HEADER LYASE 22-APR-12 4ES6
TITLE CRYSTAL STRUCTURE OF HEMD (PA5259) FROM PSEUDOMONAS AERUGINOSA (PAO1)
TITLE 2 AT 2.22 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UROPORPHYRINOGEN-III SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UROS, HYDROXYMETHYLBILANE HYDROLYASE [CYCLIZING],
COMPND 5 UROPORPHYRINOGEN-III COSYNTHASE;
COMPND 6 EC: 4.2.1.75;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: HEMD, PA5259;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HEME-BIOSYNTHESIS, UROPORPHYRINOGEN-III SYNTHASE, CYTOPLASMIC, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SCHNELL,G.SCHNEIDER
REVDAT 3 28-FEB-24 4ES6 1 REMARK SEQADV
REVDAT 2 23-JAN-13 4ES6 1 JRNL
REVDAT 1 09-JAN-13 4ES6 0
JRNL AUTH L.MOYNIE,R.SCHNELL,S.A.MCMAHON,T.SANDALOVA,W.A.BOULKEROU,
JRNL AUTH 2 J.W.SCHMIDBERGER,M.ALPHEY,C.CUKIER,F.DUTHIE,J.KOPEC,H.LIU,
JRNL AUTH 3 A.JACEWICZ,W.N.HUNTER,J.H.NAISMITH,G.SCHNEIDER
JRNL TITL THE AEROPATH PROJECT TARGETING PSEUDOMONAS AERUGINOSA:
JRNL TITL 2 CRYSTALLOGRAPHIC STUDIES FOR ASSESSMENT OF POTENTIAL TARGETS
JRNL TITL 3 IN EARLY-STAGE DRUG DISCOVERY.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 69 25 2013
JRNL REFN ESSN 1744-3091
JRNL PMID 23295481
JRNL DOI 10.1107/S1744309112044739
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 17976
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 + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 940
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1246
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.3810
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.4520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1905
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.73000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.217
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.775
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1953 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2664 ; 1.174 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 250 ; 5.562 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;32.867 ;22.529
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 311 ;16.398 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.468 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 299 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1517 ; 0.005 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1248 ; 0.625 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1991 ; 1.201 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 705 ; 1.752 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 672 ; 3.068 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ES6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000072002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979400
REMARK 200 MONOCHROMATOR : SI (311) MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18993
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 66.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : 0.53900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-CACODYLATE PH 6.7, 0.87M NA
REMARK 280 -CITRATE , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 21.22000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 66.03500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.03500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.83000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.03500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 66.03500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 10.61000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.03500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.03500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.83000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 66.03500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.03500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 10.61000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 21.22000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER 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 10 153.07 -44.44
