A**2) : -0.81380
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.41280
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 : 0.006 10960
REMARK 3 ANGLE : 1.277 14921
REMARK 3 CHIRALITY : 0.083 1738
REMARK 3 PLANARITY : 0.005 1934
REMARK 3 DIHEDRAL : 12.380 4024
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 4JAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHICS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140395
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.650
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> 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: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM TARTRATE DIBASIC, 20%
REMARK 280 W/V POLYETHYLENE GLYCOL 3350, PH 6.6, VAPOR DIFFUSION, SITTING
REMARK 280 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 24.35600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C
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: 5130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 MET D 1
REMARK 465 MET A 1
REMARK 465 MET C 1
REMARK 465 MET B 1
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 LEU D 167 70.08 -110.95
REMARK 500 PRO D 177 46.97 -73.02
REMARK 500 SER D 312 -131.43 48.40
REMARK 500 ARG D 327 75.19 49.33
REMARK 500 LEU A 167 71.15 -112.15
REMARK 500 SER A 312 -127.42 47.05
REMARK 500 ARG A 327 80.78 51.72
REMARK 500 LEU C 167 71.96 -110.80
REMARK 500 SER C 312 -130.35 50.55
REMARK 500 ARG C 327 90.51 54.11
REMARK 500 LEU B 167 71.49 -112.06
REMARK 500 PRO B 177 47.47 -77.40
REMARK 500 SER B 312 -134.23 51.32
REMARK 500 ARG B 327 82.89 51.80
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 693 DISTANCE = 5.13 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PLM C 402
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 14V D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 14V A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JAO RELATED DB: PDB
REMARK 900 RELATED ID: 4JAP RELATED DB: PDB
REMARK 900 RELATED ID: 4JAR RELATED DB: PDB
REMARK 900 RELATED ID: 4JAT RELATED DB: PDB
REMARK 900 RELATED ID: 4JD3 RELATED DB: PDB
DBREF 4JAQ D 1 353 UNP O06587 PKS11_MYCTU 1 353
DBREF 4JAQ C 1 353 UNP O06587 PKS11_MYCTU 1 353
DBREF 4JAQ B 1 353 UNP O06587 PKS11_MYCTU 1 353
DBREF 4JAQ A 1 353 UNP O06587 PKS11_MYCTU 1 353
SEQRES 1 D 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 D 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 D 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 D 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 D 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 D 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 D 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 D 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 D 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 D 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 D 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 D 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 D 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 D 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 D 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 D 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 D 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 D 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 D 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 D 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 D 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 D 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 D 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 D 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 D 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 D 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 D 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 D 353 TRP ARG
