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HEADER HALOPEROXIDASE 03-APR-98 1A88
TITLE CHLOROPEROXIDASE L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPEROXIDASE L;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: BROMOPEROXIDASE L, HALOPEROXIDASE L;
COMPND 5 EC: 1.11.1.10;
COMPND 6 ENGINEERED: YES;
COMPND 7 BIOLOGICAL_UNIT: HOMODIMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 3 STRAIN: TK64;
SOURCE 4 GENE: CPO-L;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES AUREOFACIENS;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TUE24-88;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRB882;
SOURCE 9 EXPRESSION_SYSTEM_GENE: CPO-L
KEYWDS HALOPEROXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.HOFMANN,S.TOELZER,I.PELLETIER,J.ALTENBUCHNER,K.-H.VAN PEE,
AUTHOR 2 H.-J.HECHT
REVDAT 1 14-OCT-98 1A88 0
JRNL AUTH B.HOFMANN,S.TOLZER,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. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 130.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 3 NUMBER OF REFLECTIONS : 65934
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5
REMARK 3 FREE R VALUE TEST SET COUNT : 3325
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6315
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 507
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.4
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.029 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.035 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.024 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.135 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.174 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.249 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : 0.118 ; 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) : 3.9 ; 7.00
REMARK 3 STAGGERED (DEGREES) : 16.6 ; 15.00
REMARK 3 TRANSVERSE (DEGREES) : 34.9 ; 20.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.26 ; 2.00
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.78 ; 3.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.55 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.09 ; 3.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A88 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 : MAR-1995
REMARK 200 TEMPERATURE (KELVIN) : 283
REMARK 200 PH : 8.2
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 : 65934
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 44.2
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 200 DATA REDUNDANCY : 2.0
REMARK 200 R MERGE (I) : 0.078
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.5
REMARK 200 R MERGE FOR SHELL (I) : 0.205
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.2
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1A8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.3
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE 100MM
REMARK 280 TRIS/HCL PH 8.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 1/2+X,1/2+Y,1/2+Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-Y,1/2+X,1/2+Z
