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HEADER HYDROLASE 07-MAR-08 2ZJF
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS EPOXIDE
TITLE 2 HYDROLASE B COMPLEXED WITH AN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE EPOXIDE HYDROLASE EPHB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EPOXIDE HYDRATASE, EPOXIDE HYDROLASE;
COMPND 5 EC: 3.3.2.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 ATCC: 25618;
SOURCE 6 GENE: EPHB, MT1988, RV1938;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST17_RV1938
KEYWDS X-RAY CRYSTALLOGRAPHY, HYDROLASE FOLD, INHIBITOR, ENZYME
KEYWDS 2 MECHANISM, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC
EXPDTA X-RAY DIFFRACTION
AUTHOR B.K.BISWAL,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 1 01-APR-08 2ZJF 0
JRNL AUTH B.K.BISWAL,C.MORISSEAU,G.GAREN,M.M.CHERNEY,C.GAREN,
JRNL AUTH 2 C.NIU,B.D.HAMMOCK,M.N.G.JAMES
JRNL TITL STRUCTURES OF MYCOBACTERIUM TUBERCULOSIS EPOXIDE
JRNL TITL 2 HYDROLASE B AND ITS COMPLEX WITH A LOW NANOMOLAR
JRNL TITL 3 UREA-BASED INHIBITOR.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 14403
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) : 0.202
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 724
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 117
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2709
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.47000
REMARK 3 B22 (A**2) : 10.47000
REMARK 3 B33 (A**2) : -20.93000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.35
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) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.87
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 2ZJF COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB028047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-2007
REMARK 200 TEMPERATURE (KELVIN) : 105.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14465
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12700
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.57000
REMARK 200 FOR SHELL : 2.400
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: PDB ENTRY 1EK1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ISOPROPANOL, 0.2 M CACL2, 0.1 M
REMARK 280 SODIUM ACETATE BUFFER, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 78.41450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.20750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.20750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.20725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.20750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.20750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.62175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.20750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.20750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.20725
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.20750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.20750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.62175
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 78.41450
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: DIMERIC
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 78.41450
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
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 ASN A 9 73.55 -171.57
REMARK 500 GLU A 38 -155.81 -120.07
REMARK 500 ASP A 104 -126.19 59.89
REMARK 500 SER A 128 -57.05 79.05
REMARK 500 ARG A 134 -8.87 -57.62
REMARK 500 VAL A 136 -60.23 75.19
REMARK 500 LEU A 154 -80.27 -41.42
REMARK 500 LEU A 156 59.32 74.36
REMARK 500 ALA A 157 -14.84 176.52
REMARK 500 PRO A 159 -71.63 -62.60
REMARK 500 ASP A 172 -78.49 -132.13
REMARK 500 ASP A 181 84.27 -168.16
REMARK 500 ALA A 204 46.43 -85.89
