HEADER HYDROLASE 11-JUL-06 2HM7
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE G84S EST2 MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALICYCLOBACILLUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_TAXID: 405212;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7SCII
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MENCHISE,V.ALTERIO,G.DE SIMONE
REVDAT 6 30-AUG-23 2HM7 1 REMARK
REVDAT 5 20-OCT-21 2HM7 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2HM7 1 VERSN
REVDAT 3 06-MAY-08 2HM7 1 JRNL
REVDAT 2 01-APR-08 2HM7 1 JRNL VERSN
REVDAT 1 26-JUN-07 2HM7 0
JRNL AUTH L.MANDRICH,V.MENCHISE,V.ALTERIO,G.DE SIMONE,C.PEDONE,
JRNL AUTH 2 M.ROSSI,G.MANCO
JRNL TITL FUNCTIONAL AND STRUCTURAL FEATURES OF THE OXYANION HOLE IN A
JRNL TITL 2 THERMOPHILIC ESTERASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS.
JRNL REF PROTEINS V. 71 1721 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 18076040
JRNL DOI 10.1002/PROT.21877
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.DE SIMONE,S.GALDIERO,G.MANCO,D.LANG,M.ROSSI,C.PEDONE
REMARK 1 TITL A SNAPSHOT OF THE TRANSITION STATE ANALOGUE OF A NOVEL
REMARK 1 TITL 2 THERMOPHILIC ESTERASE BELONGING TO THE SUBFAMILY OF
REMARK 1 TITL 3 MAMMALIAN HORMONE-SENSITIVE LIPASE
REMARK 1 REF J.MOL.BIOL. V. 303 761 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 17482
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) : 0.196
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 882
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2414
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038507.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17662
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.13700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EVQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 8000, 0.1M TRIS/HCL, 0.2M
REMARK 280 MAGNESIUM CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 31.83000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.83000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.08500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 82.17000
REMARK 350 BIOMT3 2 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 PRO A 2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ASP A 12
REMARK 475 GLN A 13
REMARK 475 ASN A 15
REMARK 475 ARG A 16
REMARK 475 ALA A 19
REMARK 475 PRO A 20
REMARK 475 GLU A 198
REMARK 475 GLY A 203
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 3 CD1 CD2
REMARK 480 PRO A 5 CB CG CD
REMARK 480 GLN A 8 CB CG CD OE1 NE2
REMARK 480 GLN A 9 CB CG CD OE1 NE2
REMARK 480 VAL A 10 CB CG1 CG2
REMARK 480 LEU A 14 CB CG CD1 CD2
REMARK 480 MET A 17 SD CE
REMARK 480 ASP A 21 CB CG OD1 OD2
REMARK 480 LYS A 23 CG CD CE NZ
REMARK 480 GLN A 28 CG CD OE1 NE2
REMARK 480 GLN A 33 CG CD OE1 NE2
REMARK 480 LEU A 36 CB CG CD1 CD2
REMARK 480 GLU A 68 CG CD OE1 OE2
REMARK 480 GLU A 71 CB CG CD OE1 OE2
REMARK 480 GLU A 126 CD OE1 OE2
REMARK 480 GLU A 199 CG CD OE1 OE2
REMARK 480 ALA A 201 CB
REMARK 480 GLU A 202 CB CG CD OE1 OE2
REMARK 480 LEU A 205 CG CD1 CD2
REMARK 480 LEU A 212 CG CD1 CD2
REMARK 480 LYS A 259 CE NZ
REMARK 480 LYS A 271 CD CE NZ
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 PRO A 5 -70.79 -40.53
REMARK 500 PRO A 18 -174.85 -66.92
REMARK 500 ASP A 21 79.75 -55.86
REMARK 500 TRP A 85 -0.09 62.59
REMARK 500 SER A 155 -122.64 56.77
REMARK 500 TYR A 183 57.74 32.52
REMARK 500 HIS A 192 51.58 -152.04
REMARK 500 ASN A 200 31.93 -95.99
REMARK 500 LEU A 205 -67.31 73.57
REMARK 500 SER A 231 78.77 -119.92
REMARK 500 SER A 289 -12.29 80.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 455