REMARK 290 8555 1/2+Y,1/2-X,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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 88.24568
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 88.24568
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 32.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 88.24568
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 88.24568
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 88.24568
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 88.24568
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 32.00000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 88.24568
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 88.24568
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 32.00000
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 .. 275 B 1 .. 275 0.214
REMARK 295 M 2 A 1 .. 275 C 1 .. 275 0.256
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: CTA
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD, CHAIN A.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD, CHAIN B.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTC
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD, CHAIN C.
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 14-APR-1998 TRACKING NUMBER: T14842
DBREF 1A88 A 1 275 SWS P49323 PRXC_STRLI 1 275
DBREF 1A88 B 1 275 SWS P49323 PRXC_STRLI 1 275
DBREF 1A88 C 1 275 SWS P49323 PRXC_STRLI 1 275
SEQADV 1A88 ASP A 169 SWS P49323 ASN 169 CONFLICT
SEQADV 1A88 ASP B 169 SWS P49323 ASN 169 CONFLICT
SEQADV 1A88 ASP C 169 SWS P49323 ASN 169 CONFLICT
SEQRES 1 A 275 GLY THR VAL THR THR SER ASP GLY THR ASN ILE PHE TYR
SEQRES 2 A 275 LYS ASP TRP GLY PRO ARG ASP GLY LEU PRO VAL VAL PHE
SEQRES 3 A 275 HIS HIS GLY TRP PRO LEU SER ALA ASP ASP TRP ASP ASN
SEQRES 4 A 275 GLN MET LEU PHE PHE LEU SER HIS GLY TYR ARG VAL ILE
SEQRES 5 A 275 ALA HIS ASP ARG ARG GLY HIS GLY ARG SER ASP GLN PRO
SEQRES 6 A 275 SER THR GLY HIS ASP MET ASP THR TYR ALA ALA ASP VAL
SEQRES 7 A 275 ALA ALA LEU THR GLU ALA LEU ASP LEU ARG GLY ALA VAL
SEQRES 8 A 275 HIS ILE GLY HIS SER THR GLY GLY GLY GLU VAL ALA ARG
SEQRES 9 A 275 TYR VAL ALA ARG ALA GLU PRO GLY ARG VAL ALA LYS ALA
SEQRES 10 A 275 VAL LEU VAL SER ALA VAL PRO PRO VAL MET VAL LYS SER
SEQRES 11 A 275 ASP THR ASN PRO ASP GLY LEU PRO LEU GLU VAL PHE ASP
SEQRES 12 A 275 GLU PHE ARG ALA ALA LEU ALA ALA ASN ARG ALA GLN PHE
SEQRES 13 A 275 TYR ILE ASP VAL PRO SER GLY PRO PHE TYR GLY PHE ASN
SEQRES 14 A 275 ARG GLU GLY ALA THR VAL SER GLN GLY LEU ILE ASP HIS
SEQRES 15 A 275 TRP TRP LEU GLN GLY MET MET GLY ALA ALA ASN ALA HIS
SEQRES 16 A 275 TYR GLU CYS ILE ALA ALA PHE SER GLU THR ASP PHE THR
SEQRES 17 A 275 ASP ASP LEU LYS ARG ILE ASP VAL PRO VAL LEU VAL ALA
SEQRES 18 A 275 HIS GLY THR ASP ASP GLN VAL VAL PRO TYR ALA ASP ALA
SEQRES 19 A 275 ALA PRO LYS SER ALA GLU LEU LEU ALA ASN ALA THR LEU
SEQRES 20 A 275 LYS SER TYR GLU GLY LEU PRO HIS GLY MET LEU SER THR
SEQRES 21 A 275 HIS PRO GLU VAL LEU ASN PRO ASP LEU LEU ALA PHE VAL
SEQRES 22 A 275 LYS SER
SEQRES 1 B 275 GLY THR VAL THR THR SER ASP GLY THR ASN ILE PHE TYR