SEQRES 1 A 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 A 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 A 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 A 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 A 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 A 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 A 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 A 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 A 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 A 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 A 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 A 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 A 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 A 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 A 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 A 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 A 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 A 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 A 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 A 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 A 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 A 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 A 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 A 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 A 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 A 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 A 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 A 353 TRP ARG
SEQRES 1 C 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 C 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 C 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 C 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 C 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 C 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 C 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 C 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 C 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 C 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 C 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 C 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 C 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 C 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 C 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 C 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 C 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 C 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 C 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 C 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 C 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 C 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 C 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 C 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 C 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 C 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 C 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 C 353 TRP ARG
SEQRES 1 B 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 B 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 B 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 B 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 B 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 B 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 B 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 B 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 B 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 B 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 B 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 B 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 B 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 B 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 B 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 B 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 B 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 B 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 B 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 B 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 B 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 B 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 B 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 B 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 B 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 B 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 B 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 B 353 TRP ARG
HET 14V A 401 23
HET COA C 401 48
HET COA B 401 48
HET PLM B 402 18
HET PLM C 402 17
HET 14V D 401 23
HETNAM 14V 3,5-DIOXOICOSANOIC ACID
HETNAM COA COENZYME A
HETNAM PLM PALMITIC ACID
FORMUL 5 14V 2(C20 H36 O4)
FORMUL 6 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 8 PLM 2(C16 H32 O2)
FORMUL 11 HOH *826(H2 O)
HELIX 1 1 GLN D 18 VAL D 26 1 9
HELIX 2 2 LEU D 31 GLU D 33 5 3
HELIX 3 3 HIS D 34 ALA D 44 1 11
HELIX 4 4 PRO D 55 LEU D 62 5 8
HELIX 5 5 ASP D 64 ASN D 92 1 29
HELIX 6 6 ARG D 94 ILE D 98 5 5
HELIX 7 7 SER D 113 GLY D 123 1 11
HELIX 8 8 LEU D 136 CYS D 138 5 3
HELIX 9 9 VAL D 139 ALA D 155 1 17
HELIX 10 10 SER D 169 VAL D 175 5 7
HELIX 11 11 THR D 178 PHE D 188 1 11
HELIX 12 12 GLY D 199 GLU D 204 1 6
HELIX 13 13 ASP D 244 ALA D 263 1 20
HELIX 14 14 THR D 267 ASP D 269 5 3
HELIX 15 15 GLY D 280 LEU D 291 1 12
HELIX 16 16 LEU D 298 GLY D 309 1 12
HELIX 17 17 LEU D 311 SER D 313 5 3
HELIX 18 18 ALA D 314 LYS D 326 1 13
HELIX 19 56 GLN A 18 VAL A 26 1 9
HELIX 20 57 LEU A 31 GLU A 33 5 3
HELIX 21 58 HIS A 34 ALA A 44 1 11
HELIX 22 59 PRO A 55 LEU A 62 5 8
HELIX 23 60 ASP A 64 ASN A 92 1 29
HELIX 24 61 ARG A 94 ILE A 98 5 5
HELIX 25 62 SER A 113 GLY A 123 1 11
HELIX 26 63 LEU A 136 CYS A 138 5 3
HELIX 27 64 VAL A 139 ALA A 155 1 17
HELIX 28 65 SER A 169 VAL A 175 5 7
HELIX 29 66 THR A 178 PHE A 188 1 11
HELIX 30 67 ARG A 202 ARG A 207 1 6
HELIX 31 68 SER A 224 HIS A 226 5 3
HELIX 32 69 ASP A 244 ALA A 263 1 20
HELIX 33 70 THR A 267 ASP A 269 5 3
HELIX 34 71 GLY A 280 ALA A 292 1 13
HELIX 35 72 LEU A 298 GLY A 309 1 12
HELIX 36 73 LEU A 311 SER A 313 5 3
HELIX 37 74 ALA A 314 LYS A 326 1 13
HELIX 38 19 GLN C 18 VAL C 26 1 9
HELIX 39 20 LEU C 31 GLU C 33 5 3
HELIX 40 21 HIS C 34 ALA C 45 1 12
HELIX 41 22 PRO C 55 LEU C 62 5 8
HELIX 42 23 ASP C 64 ASN C 92 1 29
HELIX 43 24 ARG C 94 ILE C 98 5 5
HELIX 44 25 SER C 113 GLY C 123 1 11
HELIX 45 26 LEU C 136 CYS C 138 5 3
HELIX 46 27 VAL C 139 GLY C 154 1 16
HELIX 47 28 SER C 169 VAL C 175 5 7
HELIX 48 29 THR C 178 PHE C 188 1 11
HELIX 49 30 GLY C 199 ARG C 207 1 9
HELIX 50 31 ASP C 244 ALA C 263 1 20
HELIX 51 32 THR C 267 ASP C 269 5 3
HELIX 52 33 GLY C 280 ALA C 292 1 13
HELIX 53 34 PRO C 294 ALA C 297 5 4
HELIX 54 35 LEU C 298 GLY C 309 1 12
HELIX 55 36 LEU C 311 SER C 313 5 3
HELIX 56 37 ALA C 314 ARG C 327 1 14
HELIX 57 38 GLN B 18 VAL B 26 1 9
HELIX 58 39 LEU B 31 GLU B 33 5 3
HELIX 59 40 HIS B 34 ALA B 45 1 12
HELIX 60 41 PRO B 55 LEU B 62 5 8
HELIX 61 42 ASP B 64 ASN B 92 1 29
HELIX 62 43 ARG B 94 ILE B 98 5 5
HELIX 63 44 SER B 113 GLY B 123 1 11
HELIX 64 45 LEU B 136 CYS B 138 5 3
HELIX 65 46 VAL B 139 ARG B 153 1 15
HELIX 66 47 SER B 169 VAL B 175 5 7
HELIX 67 48 THR B 178 PHE B 188 1 11
HELIX 68 49 GLY B 199 ARG B 207 1 9
HELIX 69 50 ASP B 244 HIS B 264 1 21
HELIX 70 51 THR B 267 ASP B 269 5 3
HELIX 71 52 GLY B 280 LEU B 291 1 12
HELIX 72 53 LEU B 298 GLY B 309 1 12
HELIX 73 54 LEU B 311 SER B 313 5 3
HELIX 74 55 ALA B 314 ARG B 327 1 14
SHEET 1 A 5 VAL D 3 ALA D 10 0
SHEET 2 A 5 ASP D 190 VAL D 198 -1 O VAL D 196 N ALA D 5
SHEET 3 A 5 VAL D 159 LEU D 167 -1 N ALA D 160 O ALA D 197
SHEET 4 A 5 MET D 100 THR D 105 1 N ALA D 102 O VAL D 161
SHEET 5 A 5 ARG D 129 PHE D 134 1 O ARG D 129 N ILE D 101
SHEET 1 B 2 ARG D 15 SER D 17 0
SHEET 2 B 2 GLY D 49 HIS D 51 -1 O ARG D 50 N TYR D 16
SHEET 1 C 4 ASP D 212 LEU D 220 0
SHEET 2 C 4 CYS D 344 ARG D 351 -1 O ARG D 351 N ASP D 212
SHEET 3 C 4 ALA D 333 GLY D 340 -1 N GLY D 334 O LEU D 350