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EVQ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE CARBOXYLESTERASE EST2 FROM
REMARK 900 ALICYCLOBACILLUS ACIDOCALDARIUS
DBREF 2HM7 A 1 310 UNP Q7SIG1 Q7SIG1_ALIAC 1 310
SEQADV 2HM7 SER A 84 UNP Q7SIG1 GLY 84 ENGINEERED MUTATION
SEQRES 1 A 310 MET PRO LEU ASP PRO VAL ILE GLN GLN VAL LEU ASP GLN
SEQRES 2 A 310 LEU ASN ARG MET PRO ALA PRO ASP TYR LYS HIS LEU SER
SEQRES 3 A 310 ALA GLN GLN PHE ARG SER GLN GLN SER LEU PHE PRO PRO
SEQRES 4 A 310 VAL LYS LYS GLU PRO VAL ALA GLU VAL ARG GLU PHE ASP
SEQRES 5 A 310 MET ASP LEU PRO GLY ARG THR LEU LYS VAL ARG MET TYR
SEQRES 6 A 310 ARG PRO GLU GLY VAL GLU PRO PRO TYR PRO ALA LEU VAL
SEQRES 7 A 310 TYR TYR HIS GLY GLY SER TRP VAL VAL GLY ASP LEU GLU
SEQRES 8 A 310 THR HIS ASP PRO VAL CYS ARG VAL LEU ALA LYS ASP GLY
SEQRES 9 A 310 ARG ALA VAL VAL PHE SER VAL ASP TYR ARG LEU ALA PRO
SEQRES 10 A 310 GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA TYR ASP
SEQRES 11 A 310 ALA LEU GLN TRP ILE ALA GLU ARG ALA ALA ASP PHE HIS
SEQRES 12 A 310 LEU ASP PRO ALA ARG ILE ALA VAL GLY GLY ASP SER ALA
SEQRES 13 A 310 GLY GLY ASN LEU ALA ALA VAL THR SER ILE LEU ALA LYS
SEQRES 14 A 310 GLU ARG GLY GLY PRO ALA LEU ALA PHE GLN LEU LEU ILE
SEQRES 15 A 310 TYR PRO SER THR GLY TYR ASP PRO ALA HIS PRO PRO ALA
SEQRES 16 A 310 SER ILE GLU GLU ASN ALA GLU GLY TYR LEU LEU THR GLY
SEQRES 17 A 310 GLY MET MET LEU TRP PHE ARG ASP GLN TYR LEU ASN SER
SEQRES 18 A 310 LEU GLU GLU LEU THR HIS PRO TRP PHE SER PRO VAL LEU
SEQRES 19 A 310 TYR PRO ASP LEU SER GLY LEU PRO PRO ALA TYR ILE ALA
SEQRES 20 A 310 THR ALA GLN TYR ASP PRO LEU ARG ASP VAL GLY LYS LEU
SEQRES 21 A 310 TYR ALA GLU ALA LEU ASN LYS ALA GLY VAL LYS VAL GLU
SEQRES 22 A 310 ILE GLU ASN PHE GLU ASP LEU ILE HIS GLY PHE ALA GLN
SEQRES 23 A 310 PHE TYR SER LEU SER PRO GLY ALA THR LYS ALA LEU VAL
SEQRES 24 A 310 ARG ILE ALA GLU LYS LEU ARG ASP ALA LEU ALA
HET SO4 A 455 4
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *162(H2 O)
HELIX 1 1 ASP A 4 ARG A 16 1 13
HELIX 2 2 ASP A 21 LEU A 25 5 5
HELIX 3 3 SER A 26 GLN A 34 1 9
HELIX 4 4 HIS A 93 ARG A 105 1 13
HELIX 5 5 PRO A 122 ARG A 138 1 17
HELIX 6 6 ALA A 139 PHE A 142 5 4
HELIX 7 7 SER A 155 ARG A 171 1 17
HELIX 8 8 PRO A 194 ASN A 200 1 7
HELIX 9 9 THR A 207 LEU A 219 1 13
HELIX 10 10 SER A 221 HIS A 227 5 7
HELIX 11 11 SER A 231 TYR A 235 5 5
HELIX 12 12 LEU A 254 ALA A 268 1 15
HELIX 13 13 GLY A 283 TYR A 288 5 6
HELIX 14 14 SER A 291 ALA A 310 1 20
SHEET 1 A 8 GLU A 47 LEU A 55 0
SHEET 2 A 8 ARG A 58 ARG A 66 -1 O MET A 64 N ARG A 49
SHEET 3 A 8 VAL A 107 VAL A 111 -1 O VAL A 108 N TYR A 65
SHEET 4 A 8 TYR A 74 TYR A 80 1 N TYR A 79 O PHE A 109
SHEET 5 A 8 LEU A 144 ASP A 154 1 O ARG A 148 N ALA A 76
SHEET 6 A 8 GLN A 179 ILE A 182 1 O LEU A 180 N VAL A 151
SHEET 7 A 8 ALA A 244 TYR A 251 1 O TYR A 245 N LEU A 181
SHEET 8 A 8 VAL A 272 ILE A 281 1 O GLU A 273 N ILE A 246
LINK OG SER A 155 S SO4 A 455 1555 1555 1.48
CISPEP 1 PHE A 37 PRO A 38 0 -0.07
CISPEP 2 PRO A 72 PRO A 73 0 -0.27
CISPEP 3 ALA A 116 PRO A 117 0 0.10
CISPEP 4 PHE A 121 PRO A 122 0 0.31
CISPEP 5 GLY A 173 PRO A 174 0 0.05
SITE 1 AC1 8 GLY A 83 SER A 84 SER A 155 ALA A 156
SITE 2 AC1 8 HIS A 282 HOH A 513 HOH A 523 HOH A 547
CRYST1 63.660 82.170 47.960 90.00 90.00 90.00 P 21 21 2 4
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 0.015708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012170 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020851 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
