HEADER TRANSCRIPTION REGULATOR 04-APR-07 2PFB
TITLE STRUCTURE OF OXIDIZED OHRR FROM XANTHAMONAS CAMPESTRIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR OHRR;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS;
SOURCE 3 ORGANISM_TAXID: 339;
SOURCE 4 GENE: OHRR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS TRANSCRIPTIONAL REGULATOR, MARR FAMILY, TRANSCRIPTION REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR R.G.BRENNAN,K.J.NEWBERRY
REVDAT 6 30-AUG-23 2PFB 1 REMARK
REVDAT 5 20-OCT-21 2PFB 1 SEQADV
REVDAT 4 18-OCT-17 2PFB 1 REMARK
REVDAT 3 13-JUL-11 2PFB 1 VERSN
REVDAT 2 24-FEB-09 2PFB 1 VERSN
REVDAT 1 11-DEC-07 2PFB 0
JRNL AUTH K.J.NEWBERRY,M.FUANGTHONG,W.PANMANEE,S.MONGKOLSUK,
JRNL AUTH 2 R.G.BRENNAN
JRNL TITL STRUCTURAL MECHANISM OF ORGANIC HYDROPEROXIDE INDUCTION OF
JRNL TITL 2 THE TRANSCRIPTION REGULATOR OHRR.
JRNL REF MOL.CELL V. 28 652 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 18042459
JRNL DOI 10.1016/J.MOLCEL.2007.09.016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.PANMANEE,P.VATTANAVIBOON,L.B.POOLE,S.MONGKOLSUK
REMARK 1 TITL NOVEL ORGANIC HYDROPEROXIDE-SENSING AND RESPONDING
REMARK 1 TITL 2 MECHANISMS FOR OHRR, A MAJOR BACTERIAL SENSOR AND REGULATOR
REMARK 1 TITL 3 OF ORGANIC HYDROPEROXIDE STRESS
REMARK 1 REF J.BACTERIOL. V. 188 1389 2006
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. 1.93 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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1872286.375
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 20477
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) : 0.219
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 995
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1012
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1975
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.33000
REMARK 3 B22 (A**2) : -1.74000
REMARK 3 B33 (A**2) : 3.07000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : -0.0
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
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) : 2.880 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.730 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.180 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.560 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 53.35
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 : 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: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2PFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042313.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 93
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, D*TREK
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20477
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 33.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.13
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
REMARK 200 R SYM FOR SHELL (I) : 0.28000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
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: RESIDUES 18 TO 107 FROM PDB ENTRY 2PEX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 300MM MAGNESIUM
REMARK 280 CHLORIDE, 100 MM TRIS, PH8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 44.44500
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 44.44500
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 30.57000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.57000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.44500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.57000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.44500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.57000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.13000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 A 1
REMARK 465 ASP A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 ALA A 9
REMARK 465 ARG A 10
REMARK 465 THR A 11
REMARK 465 ASP A 12
REMARK 465 THR A 13
REMARK 465 ALA A 96
REMARK 465 ALA A 97
REMARK 465 SER A 98
REMARK 465 ASP A 99
REMARK 465 GLU A 100
REMARK 465 ARG A 101
REMARK 465 GLN A 102
REMARK 465 LEU A 150
REMARK 465 GLY A 151
REMARK 465 ALA A 152
REMARK 465 GLY A 153
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 THR B 7
