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HEADER HALOPEROXIDASE 01-JUN-96 1BRO
TITLE BROMOPEROXIDASE A2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMOPEROXIDASE A2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HALOPEROXIDASE A2, CHLOROPEROXIDASE A2;
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS;
SOURCE 3 ATCC: 10762;
SOURCE 4 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: TK64;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PIJ486;
SOURCE 7 EXPRESSION_SYSTEM_GENE: BPOA2
KEYWDS ANTIBIOTIC BIOSYNTHESIS, OXIDOREDUCTASE, PEROXIDASE,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, HALOPEROXIDASE
EXPDTA X-RAY DIFFRACTION, SINGLE CRYSTAL
AUTHOR H.J.HECHT,H.SOBEK,T.HAAG,O.PFEIFER,K.H.VAN PEE
REVDAT 1 07-DEC-96 1BRO 0
JRNL AUTH H.J.HECHT,H.SOBEK,T.HAAG,O.PFEIFER,K.H.VAN PEE
JRNL TITL THE METAL-ION-FREE OXIDOREDUCTASE FROM STREPTOMYCES
JRNL TITL 2 AUREOFACIENS HAS AN ALPHA/BETA HYDROLASE FOLD
JRNL REF NAT.STRUCT.BIOL. V. 1 532 1994
JRNL REFN ASTM NSBIEW US ISSN 1072-8368 2024
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.H.VAN PEE,H.J.HECHT,T.HAAG,O.PFEIFER,R.BANTLEON,
REMARK 1 AUTH 2 H.SOBEK,I.PELLETIER,J.ALTENBUCHNER
REMARK 1 TITL REACTION MECHANISM AND 3-DIMENSIONAL STRUCTURE OF
REMARK 1 TITL 2 BACTERIAL NON-HAEM HALOPEROXIDASES
REMARK 1 EDIT A.GRIMVALL,E.W.B.DE LEER
REMARK 1 REF NATURALLY-PRODUCED 193 1995
REMARK 1 REF 2 ORGANOHALOGENS (IN:
REMARK 1 REF 3 ENVIRONMENT & CHEMISTRY,
REMARK 1 REF 4 V.1)
REMARK 1 PUBL DORDRECHT : KLUWER ACADEMIC PUBLISHERS
REMARK 1 REFN ISBN 0792334353 2092
REMARK 1 REFERENCE 2
REMARK 1 AUTH O.PFEIFER,I.PELLETIER,J.ALTENBUCHNER,K.H.VAN PEE
REMARK 1 TITL MOLECULAR CLONING AND SEQUENCING OF A NON-HAEM
REMARK 1 TITL 2 BROMOPEROXIDASE GENE FROM STREPTOMYCES AUREOFACIENS
REMARK 1 TITL 3 ATCC 10762
REMARK 1 REF J.GEN.MICROBIOL. V. 138 1123 1992
REMARK 1 REFN ASTM JGMIAN UK ISSN 0022-1287 0775
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 41321
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.184
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4294
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.84
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.021 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.058 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.058 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.015 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.174 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.183 ; 0.30
REMARK 3 MULTIPLE TORSION (A) : 0.267 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : 0.169 ; 0.30
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.579 ; 3.00
REMARK 3 STAGGERED (DEGREES) : 15.433; 15.00
REMARK 3 TRANSVERSE (DEGREES) : 29.657; 20.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.999 ; 1.00
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.595 ; 1.50
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.508 ; 1.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.057 ; 1.50
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CCP4 DISTRIBUTED DICT.DAT FOR
REMARK 3 PROLSQ.
REMARK 3 FINAL RMS COORD. SHIFT 0.0120 ANGSTROMS
REMARK 4
REMARK 4 1BRO COMPLIES WITH FORMAT V. 2.1, 25-OCT-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-1993
REMARK 200 TEMPERATURE (KELVIN) : 263
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : X-100
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : CCP4 AGROVATA/ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45014
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.99
REMARK 200 RESOLUTION RANGE LOW (A) : 44.7
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.080
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) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 1.99
REMARK 200 DATA REDUNDANCY IN SHELL : 2.05
REMARK 200 R MERGE FOR SHELL (I) : 0.284
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.11
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
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): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE
REMARK 280 PH 8.0.