REMARK 500 ARG A 137 -168.37 -162.39
REMARK 500 ALA A 202 -123.33 46.84
REMARK 500 ARG A 236 54.84 -91.24
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
DBREF 4ES6 A 1 251 UNP P48246 HEM4_PSEAE 1 251
SEQADV 4ES6 GLY A -2 UNP P48246 EXPRESSION TAG
SEQADV 4ES6 SER A -1 UNP P48246 EXPRESSION TAG
SEQADV 4ES6 HIS A 0 UNP P48246 EXPRESSION TAG
SEQRES 1 A 254 GLY SER HIS MET SER GLY TRP ARG LEU LEU LEU THR ARG
SEQRES 2 A 254 PRO ASP GLU GLU CYS ALA ALA LEU ALA ALA SER LEU GLY
SEQRES 3 A 254 GLU ALA GLY VAL HIS SER SER SER LEU PRO LEU LEU ALA
SEQRES 4 A 254 ILE ASP PRO LEU GLU GLU THR PRO GLU GLN ARG THR LEU
SEQRES 5 A 254 MET LEU ASP LEU ASP ARG TYR CYS ALA VAL VAL VAL VAL
SEQRES 6 A 254 SER LYS PRO ALA ALA ARG LEU GLY LEU GLU ARG LEU ASP
SEQRES 7 A 254 ARG TYR TRP PRO GLN PRO PRO GLN GLN THR TRP CYS SER
SEQRES 8 A 254 VAL GLY ALA ALA THR ALA ALA ILE LEU GLU ALA TYR GLY
SEQRES 9 A 254 LEU ASP VAL THR TYR PRO GLU GLN GLY ASP ASP SER GLU
SEQRES 10 A 254 ALA LEU LEU ALA LEU PRO ALA PHE GLN ASP SER LEU ARG
SEQRES 11 A 254 VAL HIS ASP PRO LYS VAL LEU ILE MET ARG GLY GLU GLY
SEQRES 12 A 254 GLY ARG GLU PHE LEU ALA GLU ARG LEU ARG GLY GLN GLY
SEQRES 13 A 254 VAL GLN VAL ASP TYR LEU PRO LEU TYR ARG ARG ARG ALA
SEQRES 14 A 254 PRO ASP TYR PRO ALA GLY GLU LEU LEU ALA ARG VAL ARG
SEQRES 15 A 254 ALA GLU ARG LEU ASN GLY LEU VAL VAL SER SER GLY GLN
SEQRES 16 A 254 GLY LEU GLN ASN LEU TYR GLN LEU ALA ALA ALA ASP TRP
SEQRES 17 A 254 PRO GLU ILE GLY ARG LEU PRO LEU PHE VAL PRO SER PRO
SEQRES 18 A 254 ARG VAL ALA GLU MET ALA ARG GLU LEU GLY ALA GLN ARG
SEQRES 19 A 254 VAL ILE ASP CYS ARG GLY ALA SER ALA PRO ALA LEU LEU
SEQRES 20 A 254 ALA ALA LEU THR SER ALA ALA
HET CL A 301 1
HET CL A 302 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 HOH *98(H2 O)
HELIX 1 1 PRO A 11 ALA A 25 1 15
HELIX 2 2 THR A 43 ASP A 52 1 10
HELIX 3 3 LEU A 53 TYR A 56 5 4
HELIX 4 4 SER A 63 TRP A 78 1 16
HELIX 5 5 GLY A 90 GLY A 101 1 12
HELIX 6 6 ASP A 112 ALA A 118 1 7
HELIX 7 7 LEU A 119 LEU A 126 1 8
HELIX 8 8 GLU A 143 GLN A 152 1 10
HELIX 9 9 GLY A 172 GLU A 181 1 10
HELIX 10 10 SER A 190 ALA A 202 1 13
HELIX 11 11 ASP A 204 GLY A 209 1 6
HELIX 12 12 SER A 217 LEU A 227 1 11
HELIX 13 13 SER A 239 ALA A 250 1 12
SHEET 1 A 5 HIS A 28 SER A 31 0
SHEET 2 A 5 ARG A 5 LEU A 8 1 N LEU A 6 O SER A 30
SHEET 3 A 5 GLY A 185 VAL A 187 1 O VAL A 187 N LEU A 7
SHEET 4 A 5 LEU A 213 VAL A 215 1 O PHE A 214 N LEU A 186
SHEET 5 A 5 VAL A 232 ASP A 234 1 O ILE A 233 N LEU A 213
SHEET 1 B 2 ALA A 36 PRO A 39 0
SHEET 2 B 2 TYR A 162 ARG A 165 -1 O ARG A 165 N ALA A 36
SHEET 1 C 5 VAL A 104 THR A 105 0
SHEET 2 C 5 THR A 85 SER A 88 1 N TRP A 86 O THR A 105
SHEET 3 C 5 ALA A 58 VAL A 61 1 N VAL A 59 O CYS A 87
SHEET 4 C 5 LYS A 132 ARG A 137 1 O MET A 136 N VAL A 60
SHEET 5 C 5 GLN A 155 PRO A 160 1 O ASP A 157 N ILE A 135
SITE 1 AC1 3 THR A 9 ARG A 10 VAL A 187
SITE 1 AC2 3 GLU A 139 GLY A 140 ARG A 164
CRYST1 132.070 132.070 42.440 90.00 90.00 90.00 P 43 21 2 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 0.007572 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
