HEADER LYASE 26-APR-08 3CYV
TITLE CRYSTAL STRUCTURE OF UROPORPHYRINOGEN DECARBOXYLASE FROM SHIGELLA
TITLE 2 FLEXINERI: NEW INSIGHTS INTO ITS CATALYTIC MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UROPORPHYRINOGEN DECARBOXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: URO-D, UPD;
COMPND 5 EC: 4.1.1.37;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;
SOURCE 3 ORGANISM_TAXID: 623;
SOURCE 4 STRAIN: 2A STR. 301;
SOURCE 5 GENE: UROD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS ALPHA/BETA BARREL, CYTOPLASM, DECARBOXYLASE, LYASE, PORPHYRIN
KEYWDS 2 BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LIU,H.ZHOU,R.BI
REVDAT 2 01-NOV-23 3CYV 1 REMARK
REVDAT 1 28-APR-09 3CYV 0
JRNL AUTH H.LIU,H.ZHOU,R.BI
JRNL TITL CRYSTAL STRUCTURE OF UROPORPHYRINOGEN III DECARBOXYLASE FROM
JRNL TITL 2 SHIGELLA FLEXINERI: NEW INSIGHTS INTO ITS CATALYTIC
JRNL TITL 3 MECHANISM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1764582.510
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 9240
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.200
REMARK 3 FREE R VALUE TEST SET COUNT : 576
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1411
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 91
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2743
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.29000
REMARK 3 B22 (A**2) : -3.18000
REMARK 3 B33 (A**2) : -6.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.36
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.030
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 33.21
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-05
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 : BSRF
REMARK 200 BEAMLINE : 3W1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97954
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9240
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.30900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
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: PDB ENTRY 1URO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 38.92250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.92250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.20300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.08500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.20300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.08500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.92250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.20300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 68.08500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.92250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.20300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 68.08500
REMARK 290 SMTRY3 8 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: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 68.40600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 38.92250
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 A 1
REMARK 465 THR A 2
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 ARG A 8 -69.23 -18.40
REMARK 500 TRP A 24 144.46 -170.60
REMARK 500 LEU A 79 22.13 -79.27
REMARK 500 ALA A 93 -3.28 -50.67
REMARK 500 GLU A 95 -87.53 -52.95
REMARK 500 THR A 104 -66.40 -96.86
REMARK 500 CYS A 105 -163.10 -117.05
REMARK 500 ASP A 119 -92.54 -81.48
REMARK 500 LYS A 136 54.67 35.17
REMARK 500 ASP A 174 53.87 -146.12
REMARK 500 SER A 188 -70.68 -49.79
REMARK 500 ASP A 208 50.75 -113.00
REMARK 500 SER A 223 -59.07 -136.02
REMARK 500 ASN A 238 149.67 -176.38
REMARK 500 TRP A 271 -3.66 -48.89
REMARK 500 VAL A 282 -13.77 -150.92