SEQRES 2 B 275 LYS ASP TRP GLY PRO ARG ASP GLY LEU PRO VAL VAL PHE
SEQRES 3 B 275 HIS HIS GLY TRP PRO LEU SER ALA ASP ASP TRP ASP ASN
SEQRES 4 B 275 GLN MET LEU PHE PHE LEU SER HIS GLY TYR ARG VAL ILE
SEQRES 5 B 275 ALA HIS ASP ARG ARG GLY HIS GLY ARG SER ASP GLN PRO
SEQRES 6 B 275 SER THR GLY HIS ASP MET ASP THR TYR ALA ALA ASP VAL
SEQRES 7 B 275 ALA ALA LEU THR GLU ALA LEU ASP LEU ARG GLY ALA VAL
SEQRES 8 B 275 HIS ILE GLY HIS SER THR GLY GLY GLY GLU VAL ALA ARG
SEQRES 9 B 275 TYR VAL ALA ARG ALA GLU PRO GLY ARG VAL ALA LYS ALA
SEQRES 10 B 275 VAL LEU VAL SER ALA VAL PRO PRO VAL MET VAL LYS SER
SEQRES 11 B 275 ASP THR ASN PRO ASP GLY LEU PRO LEU GLU VAL PHE ASP
SEQRES 12 B 275 GLU PHE ARG ALA ALA LEU ALA ALA ASN ARG ALA GLN PHE
SEQRES 13 B 275 TYR ILE ASP VAL PRO SER GLY PRO PHE TYR GLY PHE ASN
SEQRES 14 B 275 ARG GLU GLY ALA THR VAL SER GLN GLY LEU ILE ASP HIS
SEQRES 15 B 275 TRP TRP LEU GLN GLY MET MET GLY ALA ALA ASN ALA HIS
SEQRES 16 B 275 TYR GLU CYS ILE ALA ALA PHE SER GLU THR ASP PHE THR
SEQRES 17 B 275 ASP ASP LEU LYS ARG ILE ASP VAL PRO VAL LEU VAL ALA
SEQRES 18 B 275 HIS GLY THR ASP ASP GLN VAL VAL PRO TYR ALA ASP ALA
SEQRES 19 B 275 ALA PRO LYS SER ALA GLU LEU LEU ALA ASN ALA THR LEU
SEQRES 20 B 275 LYS SER TYR GLU GLY LEU PRO HIS GLY MET LEU SER THR
SEQRES 21 B 275 HIS PRO GLU VAL LEU ASN PRO ASP LEU LEU ALA PHE VAL
SEQRES 22 B 275 LYS SER
SEQRES 1 C 275 GLY THR VAL THR THR SER ASP GLY THR ASN ILE PHE TYR
SEQRES 2 C 275 LYS ASP TRP GLY PRO ARG ASP GLY LEU PRO VAL VAL PHE
SEQRES 3 C 275 HIS HIS GLY TRP PRO LEU SER ALA ASP ASP TRP ASP ASN
SEQRES 4 C 275 GLN MET LEU PHE PHE LEU SER HIS GLY TYR ARG VAL ILE
SEQRES 5 C 275 ALA HIS ASP ARG ARG GLY HIS GLY ARG SER ASP GLN PRO
SEQRES 6 C 275 SER THR GLY HIS ASP MET ASP THR TYR ALA ALA ASP VAL
SEQRES 7 C 275 ALA ALA LEU THR GLU ALA LEU ASP LEU ARG GLY ALA VAL
SEQRES 8 C 275 HIS ILE GLY HIS SER THR GLY GLY GLY GLU VAL ALA ARG
SEQRES 9 C 275 TYR VAL ALA ARG ALA GLU PRO GLY ARG VAL ALA LYS ALA
SEQRES 10 C 275 VAL LEU VAL SER ALA VAL PRO PRO VAL MET VAL LYS SER
SEQRES 11 C 275 ASP THR ASN PRO ASP GLY LEU PRO LEU GLU VAL PHE ASP
SEQRES 12 C 275 GLU PHE ARG ALA ALA LEU ALA ALA ASN ARG ALA GLN PHE
SEQRES 13 C 275 TYR ILE ASP VAL PRO SER GLY PRO PHE TYR GLY PHE ASN
SEQRES 14 C 275 ARG GLU GLY ALA THR VAL SER GLN GLY LEU ILE ASP HIS
SEQRES 15 C 275 TRP TRP LEU GLN GLY MET MET GLY ALA ALA ASN ALA HIS
SEQRES 16 C 275 TYR GLU CYS ILE ALA ALA PHE SER GLU THR ASP PHE THR
SEQRES 17 C 275 ASP ASP LEU LYS ARG ILE ASP VAL PRO VAL LEU VAL ALA
SEQRES 18 C 275 HIS GLY THR ASP ASP GLN VAL VAL PRO TYR ALA ASP ALA
SEQRES 19 C 275 ALA PRO LYS SER ALA GLU LEU LEU ALA ASN ALA THR LEU
SEQRES 20 C 275 LYS SER TYR GLU GLY LEU PRO HIS GLY MET LEU SER THR
SEQRES 21 C 275 HIS PRO GLU VAL LEU ASN PRO ASP LEU LEU ALA PHE VAL
SEQRES 22 C 275 LYS SER
FORMUL 4 HOH *507(H2 O1)
HELIX 1 1 ALA A 34 HIS A 47 5 14
HELIX 2 2 MET A 71 LEU A 85 1 15
HELIX 3 3 SER A 96 ARG A 108 5 13
HELIX 4 4 LEU A 139 ALA A 151 1 13
HELIX 5 5 ARG A 153 SER A 162 1 10
HELIX 6 6 GLN A 177 MET A 189 1 13
HELIX 7 7 ALA A 192 GLU A 204 1 13
HELIX 8 8 THR A 208 ARG A 213 1 6