REMARK 465 THR B 8
REMARK 465 ALA B 9
REMARK 465 ARG B 10
REMARK 465 THR B 11
REMARK 465 ASP B 12
REMARK 465 THR B 13
REMARK 465 LEU B 14
REMARK 465 LEU B 15
REMARK 465 GLN B 16
REMARK 465 LEU B 17
REMARK 465 ALA B 96
REMARK 465 ALA B 97
REMARK 465 SER B 98
REMARK 465 ASP B 99
REMARK 465 GLU B 100
REMARK 465 ARG B 101
REMARK 465 ARG B 147
REMARK 465 SER B 148
REMARK 465 SER B 149
REMARK 465 LEU B 150
REMARK 465 GLY B 151
REMARK 465 ALA B 152
REMARK 465 GLY B 153
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 ARG A 95 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 95 CG CD NE CZ NH1 NH2
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 VAL B 121 58.97 31.27
REMARK 500 LYS B 145 -15.20 -157.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PEX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF REDUCED C22S OHRR FROM XANTHAMONAS CAMPESTRIS
REMARK 900 RELATED ID: 1Z91 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF OHRR C15S FROM BACILLUS SUBTILIS
REMARK 900 RELATED ID: 1Z9C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF OHRR BOUND TO THE OHRA PROMOTER FROM BACILLUS
REMARK 900 SUBTILIS
DBREF 2PFB A 1 153 UNP Q93R11 Q93R11_XANCH 1 153
DBREF 2PFB B 1 153 UNP Q93R11 Q93R11_XANCH 1 153
SEQADV 2PFB SER A 131 UNP Q93R11 CYS 131 ENGINEERED MUTATION
SEQADV 2PFB SER B 131 UNP Q93R11 CYS 131 ENGINEERED MUTATION
SEQRES 1 A 153 MET ASP THR THR THR ALA THR THR ALA ARG THR ASP THR
SEQRES 2 A 153 LEU LEU GLN LEU ASP ASN GLN LEU CYS PHE ALA LEU TYR
SEQRES 3 A 153 SER ALA ASN LEU ALA MET HIS LYS LEU TYR ARG GLY LEU
SEQRES 4 A 153 LEU LYS ALA LEU ASP LEU THR TYR PRO GLN TYR LEU VAL
SEQRES 5 A 153 MET LEU VAL LEU TRP GLU THR ASP GLU ARG SER VAL SER
SEQRES 6 A 153 GLU ILE GLY GLU ARG LEU TYR LEU ASP SER ALA THR LEU
SEQRES 7 A 153 THR PRO LEU LEU LYS ARG LEU GLN ALA ALA GLY LEU VAL
SEQRES 8 A 153 THR ARG THR ARG ALA ALA SER ASP GLU ARG GLN VAL ILE
SEQRES 9 A 153 ILE ALA LEU THR GLU THR GLY ARG ALA LEU ARG SER LYS
SEQRES 10 A 153 ALA GLY ALA VAL PRO GLU GLN VAL PHE CYS ALA SER ALA
SEQRES 11 A 153 SER SER LEU ASP GLU LEU ARG GLN LEU LYS GLN GLU LEU
SEQRES 12 A 153 GLU LYS LEU ARG SER SER LEU GLY ALA GLY
SEQRES 1 B 153 MET ASP THR THR THR ALA THR THR ALA ARG THR ASP THR
SEQRES 2 B 153 LEU LEU GLN LEU ASP ASN GLN LEU CYS PHE ALA LEU TYR
SEQRES 3 B 153 SER ALA ASN LEU ALA MET HIS LYS LEU TYR ARG GLY LEU
SEQRES 4 B 153 LEU LYS ALA LEU ASP LEU THR TYR PRO GLN TYR LEU VAL
SEQRES 5 B 153 MET LEU VAL LEU TRP GLU THR ASP GLU ARG SER VAL SER
SEQRES 6 B 153 GLU ILE GLY GLU ARG LEU TYR LEU ASP SER ALA THR LEU
SEQRES 7 B 153 THR PRO LEU LEU LYS ARG LEU GLN ALA ALA GLY LEU VAL
SEQRES 8 B 153 THR ARG THR ARG ALA ALA SER ASP GLU ARG GLN VAL ILE
SEQRES 9 B 153 ILE ALA LEU THR GLU THR GLY ARG ALA LEU ARG SER LYS
SEQRES 10 B 153 ALA GLY ALA VAL PRO GLU GLN VAL PHE CYS ALA SER ALA
SEQRES 11 B 153 SER SER LEU ASP GLU LEU ARG GLN LEU LYS GLN GLU LEU
SEQRES 12 B 153 GLU LYS LEU ARG SER SER LEU GLY ALA GLY
FORMUL 3 HOH *84(H2 O)
HELIX 1 1 ASN A 19 ASP A 44 1 26
HELIX 2 2 THR A 46 THR A 59 1 14
HELIX 3 3 VAL A 64 TYR A 72 1 9
HELIX 4 4 ASP A 74 ALA A 88 1 15
HELIX 5 5 THR A 108 ARG A 115 1 8
HELIX 6 6 SER A 116 GLY A 119 5 4
HELIX 7 7 VAL A 121 PHE A 126 1 6
HELIX 8 8 CYS A 127 SER A 131 5 5
HELIX 9 9 LEU A 133 SER A 149 1 17
HELIX 10 10 ASN B 19 ASP B 44 1 26
HELIX 11 11 THR B 46 THR B 59 1 14
HELIX 12 12 VAL B 64 TYR B 72 1 9
HELIX 13 13 ASP B 74 ALA B 88 1 15
HELIX 14 14 THR B 108 ALA B 118 1 11
HELIX 15 15 VAL B 121 PHE B 126 1 6
HELIX 16 16 CYS B 127 SER B 131 5 5
HELIX 17 17 LEU B 133 GLU B 144 1 12
SHEET 1 A 3 ARG A 62 SER A 63 0
SHEET 2 A 3 ILE A 104 LEU A 107 -1 O ILE A 105 N ARG A 62
SHEET 3 A 3 VAL A 91 THR A 94 -1 N THR A 94 O ILE A 104
SHEET 1 B 3 ARG B 62 SER B 63 0
SHEET 2 B 3 ILE B 104 LEU B 107 -1 O ILE B 105 N ARG B 62
SHEET 3 B 3 VAL B 91 THR B 94 -1 N THR B 94 O ILE B 104
SSBOND 1 CYS A 22 CYS B 127 1555 1555 2.04
SSBOND 2 CYS A 127 CYS B 22 1555 1555 2.05
CRYST1 61.140 98.260 88.890 90.00 90.00 90.00 C 2 2 21 16
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 0.016356 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010177 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011250 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
