HEADER SIGNALING PROTEIN, TRANSFERASE 27-JAN-08 3C38
TITLE CRYSTAL STRUCTURE OF THE PERIPLASMIC DOMAIN OF VIBRIO
TITLE 2 CHOLERAE LUXQ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOINDUCER 2 SENSOR KINASE/PHOSPHATASE LUXQ;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.13.3, 3.1.3.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 GENE: LUXQ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS 2-COMPONENT SYSTEM, QUORUM SENSING, HISTIDINE KINASE,
KEYWDS 2 HYDROLASE, INNER MEMBRANE, MEMBRANE, PHOSPHOPROTEIN,
KEYWDS 3 PROTEIN PHOSPHATASE, TRANSFERASE, TRANSMEMBRANE, TWO-
KEYWDS 4 COMPONENT REGULATORY SYSTEM, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SLAMA,W.HENDRICKSON
REVDAT 1 27-JAN-09 3C38 0
JRNL AUTH B.SLAMA,W.HENDRICKSON
JRNL TITL CRYSTAL STRUCTURE OF THE PERIPLASMIC DOMAIN OF
JRNL TITL 2 VIBRIO CHOLERAE LUXQ
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1525864.440
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 11923
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) : 0.243
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 571
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1833
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 96
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1708
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.45000
REMARK 3 B22 (A**2) : 1.45000
REMARK 3 B33 (A**2) : -2.91000
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) : 0.33
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.81
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.640 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.830 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 59.35
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 : MES+PEGS_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3C38 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-08.
REMARK 100 THE RCSB ID CODE IS RCSB046284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11949
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 31.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% V/V PEG 20000, 0.1M MES, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 80.70750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.82800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.82800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.35375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.82800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.82800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 121.06125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.82800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.82800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.35375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.82800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.82800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 121.06125
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 80.70750
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 32
REMARK 465 SER A 33
REMARK 465 HIS A 34
REMARK 465 MET A 35
REMARK 465 GLN A 36
REMARK 465 SER A 37
REMARK 465 TYR A 38
REMARK 465 GLN A 39
REMARK 465 ILE A 40
REMARK 465 SER A 41
REMARK 465 SER A 42
REMARK 465 ARG A 43
REMARK 465 LEU A 44
REMARK 465 MET A 45
REMARK 465 ALA A 46
REMARK 465 GLN A 47
REMARK 465 GLU A 48
REMARK 465 GLY A 49
REMARK 465 GLN A 50
REMARK 465 ARG A 51
REMARK 465 THR A 179
REMARK 465 MET A 243
REMARK 465 ARG A 244
REMARK 465 GLN A 272
REMARK 465 ASN A 273
REMARK 465 VAL A 274
REMARK 465 LEU A 275
REMARK 465 THR A 276
REMARK 465 LEU A 277
REMARK 465 ARG A 278
REMARK 465 ASP A 279
REMARK 465 ASN A 280
REMARK 465 GLU A 281
REMARK 465 SER A 282
REMARK 465 VAL A 283
REMARK 465 PRO A 284
REMARK 465 THR A 285
REMARK 465 TYR A 286
REMARK 465 LEU A 287
REMARK 465 CYS A 288
REMARK 465 VAL A 289
REMARK 465 TYR A 290
REMARK 465 SER A 291
REMARK 465 ILE A 292
REMARK 465 GLN A 293
REMARK 465 THR A 294
REMARK 465 ASN A 295
REMARK 465 GLN A 296
REMARK 465 ASN A 297
REMARK 465 VAL A 298
REMARK 465 ARG A 299
REMARK 465 HIS A 300
REMARK 465 GLN A 301
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 OD1 ASP A 245 O HOH A 331 2.12
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 SER A 53 -75.17 -37.13
REMARK 500 ARG A 91 19.71 52.13
REMARK 500 GLU A 107 30.65 -154.19
REMARK 500 LEU A 108 -36.21 -37.83
REMARK 500 HIS A 120 -164.76 66.63
REMARK 500 ASP A 121 8.09 -60.60
REMARK 500 SER A 160 -157.47 -121.22