REMARK 500 LYS A 285 -41.34 -177.50
REMARK 500 ASN A 291 -18.42 177.19
REMARK 500 PHE A 315 -78.43 -115.01
REMARK 500 HIS A 317 -49.85 -14.58
REMARK 500 GLU A 319 -32.51 -130.86
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3CYV A 1 354 UNP Q83PB7 DCUP_SHIFL 1 354
SEQRES 1 A 354 MET THR GLU LEU LYS ASN ASP ARG TYR LEU ARG ALA LEU
SEQRES 2 A 354 LEU ARG GLN PRO VAL ASP VAL THR PRO VAL TRP MET MET
SEQRES 3 A 354 ARG GLN ALA GLY ARG TYR LEU PRO GLU TYR LYS ALA THR
SEQRES 4 A 354 ARG ALA GLN ALA GLY ASP PHE MET SER LEU CYS LYS ASN
SEQRES 5 A 354 ALA GLU LEU ALA CYS GLU VAL THR LEU GLN PRO LEU ARG
SEQRES 6 A 354 ARG TYR PRO LEU ASP ALA ALA ILE LEU PHE SER ASP ILE
SEQRES 7 A 354 LEU THR VAL PRO ASP ALA MET GLY LEU GLY LEU TYR PHE
SEQRES 8 A 354 GLU ALA GLY GLU GLY PRO ARG PHE THR SER PRO VAL THR
SEQRES 9 A 354 CYS LYS ALA ASP VAL ASP LYS LEU PRO ILE PRO ASP PRO
SEQRES 10 A 354 GLU ASP GLU LEU GLY TYR VAL MET ASN ALA VAL ARG THR
SEQRES 11 A 354 ILE ARG HIS GLU LEU LYS GLY GLU VAL PRO LEU ILE GLY
SEQRES 12 A 354 PHE SER GLY SER PRO TRP THR LEU ALA THR TYR MET VAL
SEQRES 13 A 354 GLU GLY GLY SER SER LYS ALA PHE THR VAL ILE LYS LYS
SEQRES 14 A 354 MET MET TYR ALA ASP PRO GLN ALA LEU HIS ALA LEU LEU
SEQRES 15 A 354 ASP LYS LEU ALA LYS SER VAL THR LEU TYR LEU ASN ALA
SEQRES 16 A 354 GLN ILE LYS ALA GLY ALA GLN ALA VAL MET ILE PHE ASP
SEQRES 17 A 354 THR TRP GLY GLY VAL LEU THR GLY ARG ASP TYR GLN GLN
SEQRES 18 A 354 PHE SER LEU TYR TYR MET HIS LYS ILE VAL ASP GLY LEU
SEQRES 19 A 354 LEU ARG GLU ASN ASP GLY ARG ARG VAL PRO VAL THR LEU
SEQRES 20 A 354 PHE THR LYS GLY GLY GLY GLN TRP LEU GLU ALA MET ALA
SEQRES 21 A 354 GLU THR GLY CYS ASP ALA LEU GLY LEU ASP TRP THR THR
SEQRES 22 A 354 ASP ILE ALA ASP ALA ARG ARG ARG VAL GLY ASN LYS VAL
SEQRES 23 A 354 ALA LEU GLN GLY ASN MET ASP PRO SER MET LEU TYR ALA
SEQRES 24 A 354 PRO PRO ALA ARG ILE GLU GLU GLU VAL ALA THR ILE LEU
SEQRES 25 A 354 ALA GLY PHE GLY HIS GLY GLU GLY HIS VAL PHE ASN LEU
SEQRES 26 A 354 GLY HIS GLY ILE HIS GLN ASP VAL PRO PRO GLU HIS ALA
SEQRES 27 A 354 GLY VAL PHE VAL GLU ALA VAL HIS ARG LEU SER GLU GLN
SEQRES 28 A 354 TYR HIS ARG
FORMUL 2 HOH *229(H2 O)
HELIX 1 1 ASP A 7 LEU A 14 1 8
HELIX 2 2 LEU A 33 GLY A 44 1 12
HELIX 3 3 ASP A 45 CYS A 50 1 6
HELIX 4 4 ASN A 52 GLN A 62 1 11
HELIX 5 5 PRO A 63 ARG A 66 5 4
HELIX 6 6 LEU A 79 ALA A 84 1 6
HELIX 7 7 CYS A 105 LYS A 111 1 7
HELIX 8 8 LEU A 121 LEU A 135 1 15
HELIX 9 9 SER A 147 GLY A 158 1 12
HELIX 10 10 PHE A 164 TYR A 172 1 9
HELIX 11 11 ASP A 174 ALA A 199 1 26
HELIX 12 12 TRP A 210 LEU A 214 5 5
HELIX 13 13 THR A 215 SER A 223 1 9
HELIX 14 14 SER A 223 LEU A 234 1 12
HELIX 15 15 TRP A 255 GLU A 261 1 7
HELIX 16 16 ASP A 274 GLY A 283 1 10
HELIX 17 17 ASP A 293 ALA A 299 5 7
HELIX 18 18 PRO A 300 ALA A 313 1 14
HELIX 19 19 PRO A 334 GLU A 350 1 17
HELIX 20 20 GLN A 351 ARG A 354 5 4
SHEET 1 A 7 ALA A 72 ILE A 73 0
SHEET 2 A 7 LEU A 141 GLY A 146 1 O ILE A 142 N ALA A 72
SHEET 3 A 7 ALA A 203 PHE A 207 1 O PHE A 207 N SER A 145
SHEET 4 A 7 VAL A 245 PHE A 248 1 O THR A 246 N ILE A 206
SHEET 5 A 7 ALA A 266 GLY A 268 1 O ALA A 266 N LEU A 247
SHEET 6 A 7 ALA A 287 GLN A 289 1 O ALA A 287 N LEU A 267
SHEET 7 A 7 HIS A 321 VAL A 322 1 O VAL A 322 N LEU A 288
SHEET 1 B 2 LEU A 89 PHE A 91 0
SHEET 2 B 2 PRO A 97 PHE A 99 -1 O ARG A 98 N TYR A 90
SHEET 1 C 2 GLU A 237 ASN A 238 0
SHEET 2 C 2 ARG A 241 ARG A 242 -1 O ARG A 241 N ASN A 238
CRYST1 68.406 136.170 77.845 90.00 90.00 90.00 C 2 2 21 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 0.014619 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007344 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