HELIX 9 9 ALA A 235 LEU A 241 1 7
HELIX 10 10 MET A 257 THR A 260 1 4
HELIX 11 11 PRO A 262 VAL A 273 1 12
HELIX 12 12 ALA B 34 HIS B 47 5 14
HELIX 13 13 MET B 71 LEU B 85 1 15
HELIX 14 14 SER B 96 ARG B 108 5 13
HELIX 15 15 LEU B 139 ALA B 151 1 13
HELIX 16 16 ARG B 153 SER B 162 1 10
HELIX 17 17 GLN B 177 MET B 189 1 13
HELIX 18 18 ALA B 192 GLU B 204 1 13
HELIX 19 19 THR B 208 ARG B 213 1 6
HELIX 20 20 ALA B 235 LEU B 241 1 7
HELIX 21 21 MET B 257 THR B 260 1 4
HELIX 22 22 PRO B 262 VAL B 273 1 12
HELIX 23 23 ALA C 34 HIS C 47 5 14
HELIX 24 24 MET C 71 LEU C 85 1 15
HELIX 25 25 SER C 96 ARG C 108 5 13
HELIX 26 26 LEU C 139 ALA C 151 1 13
HELIX 27 27 ARG C 153 SER C 162 1 10
HELIX 28 28 GLN C 177 MET C 189 1 13
HELIX 29 29 ALA C 192 GLU C 204 1 13
HELIX 30 30 THR C 208 ARG C 213 1 6
HELIX 31 31 ALA C 235 LEU C 241 1 7
HELIX 32 32 MET C 257 THR C 260 1 4
HELIX 33 33 PRO C 262 VAL C 273 1 12
SHEET 1 A 2 THR A 2 THR A 4 0
SHEET 2 A 2 ASN A 10 PHE A 12 -1 N ILE A 11 O VAL A 3
SHEET 1 B 7 TYR A 13 TRP A 16 0
SHEET 2 B 7 ARG A 50 HIS A 54 -1 N ALA A 53 O LYS A 14
SHEET 3 B 7 PRO A 23 HIS A 27 1 N VAL A 24 O ARG A 50
SHEET 4 B 7 ALA A 90 HIS A 95 1 N VAL A 91 O VAL A 25
SHEET 5 B 7 VAL A 114 VAL A 120 1 N ALA A 115 O ALA A 90
SHEET 6 B 7 PRO A 217 GLY A 223 1 N PRO A 217 O ALA A 117
SHEET 7 B 7 ALA A 245 TYR A 250 1 N THR A 246 O VAL A 218
SHEET 1 C 2 THR B 2 THR B 4 0
SHEET 2 C 2 ASN B 10 PHE B 12 -1 N ILE B 11 O VAL B 3
SHEET 1 D 7 TYR B 13 TRP B 16 0
SHEET 2 D 7 ARG B 50 HIS B 54 -1 N ALA B 53 O LYS B 14
SHEET 3 D 7 PRO B 23 HIS B 27 1 N VAL B 24 O ARG B 50
SHEET 4 D 7 ALA B 90 HIS B 95 1 N VAL B 91 O VAL B 25
SHEET 5 D 7 VAL B 114 VAL B 120 1 N ALA B 115 O ALA B 90
SHEET 6 D 7 PRO B 217 GLY B 223 1 N PRO B 217 O ALA B 117
SHEET 7 D 7 ALA B 245 TYR B 250 1 N THR B 246 O VAL B 218
SHEET 1 E 2 THR C 2 THR C 4 0
SHEET 2 E 2 ASN C 10 PHE C 12 -1 N ILE C 11 O VAL C 3
SHEET 1 F 7 TYR C 13 TRP C 16 0
SHEET 2 F 7 ARG C 50 HIS C 54 -1 N ALA C 53 O LYS C 14
SHEET 3 F 7 PRO C 23 HIS C 27 1 N VAL C 24 O ARG C 50
SHEET 4 F 7 ALA C 90 HIS C 95 1 N VAL C 91 O VAL C 25
SHEET 5 F 7 VAL C 114 VAL C 120 1 N ALA C 115 O ALA C 90
SHEET 6 F 7 PRO C 217 GLY C 223 1 N PRO C 217 O ALA C 117
SHEET 7 F 7 ALA C 245 TYR C 250 1 N THR C 246 O VAL C 218
CISPEP 1 TRP A 30 PRO A 31 0 -7.15
CISPEP 2 PRO A 124 PRO A 125 0 -2.14
CISPEP 3 TRP B 30 PRO B 31 0 -5.24
CISPEP 4 PRO B 124 PRO B 125 0 2.62
CISPEP 5 TRP C 30 PRO C 31 0 -7.83
CISPEP 6 PRO C 124 PRO C 125 0 3.15
SITE 1 CTA 3 SER A 96 ASP A 226 HIS A 255
SITE 1 CTB 3 SER B 96 ASP B 226 HIS B 255
SITE 1 CTC 3 SER C 96 ASP C 226 HIS C 255
CRYST1 176.500 176.500 64.000 90.00 90.00 90.00 I 4 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 0.005666 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015625 0.00000
MTRIX1 1 -0.311822 -0.852843 -0.418837 70.96638 1
MTRIX2 1 0.024857 0.433343 -0.900886 14.80369 1
MTRIX3 1 0.949815 -0.291327 -0.113927 -25.69099 1
MTRIX1 2 -0.312554 0.020945 0.949669 46.42327 1
MTRIX2 2 -0.860924 0.416218 -0.292526 47.53159 1
MTRIX3 2 -0.401396 -0.909024 -0.112059 40.50269 1 |