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HEADER HYDROLASE 27-NOV-06 2E3J
TITLE THE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE B (RV1938) FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS AT 2.1 ANGSTROM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE EPHB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EPOXIDE HYDROLASE B, EPOXIDE HYDRATASE, EPOXIDE
COMPND 5 HYDROLASE;
COMPND 6 EC: 3.3.2.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 (AI);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS EPOXIDE HYDROLASE B, MYCOBACTERIUM TUBERCULOSIS, X-RAY
KEYWDS 2 CRYSTALLOGRAPHY, STRUCTURAL GENOMICS, MYCOBACTERIUM
KEYWDS 3 TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT, XMTB
EXPDTA X-RAY DIFFRACTION
AUTHOR B.K.BISWAL,MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS
AUTHOR 2 PROJECT (XMTB)
REVDAT 1 04-DEC-07 2E3J 0
JRNL AUTH B.K.BISWAL,G.GAREN,M.M.CHERNEY,C.GAREN,M.N.JAMES
JRNL TITL THE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE B
JRNL TITL 2 (RV1938) FROM MYCOBACTERIUM TUBERCULOSIS AT 2.1
JRNL TITL 3 ANGSTROM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.28
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) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 20701
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1038
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3900
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2708
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.28000
REMARK 3 B22 (A**2) : 12.28000
REMARK 3 B33 (A**2) : -24.57000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.26
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 2E3J COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB026179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115869
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 : 20701
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 39.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49200
REMARK 200 FOR SHELL : 2.100
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 245-541 (C-TREMINAL DOMAIN) OF PDB ID
REMARK 200 1EK1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% 2-PROPANOL, 0.2M CACL2, 0.1M
REMARK 280 SODIUM ACETATE BUFFER, PROTEIN CONCENTRATION 5-10MG/ML, PH
REMARK 280 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-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 78.55450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.12900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.12900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.27725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.12900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.12900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.83175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.12900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.12900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.27725
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.12900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.12900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.83175
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 78.55450
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: DIMER
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 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 78.55450
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2091 LIES ON A SPECIAL POSITION.
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 VAL A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 ASP A 207
REMARK 465 ALA A 208
REMARK 465 GLY A 209
REMARK 465 VAL A 210
REMARK 465 ASP A 211
REMARK 465 LEU A 212
REMARK 465 GLU A 213
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 GLU A 38 -155.33 -117.78
REMARK 500 ASP A 104 -127.30 51.54
REMARK 500 SER A 128 -53.91 78.54
REMARK 500 VAL A 136 -59.15 70.56
REMARK 500 LEU A 154 -81.84 -40.57
REMARK 500 LEU A 156 72.05 60.02
REMARK 500 ALA A 157 -7.86 168.39
REMARK 500 PRO A 159 -71.05 -52.43
REMARK 500 ASP A 172 -72.22 -129.99
REMARK 500 ASP A 181 83.63 -161.87
REMARK 500 ALA A 204 39.39 -79.13
REMARK 500 GLU A 230 131.89 -39.02
