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HEADER HALOPEROXIDASE 26-MAR-98 1A8U
TITLE CHLOROPEROXIDASE T/BENZOATE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPEROXIDASE T;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BROMOPEROXIDASE T;
COMPND 5 EC: 1.11.1.10;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: COMPLEX WITH BENZOIC ACID
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS;
SOURCE 3 STRAIN: TUE24;
SOURCE 4 GENE: CPOT;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TK64;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PIJ486;
SOURCE 9 EXPRESSION_SYSTEM_GENE: CPOT
KEYWDS HALOPEROXIDASE, OXIDOREDUCTASE, BENZOATE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.HOFMANN,S.TOELZER,I.PELLETIER,J.ALTENBUCHNER,K.-H.VAN PEE,
AUTHOR 2 H.-J.HECHT
REVDAT 1 17-JUN-98 1A8U 0
JRNL AUTH B.HOFMANN,S.TOELZER,I.PELLETIER,J.ALTENBUCHNER,
JRNL AUTH 2 K.H.VAN PEE,H.J.HECHT
JRNL TITL STRUCTURAL INVESTIGATION OF THE COFACTOR-FREE
JRNL TITL 2 CHLOROPEROXIDASES
JRNL REF J.MOL.BIOL. V. 279 889 1998
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 84499
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT : 4229
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.149
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.152
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4429
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 84499
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4290
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 671
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.02
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.026 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.022 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.131 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.169 ; 0.30
REMARK 3 MULTIPLE TORSION (A) : 0.250 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : 0.093 ; 0.30
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 0.0 ; 15.0
REMARK 3 PLANAR (DEGREES) : 4.1 ; 7.00
REMARK 3 STAGGERED (DEGREES) : 11.9 ; 15.00
REMARK 3 TRANSVERSE (DEGREES) : 30.4 ; 20.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.07 ; 2.00
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.57 ; 3.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.69 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.42 ; 3.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A8U COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-1997
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84499
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 28.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.7
REMARK 200 R MERGE (I) : 0.076
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.0
REMARK 200 R MERGE FOR SHELL (I) : 0.18
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.0
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1A7U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE PH 7.8.,
REMARK 280 SMALL AMOUNTS OF SOLID SODIUM BENZOATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 1/2+Z,1/2-X,-Y
REMARK 290 7555 1/2-Z,-X,1/2+Y
REMARK 290 8555 -Z,1/2+X,1/2-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,1/2+Z,1/2-X
REMARK 290 11555 1/2+Y,1/2-Z,-X
REMARK 290 12555 1/2-Y,-Z,1/2+X
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 62.43756
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.43756
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.43756
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.43756
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.43756
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.43756
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 62.43756
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 62.43756
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 62.43756
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 62.43756
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 62.43756
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 62.43756
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 62.43756
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 62.43756
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 62.43756
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 62.43756
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 62.43756
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 62.43756
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 1 .. 277 B 1 .. 277 0.345
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUA
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: NUB
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1A8U A GB 2625105 1 - 1 NOT IN ATOMS LIST
REMARK 999 1A8U B GB 2625105 1 - 1 NOT IN ATOMS LIST
DBREF 1A8U A 1 277 GB 2625105 AF031242 2 278
DBREF 1A8U B 1 277 GB 2625105 AF031242 2 278
SEQRES 1 A 277 PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER ILE
SEQRES 2 A 277 ASP LEU TYR TYR GLU ASP HIS GLY ALA GLY GLN PRO VAL
SEQRES 3 A 277 VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER TRP
SEQRES 4 A 277 GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR ARG
SEQRES 5 A 277 VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER SER
SEQRES 6 A 277 GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA ALA
SEQRES 7 A 277 ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN ASP