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 63.25111
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.25111
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.25111
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.25111
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.25111
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.25111
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 63.25111
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 63.25111
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 63.25111
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 63.25111
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 63.25111
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 63.25111
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 63.25111
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 63.25111
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 63.25111
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 63.25111
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 63.25111
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 63.25111
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 B 1 .. 277 A 1 .. 277 0.292
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THE BIOLOGICALLY FUNCTIONAL MOLECULE IS A TRIMER
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 5 0.000000 0.000000 -1.000000 63.25111
REMARK 350 BIOMT2 5 -1.000000 0.000000 0.000000 126.50221
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 -63.25111
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 6 0.000000 -1.000000 0.000000 126.50221
REMARK 350 BIOMT2 6 0.000000 0.000000 1.000000 63.25111
REMARK 350 BIOMT3 6 -1.000000 0.000000 0.000000 63.25111
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: BCT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
DBREF 1BRO A 1 277 SWS P29715 BPA2_STRAU 1 277
DBREF 1BRO B 1 277 SWS P29715 BPA2_STRAU 1 277
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 THR 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 GLN 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 THR 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 GLN 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
FORMUL 3 HOH *235(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 GLN A 142 ALA A 154 1 13
HELIX 5 5 ARG A 156 TYR A 168 1 13
HELIX 6 6 LEU A 170 ASN A 173 1 4
HELIX 7 7 GLU A 180 ALA A 191 1 12
HELIX 8 8 PHE A 195 THR A 204 1 10
HELIX 9 9 ILE A 213 ARG A 215 5 3
HELIX 10 10 ALA A 237 ALA A 243 1 7
HELIX 11 11 LEU A 259 THR A 262 1 4
HELIX 12 12 ALA A 264 ALA A 276 1 13
HELIX 13 13 GLY B 36 ASP B 48 5 13
HELIX 14 14 TYR B 73 LEU B 87 1 15
HELIX 15 15 SER B 98 TYR B 111 5 14
HELIX 16 16 GLN B 142 ALA B 154 1 13
HELIX 17 17 ARG B 156 PHE B 167 1 12
HELIX 18 18 LEU B 170 ASN B 173 1 4
HELIX 19 19 GLU B 180 ALA B 191 1 12
HELIX 20 20 PHE B 195 THR B 204 1 10
HELIX 21 21 ARG B 210 ARG B 215 1 6
HELIX 22 22 ALA B 237 ALA B 243 1 7
HELIX 23 23 LEU B 259 THR B 262 1 4
HELIX 24 24 ALA B 264 LEU B 275 1 12
SHEET 1 A 7 TYR A 17 HIS A 20 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 7 TYR B 17 HIS B 20 0
SHEET 2 B 7 ARG B 52 TYR B 56 -1 N THR B 55 O GLU B 18
SHEET 3 B 7 PRO B 25 ILE B 29 1 N VAL B 26 O ARG B 52
SHEET 4 B 7 ALA B 92 PHE B 97 1 N VAL B 93 O VAL B 27
SHEET 5 B 7 ILE B 116 LEU B 122 1 N ALA B 117 O ALA B 92
SHEET 6 B 7 PRO B 219 GLY B 225 1 N PRO B 219 O VAL B 119
SHEET 7 B 7 GLU B 248 VAL B 252 1 N GLU B 248 O ILE B 222
SHEET 1 C 2 PHE A 2 GLU A 8 0
SHEET 2 C 2 THR A 11 TYR A 16 -1 N LEU A 15 O ILE A 3
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 -3.72
CISPEP 2 GLU A 126 PRO A 127 0 1.88
CISPEP 3 PHE B 32 PRO B 33 0 -3.46
CISPEP 4 GLU B 126 PRO B 127 0 1.25
SITE 1 ACT 3 SER A 98 ASP A 228 HIS A 257
SITE 1 BCT 3 SER B 98 ASP B 228 HIS B 257
CRYST1 126.500 126.500 126.500 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 0.007905 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007905 0.00000
MTRIX1 1 0.338640 0.724930 0.599830 -54.00097 1
MTRIX2 1 -0.724980 0.607390 -0.324780 20.21999 1
MTRIX3 1 -0.599770 -0.324880 0.731250 71.15529 1 |