SHEET 4 C 4 ILE D 271 SER D 276 1 N VAL D 275 O LEU D 335
SHEET 1 D 2 MET D 228 GLY D 233 0
SHEET 2 D 2 GLY D 236 LEU D 241 -1 O ARG D 238 N ASP D 231
SHEET 1 E 5 VAL C 3 ALA C 10 0
SHEET 2 E 5 ASP C 190 VAL C 198 -1 O VAL C 196 N ALA C 5
SHEET 3 E 5 VAL C 159 LEU C 167 -1 N SER C 164 O ALA C 193
SHEET 4 E 5 MET C 100 THR C 105 1 N ALA C 102 O VAL C 161
SHEET 5 E 5 ARG C 129 PHE C 134 1 O ARG C 129 N ILE C 101
SHEET 1 F 2 HIS C 14 SER C 17 0
SHEET 2 F 2 GLY C 49 LEU C 52 -1 O LEU C 52 N HIS C 14
SHEET 1 G 4 ASP C 212 LEU C 220 0
SHEET 2 G 4 CYS C 344 ARG C 351 -1 O LEU C 349 N ASP C 215
SHEET 3 G 4 ALA C 333 GLY C 340 -1 N GLY C 334 O LEU C 350
SHEET 4 G 4 ILE C 271 SER C 276 1 N GLY C 272 O ALA C 333
SHEET 1 H 2 MET C 228 GLY C 233 0
SHEET 2 H 2 GLY C 236 LEU C 241 -1 O ARG C 240 N GLY C 229
SHEET 1 I 5 VAL B 3 ALA B 10 0
SHEET 2 I 5 ASP B 190 VAL B 198 -1 O VAL B 196 N ALA B 5
SHEET 3 I 5 VAL B 159 LEU B 167 -1 N SER B 164 O ALA B 193
SHEET 4 I 5 MET B 100 THR B 105 1 N ALA B 102 O VAL B 161
SHEET 5 I 5 ARG B 129 PHE B 134 1 O ARG B 129 N ILE B 101
SHEET 1 J 2 HIS B 14 SER B 17 0
SHEET 2 J 2 GLY B 49 LEU B 52 -1 O LEU B 52 N HIS B 14
SHEET 1 K 4 ASP B 212 LEU B 220 0
SHEET 2 K 4 CYS B 344 ARG B 351 -1 O LEU B 349 N LEU B 214
SHEET 3 K 4 ALA B 333 GLY B 340 -1 N GLY B 334 O LEU B 350
SHEET 4 K 4 ILE B 271 SER B 276 1 N VAL B 275 O LEU B 335
SHEET 1 L 2 MET B 228 GLY B 233 0
SHEET 2 L 2 GLY B 236 LEU B 241 -1 O ARG B 238 N ASP B 231
SHEET 1 M 5 VAL A 3 ALA A 10 0
SHEET 2 M 5 ASP A 190 VAL A 198 -1 O VAL A 196 N ALA A 5
SHEET 3 M 5 VAL A 159 LEU A 167 -1 N SER A 164 O ALA A 193
SHEET 4 M 5 MET A 100 THR A 105 1 N ALA A 104 O VAL A 163
SHEET 5 M 5 ARG A 129 PHE A 134 1 O ARG A 129 N ILE A 101
SHEET 1 N 2 ARG A 15 SER A 17 0
SHEET 2 N 2 GLY A 49 HIS A 51 -1 O ARG A 50 N TYR A 16
SHEET 1 O 4 ASP A 212 LEU A 220 0
SHEET 2 O 4 CYS A 344 ARG A 351 -1 O LEU A 349 N ASP A 215
SHEET 3 O 4 ALA A 333 GLY A 340 -1 N GLY A 334 O LEU A 350
SHEET 4 O 4 ILE A 271 SER A 276 1 N VAL A 275 O LEU A 335
SHEET 1 P 2 MET A 228 GLY A 233 0
SHEET 2 P 2 GLY A 236 LEU A 241 -1 O ARG A 238 N ASP A 231
LINK SG CYS D 138 CAE 14V D 401 1555 1555 1.77
LINK SG CYS A 138 CAE 14V A 401 1555 1555 1.77
LINK SG CYS C 138 C1 PLM C 402 1555 1555 1.77
CISPEP 1 VAL D 111 PRO D 112 0 5.03
CISPEP 2 GLY D 342 PHE D 343 0 -8.16
CISPEP 3 VAL A 111 PRO A 112 0 1.89
CISPEP 4 GLY A 210 PRO A 211 0 2.18
CISPEP 5 GLY A 342 PHE A 343 0 -5.57
CISPEP 6 VAL C 111 PRO C 112 0 4.01
CISPEP 7 GLY C 210 PRO C 211 0 1.97
CISPEP 8 GLY C 342 PHE C 343 0 -6.43
CISPEP 9 VAL B 111 PRO B 112 0 -0.46
CISPEP 10 GLY B 210 PRO B 211 0 -0.18
CISPEP 11 GLY B 342 PHE B 343 0 -6.92
SITE 1 AC1 12 PHE D 28 LEU D 56 VAL D 106 GLY D 137
SITE 2 AC1 12 CYS D 138 THR D 171 PHE D 188 MET D 228
SITE 3 AC1 12 TRP D 230 LEU D 239 SER D 312 PRO D 341
SITE 1 AC2 11 PHE A 28 TYR A 59 VAL A 106 GLY A 137
SITE 2 AC2 11 CYS A 138 SER A 169 THR A 171 MET A 228
SITE 3 AC2 11 TRP A 230 LEU A 241 PRO A 341
SITE 1 AC3 15 ALA C 44 VAL C 179 SER C 180 VAL C 183
SITE 2 AC3 15 MET C 228 LEU C 241 PRO C 243 GLY C 279
SITE 3 AC3 15 PRO C 281 LYS C 282 MET C 339 HOH C 625
SITE 4 AC3 15 HOH C 647 HOH C 656 HOH C 714
SITE 1 AC4 10 VAL C 106 GLY C 137 CYS C 138 CYS C 168
SITE 2 AC4 10 THR C 171 PHE C 188 MET C 228 TRP C 230
SITE 3 AC4 10 SER C 312 HOH C 715
SITE 1 AC5 16 ARG B 40 ALA B 44 VAL B 179 SER B 180
SITE 2 AC5 16 VAL B 183 MET B 228 LEU B 241 PRO B 243
SITE 3 AC5 16 GLY B 279 PRO B 281 LYS B 282 VAL B 283
SITE 4 AC5 16 MET B 339 HOH B 641 HOH B 677 HOH B 721
SITE 1 AC6 9 ILE B 21 LEU B 56 VAL B 106 CYS B 138
SITE 2 AC6 9 THR B 171 PHE B 188 TRP B 230 SER B 312
SITE 3 AC6 9 HOH B 722
CRYST1 72.006 48.712 194.295 90.00 97.89 90.00 P 1 21 1 8
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 0.013888 0.000000 0.001925 0.00000
SCALE2 0.000000 0.020529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005196 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