REMARK 500 ALA A 177 109.98 -29.82
REMARK 500 GLN A 181 -142.59 -144.99
REMARK 500 VAL A 182 109.10 -39.85
REMARK 500 ASP A 194 17.42 56.60
REMARK 500 ASP A 216 -101.28 70.43
REMARK 500 ASP A 241 56.89 28.08
REMARK 500 SER A 258 17.10 55.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C30 RELATED DB: PDB
REMARK 900 VIBRIO CHOLERAE SEMET LUXQ RESIDUES 36-280
DBREF 3C38 A 36 280 UNP Q9KLK7 LUXQ_VIBCH 36 280
SEQADV 3C38 GLY A 32 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 SER A 33 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 HIS A 34 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 MET A 35 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 GLU A 281 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 SER A 282 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 VAL A 283 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 PRO A 284 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 THR A 285 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 TYR A 286 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 LEU A 287 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 CYS A 288 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 VAL A 289 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 TYR A 290 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 SER A 291 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 ILE A 292 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 GLN A 293 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 THR A 294 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 ASN A 295 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 GLN A 296 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 ASN A 297 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 VAL A 298 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 ARG A 299 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 HIS A 300 UNP Q9KLK7 EXPRESSION TAG
SEQADV 3C38 GLN A 301 UNP Q9KLK7 EXPRESSION TAG
SEQRES 1 A 270 GLY SER HIS MET GLN SER TYR GLN ILE SER SER ARG LEU
SEQRES 2 A 270 MET ALA GLN GLU GLY GLN ARG THR SER VAL GLN THR SER
SEQRES 3 A 270 SER LEU ILE GLN SER LEU PHE ASP PHE ARG LEU ALA ALA
SEQRES 4 A 270 LEU ARG ILE HIS GLN ASP SER THR ALA LYS ASN ALA SER
SEQRES 5 A 270 LEU ILE ASN ALA LEU VAL SER ARG ASP SER SER ARG LEU
SEQRES 6 A 270 ASP GLU PHE PHE SER SER VAL ASP GLU LEU GLU LEU SER
SEQRES 7 A 270 ASN ALA PRO ASP LEU ARG PHE ILE SER SER HIS ASP ASN
SEQRES 8 A 270 ILE LEU TRP ASP ASP GLY ASN ALA SER PHE TYR GLY ILE
SEQRES 9 A 270 ALA GLN GLN GLU LEU ASN LYS LEU ILE ARG ARG VAL ALA
SEQRES 10 A 270 ILE SER GLY ASN TRP HIS LEU VAL GLN THR PRO SER GLU
SEQRES 11 A 270 GLY LYS SER VAL HIS ILE LEU MET ARG ARG SER SER LEU
SEQRES 12 A 270 ILE GLU ALA GLY THR GLY GLN VAL VAL GLY TYR LEU TYR
SEQRES 13 A 270 VAL GLY ILE VAL LEU ASN ASP ASN PHE ALA LEU LEU GLU
SEQRES 14 A 270 ASN ILE ARG SER GLY SER ASN SER GLU ASN LEU VAL LEU
SEQRES 15 A 270 ALA VAL ASP THR THR PRO LEU VAL SER THR LEU LYS GLY
SEQRES 16 A 270 ASN GLU PRO TYR SER LEU ASP TYR VAL VAL HIS SER ALA
SEQRES 17 A 270 LYS ASP ALA MET ARG ASP SER PHE ILE VAL GLY GLN THR
SEQRES 18 A 270 PHE LEU GLU VAL GLU SER VAL PRO THR TYR LEU CYS VAL
SEQRES 19 A 270 TYR SER ILE GLN THR ASN GLN ASN VAL LEU THR LEU ARG
SEQRES 20 A 270 ASP ASN GLU SER VAL PRO THR TYR LEU CYS VAL TYR SER
SEQRES 21 A 270 ILE GLN THR ASN GLN ASN VAL ARG HIS GLN
FORMUL 2 HOH *116(H2 O)
HELIX 1 1 THR A 52 ALA A 79 1 28
HELIX 2 2 ASN A 81 SER A 90 1 10
HELIX 3 3 ARG A 95 LEU A 106 1 12
HELIX 4 4 GLU A 107 ALA A 111 5 5
HELIX 5 5 ASN A 129 GLY A 134 5 6
HELIX 6 6 ALA A 136 VAL A 147 1 12
HELIX 7 7 ASN A 195 SER A 206 1 12
HELIX 8 8 SER A 231 HIS A 237 1 7
SHEET 1 A 5 ASN A 122 ASP A 126 0
SHEET 2 A 5 LEU A 114 SER A 119 -1 N SER A 119 O ASN A 122
SHEET 3 A 5 GLY A 184 VAL A 191 -1 O TYR A 187 N PHE A 116
SHEET 4 A 5 VAL A 165 LEU A 174 -1 N LEU A 174 O GLY A 184
SHEET 5 A 5 HIS A 154 THR A 158 -1 N VAL A 156 O ILE A 167
SHEET 1 B 4 THR A 218 SER A 222 0
SHEET 2 B 4 ASN A 210 VAL A 215 -1 N LEU A 213 O LEU A 220
SHEET 3 B 4 VAL A 259 THR A 270 -1 O TYR A 266 N VAL A 212
SHEET 4 B 4 PHE A 247 VAL A 256 -1 N THR A 252 O VAL A 265
CRYST1 55.656 55.656 161.415 90.00 90.00 90.00 P 41 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 0.017968 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017968 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006195 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