SEQRES 8 A 277 ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU VAL
SEQRES 9 A 277 ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE ALA
SEQRES 10 A 277 LYS VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU LEU
SEQRES 11 A 277 LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO LYS GLU
SEQRES 12 A 277 PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP ARG
SEQRES 13 A 277 TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR ASN
SEQRES 14 A 277 LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU ALA
SEQRES 15 A 277 VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY PHE
SEQRES 16 A 277 PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR ASP
SEQRES 17 A 277 PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA LEU
SEQRES 18 A 277 ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE GLU
SEQRES 19 A 277 ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER ALA
SEQRES 20 A 277 GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU LEU
SEQRES 21 A 277 TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU ALA
SEQRES 22 A 277 PHE LEU ALA LYS
SEQRES 1 B 277 PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER ILE
SEQRES 2 B 277 ASP LEU TYR TYR GLU ASP HIS GLY ALA GLY GLN PRO VAL
SEQRES 3 B 277 VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER TRP
SEQRES 4 B 277 GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR ARG
SEQRES 5 B 277 VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER SER
SEQRES 6 B 277 GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA ALA
SEQRES 7 B 277 ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN ASP
SEQRES 8 B 277 ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU VAL
SEQRES 9 B 277 ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE ALA
SEQRES 10 B 277 LYS VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU LEU
SEQRES 11 B 277 LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO LYS GLU
SEQRES 12 B 277 PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP ARG
SEQRES 13 B 277 TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR ASN
SEQRES 14 B 277 LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU ALA
SEQRES 15 B 277 VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY PHE
SEQRES 16 B 277 PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR ASP
SEQRES 17 B 277 PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA LEU
SEQRES 18 B 277 ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE GLU
SEQRES 19 B 277 ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER ALA
SEQRES 20 B 277 GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU LEU
SEQRES 21 B 277 TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU ALA
SEQRES 22 B 277 PHE LEU ALA LYS
HET BEZ A 1 9
HET SO4 A 290 5
HET SO4 A 292 5
HET SO4 A 294 5
HET BEZ B 2 9
HET SO4 B 291 5
HET SO4 B 293 5
HETNAM BEZ BENZOIC ACID
HETNAM SO4 SULFATE ION
FORMUL 3 BEZ 2(C7 H6 O2)
FORMUL 4 SO4 5(O4 S1 2-)
FORMUL 5 HOH *671(H2 O1)
HELIX 1 1 GLY A 36 ASP A 48 5 13
HELIX 2 2 TYR A 73 LEU A 87 1 15
HELIX 3 3 SER A 98 TYR A 111 5 14
HELIX 4 4 LYS A 142 ALA A 154 1 13
HELIX 5 5 ARG A 156 PHE A 167 1 12
HELIX 6 6 LEU A 170 ASN A 173 1 4
HELIX 7 7 GLU A 180 SER A 192 1 13
HELIX 8 8 PHE A 195 TYR A 206 1 12
HELIX 9 9 ARG A 210 ARG A 215 1 6
HELIX 10 10 ILE A 233 ASN A 235 5 3
HELIX 11 11 ALA A 237 ALA A 243 1 7
HELIX 12 12 LEU A 259 THR A 262 1 4
HELIX 13 13 ALA A 264 LEU A 275 1 12
HELIX 14 14 GLY B 36 ALA B 49 5 14
HELIX 15 15 TYR B 73 LEU B 87 1 15
HELIX 16 16 SER B 98 TYR B 111 5 14
HELIX 17 17 LYS B 142 ALA B 154 1 13
HELIX 18 18 ARG B 156 PHE B 167 1 12
HELIX 19 19 LEU B 170 ASN B 173 1 4
HELIX 20 20 GLU B 180 SER B 192 1 13
HELIX 21 21 PHE B 195 TRP B 205 1 11
HELIX 22 22 ARG B 210 ARG B 215 1 6
HELIX 23 23 ILE B 233 ASN B 235 5 3
HELIX 24 24 ALA B 237 ALA B 243 1 7
HELIX 25 25 LEU B 259 THR B 262 1 4
HELIX 26 26 ALA B 264 LEU B 275 1 12
SHEET 1 A 7 TYR A 17 GLY A 21 0
SHEET 2 A 7 ARG A 52 TYR A 56 -1 N THR A 55 O GLU A 18
SHEET 3 A 7 PRO A 25 ILE A 29 1 N VAL A 26 O ARG A 52
SHEET 4 A 7 ALA A 92 PHE A 97 1 N VAL A 93 O VAL A 27
SHEET 5 A 7 ILE A 116 LEU A 122 1 N ALA A 117 O ALA A 92
SHEET 6 A 7 PRO A 219 GLY A 225 1 N PRO A 219 O VAL A 119
SHEET 7 A 7 GLU A 248 VAL A 252 1 N GLU A 248 O ILE A 222
SHEET 1 B 2 PHE A 2 GLU A 8 0
SHEET 2 B 2 THR A 11 TYR A 16 -1 N LEU A 15 O ILE A 3
SHEET 1 C 7 TYR B 17 GLY B 21 0
SHEET 2 C 7 ARG B 52 TYR B 56 -1 N THR B 55 O GLU B 18
SHEET 3 C 7 PRO B 25 ILE B 29 1 N VAL B 26 O ARG B 52
SHEET 4 C 7 ALA B 92 PHE B 97 1 N VAL B 93 O VAL B 27
SHEET 5 C 7 ILE B 116 LEU B 122 1 N ALA B 117 O ALA B 92
SHEET 6 C 7 PRO B 219 GLY B 225 1 N PRO B 219 O VAL B 119
SHEET 7 C 7 GLU B 248 VAL B 252 1 N GLU B 248 O ILE B 222
SHEET 1 D 2 PHE B 2 GLU B 8 0
SHEET 2 D 2 THR B 11 TYR B 16 -1 N LEU B 15 O ILE B 3
CISPEP 1 PHE A 32 PRO A 33 0 -7.21
CISPEP 2 GLU A 126 PRO A 127 0 3.46
CISPEP 3 PHE B 32 PRO B 33 0 -11.93
CISPEP 4 GLU B 126 PRO B 127 0 3.12
SITE 1 NUA 3 SER A 98 ASP A 228 HIS A 257
SITE 1 NUB 3 SER B 98 ASP B 228 HIS B 257
CRYST1 124.870 124.870 124.870 90.00 90.00 90.00 P 21 3 24
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 0.008008 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008008 0.00000
MTRIX1 1 0.337597 -0.723701 -0.601901 74.69800 1
MTRIX2 1 0.721281 0.609746 -0.328578 49.79800 1
MTRIX3 1 0.604799 -0.323213 0.727840 -12.76600 1 |