REMARK 500 ASP A 284 21.19 -63.83
REMARK 500 ASP A 330 -9.37 67.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2084 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A2114 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH A2137 DISTANCE = 5.25 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1938 RELATED DB: TARGETDB
DBREF 2E3J A 2 356 UNP P95276 P95276_MYCTU 2 356
SEQADV 2E3J VAL A 1 UNP P95276 EXPRESSION TAG
SEQRES 1 A 356 VAL SER GLN VAL HIS ARG ILE LEU ASN CYS ARG GLY THR
SEQRES 2 A 356 ARG ILE HIS ALA VAL ALA ASP SER PRO PRO ASP GLN GLN
SEQRES 3 A 356 GLY PRO LEU VAL VAL LEU LEU HIS GLY PHE PRO GLU SER
SEQRES 4 A 356 TRP TYR SER TRP ARG HIS GLN ILE PRO ALA LEU ALA GLY
SEQRES 5 A 356 ALA GLY TYR ARG VAL VAL ALA ILE ASP GLN ARG GLY TYR
SEQRES 6 A 356 GLY ARG SER SER LYS TYR ARG VAL GLN LYS ALA TYR ARG
SEQRES 7 A 356 ILE LYS GLU LEU VAL GLY ASP VAL VAL GLY VAL LEU ASP
SEQRES 8 A 356 SER TYR GLY ALA GLU GLN ALA PHE VAL VAL GLY HIS ASP
SEQRES 9 A 356 TRP GLY ALA PRO VAL ALA TRP THR PHE ALA TRP LEU HIS
SEQRES 10 A 356 PRO ASP ARG CYS ALA GLY VAL VAL GLY ILE SER VAL PRO
SEQRES 11 A 356 PHE ALA GLY ARG GLY VAL ILE GLY LEU PRO GLY SER PRO
SEQRES 12 A 356 PHE GLY GLU ARG ARG PRO SER ASP TYR HIS LEU GLU LEU
SEQRES 13 A 356 ALA GLY PRO GLY ARG VAL TRP TYR GLN ASP TYR PHE ALA
SEQRES 14 A 356 VAL GLN ASP GLY ILE ILE THR GLU ILE GLU GLU ASP LEU
SEQRES 15 A 356 ARG GLY TRP LEU LEU GLY LEU THR TYR THR VAL SER GLY
SEQRES 16 A 356 GLU GLY MET MET ALA ALA THR LYS ALA ALA VAL ASP ALA
SEQRES 17 A 356 GLY VAL ASP LEU GLU SER MET ASP PRO ILE ASP VAL ILE
SEQRES 18 A 356 ARG ALA GLY PRO LEU CYS MET ALA GLU GLY ALA ARG LEU
SEQRES 19 A 356 LYS ASP ALA PHE VAL TYR PRO GLU THR MET PRO ALA TRP
SEQRES 20 A 356 PHE THR GLU ALA ASP LEU ASP PHE TYR THR GLY GLU PHE
SEQRES 21 A 356 GLU ARG SER GLY PHE GLY GLY PRO LEU SER PHE TYR HIS
SEQRES 22 A 356 ASN ILE ASP ASN ASP TRP HIS ASP LEU ALA ASP GLN GLN
SEQRES 23 A 356 GLY LYS PRO LEU THR PRO PRO ALA LEU PHE ILE GLY GLY
SEQRES 24 A 356 GLN TYR ASP VAL GLY THR ILE TRP GLY ALA GLN ALA ILE
SEQRES 25 A 356 GLU ARG ALA HIS GLU VAL MET PRO ASN TYR ARG GLY THR
SEQRES 26 A 356 HIS MET ILE ALA ASP VAL GLY HIS TRP ILE GLN GLN GLU
SEQRES 27 A 356 ALA PRO GLU GLU THR ASN ARG LEU LEU LEU ASP PHE LEU
SEQRES 28 A 356 GLY GLY LEU ARG PRO
HET ACT A2001 4
HET ACT A2002 4
HET ACT A2003 4
HET ACT A2004 4
HET ACT A2005 4
HET ACT A2006 4
HET ACT A2007 4
HET ACT A2008 4
HET ACT A2009 4
HETNAM ACT ACETATE ION
FORMUL 2 ACT 9(C2 H3 O2 1-)
FORMUL 11 HOH *128(H2 O)
HELIX 1 1 SER A 39 ARG A 44 5 6
HELIX 2 2 GLN A 46 ALA A 53 1 8
HELIX 3 3 VAL A 73 TYR A 77 5 5
HELIX 4 4 ARG A 78 TYR A 93 1 16
HELIX 5 5 TRP A 105 HIS A 117 1 13
HELIX 6 6 ALA A 132 VAL A 136 5 5
HELIX 7 7 ARG A 148 GLU A 155 1 8
HELIX 8 8 TYR A 164 GLN A 171 1 8
HELIX 9 9 ASP A 172 GLU A 180 1 9
HELIX 10 10 ASP A 181 VAL A 193 1 13
HELIX 11 11 SER A 194 ALA A 204 1 11
HELIX 12 12 ASP A 216 VAL A 220 5 5
HELIX 13 13 ARG A 233 PHE A 238 5 6
HELIX 14 14 THR A 249 GLY A 264 1 16
HELIX 15 15 PHE A 265 ASN A 274 1 10
HELIX 16 16 ASN A 274 LEU A 282 1 9
HELIX 17 17 ALA A 283 GLN A 286 5 4
HELIX 18 18 ASP A 302 GLY A 308 1 7
HELIX 19 19 GLY A 308 ARG A 314 1 7
HELIX 20 20 ARG A 314 MET A 319 1 6
HELIX 21 21 TRP A 334 ALA A 339 1 6
HELIX 22 22 ALA A 339 GLY A 353 1 15
SHEET 1 A 8 HIS A 5 CYS A 10 0
SHEET 2 A 8 THR A 13 ASP A 20 -1 O THR A 13 N CYS A 10
SHEET 3 A 8 ARG A 56 ILE A 60 -1 O VAL A 57 N ASP A 20
SHEET 4 A 8 LEU A 29 LEU A 33 1 N LEU A 32 O VAL A 58
SHEET 5 A 8 ALA A 98 HIS A 103 1 O VAL A 101 N LEU A 33
SHEET 6 A 8 CYS A 121 ILE A 127 1 O ILE A 127 N GLY A 102
SHEET 7 A 8 ALA A 294 GLY A 299 1 O LEU A 295 N GLY A 126
SHEET 8 A 8 TYR A 322 ILE A 328 1 O ARG A 323 N ALA A 294
SHEET 1 B 2 ARG A 161 TRP A 163 0
SHEET 2 B 2 CYS A 227 ALA A 229 -1 O MET A 228 N VAL A 162
CISPEP 1 PHE A 36 PRO A 37 0 -0.59
CRYST1 66.258 66.258 157.109 90.00 90.00 90.00 P 41 21 2 8
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 0.015093 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006365 0.00000
TER 2709 PRO A 356
MASTER 304 0 9 22 10 0 0 6 2872 1 36 28
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