REMARK 500 MET A 215 112.32 -175.92
REMARK 500 ASP A 216 105.95 48.72
REMARK 500 ASP A 284 6.76 -67.20
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 A 464 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 470 DISTANCE = 5.06 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 357
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 358
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 359
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BSU BINDING SITE FOR RESIDUE A 360
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1938 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2E3J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE B (RV1938) FROM
REMARK 900 MYCOBACTERIUM TUBERCULOSIS AT 2.1 ANGSTROM RESOLUTION
DBREF 2ZJF A 2 356 UNP P95276 P95276_MYCTU 2 356
SEQADV 2ZJF HIS A -5 UNP P95276 EXPRESSION TAG
SEQADV 2ZJF HIS A -4 UNP P95276 EXPRESSION TAG
SEQADV 2ZJF HIS A -3 UNP P95276 EXPRESSION TAG
SEQADV 2ZJF HIS A -2 UNP P95276 EXPRESSION TAG
SEQADV 2ZJF HIS A -1 UNP P95276 EXPRESSION TAG
SEQADV 2ZJF HIS A 0 UNP P95276 EXPRESSION TAG
SEQADV 2ZJF VAL A 1 UNP P95276 EXPRESSION TAG
SEQRES 1 A 362 HIS HIS HIS HIS HIS HIS VAL SER GLN VAL HIS ARG ILE
SEQRES 2 A 362 LEU ASN CYS ARG GLY THR ARG ILE HIS ALA VAL ALA ASP
SEQRES 3 A 362 SER PRO PRO ASP GLN GLN GLY PRO LEU VAL VAL LEU LEU
SEQRES 4 A 362 HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG HIS GLN
SEQRES 5 A 362 ILE PRO ALA LEU ALA GLY ALA GLY TYR ARG VAL VAL ALA
SEQRES 6 A 362 ILE ASP GLN ARG GLY TYR GLY ARG SER SER LYS TYR ARG
SEQRES 7 A 362 VAL GLN LYS ALA TYR ARG ILE LYS GLU LEU VAL GLY ASP
SEQRES 8 A 362 VAL VAL GLY VAL LEU ASP SER TYR GLY ALA GLU GLN ALA
SEQRES 9 A 362 PHE VAL VAL GLY HIS ASP TRP GLY ALA PRO VAL ALA TRP
SEQRES 10 A 362 THR PHE ALA TRP LEU HIS PRO ASP ARG CYS ALA GLY VAL
SEQRES 11 A 362 VAL GLY ILE SER VAL PRO PHE ALA GLY ARG GLY VAL ILE
SEQRES 12 A 362 GLY LEU PRO GLY SER PRO PHE GLY GLU ARG ARG PRO SER
SEQRES 13 A 362 ASP TYR HIS LEU GLU LEU ALA GLY PRO GLY ARG VAL TRP
SEQRES 14 A 362 TYR GLN ASP TYR PHE ALA VAL GLN ASP GLY ILE ILE THR
SEQRES 15 A 362 GLU ILE GLU GLU ASP LEU ARG GLY TRP LEU LEU GLY LEU
SEQRES 16 A 362 THR TYR THR VAL SER GLY GLU GLY MET MET ALA ALA THR
SEQRES 17 A 362 LYS ALA ALA VAL ASP ALA GLY VAL ASP LEU GLU SER MET
SEQRES 18 A 362 ASP PRO ILE ASP VAL ILE ARG ALA GLY PRO LEU CYS MET
SEQRES 19 A 362 ALA GLU GLY ALA ARG LEU LYS ASP ALA PHE VAL TYR PRO
SEQRES 20 A 362 GLU THR MET PRO ALA TRP PHE THR GLU ALA ASP LEU ASP
SEQRES 21 A 362 PHE TYR THR GLY GLU PHE GLU ARG SER GLY PHE GLY GLY
SEQRES 22 A 362 PRO LEU SER PHE TYR HIS ASN ILE ASP ASN ASP TRP HIS
SEQRES 23 A 362 ASP LEU ALA ASP GLN GLN GLY LYS PRO LEU THR PRO PRO
SEQRES 24 A 362 ALA LEU PHE ILE GLY GLY GLN TYR ASP VAL GLY THR ILE
SEQRES 25 A 362 TRP GLY ALA GLN ALA ILE GLU ARG ALA HIS GLU VAL MET
SEQRES 26 A 362 PRO ASN TYR ARG GLY THR HIS MET ILE ALA ASP VAL GLY
SEQRES 27 A 362 HIS TRP ILE GLN GLN GLU ALA PRO GLU GLU THR ASN ARG
SEQRES 28 A 362 LEU LEU LEU ASP PHE LEU GLY GLY LEU ARG PRO
HET ACT A 357 4
HET ACT A 358 4
HET ACT A 359 4
HET BSU A 360 16
HETNAM ACT ACETATE ION
HETNAM BSU 1,3-DIPHENYLUREA
HETSYN BSU DIPHENYLCARBAMIDE
FORMUL 2 ACT 3(C2 H3 O2 1-)
FORMUL 5 BSU C13 H12 N2 O
FORMUL 6 HOH *120(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 LEU A 8 0
SHEET 2 A 8 ILE A 15 ASP A 20 -1 O ALA A 17 N ARG A 6
SHEET 3 A 8 ARG A 56 ILE A 60 -1 O ALA A 59 N VAL A 18
SHEET 4 A 8 LEU A 29 LEU A 33 1 N VAL A 30 O ARG A 56
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 ILE A 297 N GLY A 126
SHEET 8 A 8 TYR A 322 ILE A 328 1 O HIS A 326 N GLY A 298
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 -0.60
SITE 1 AC1 5 PRO A 37 THR A 190 TYR A 256 TRP A 334
SITE 2 AC1 5 GLN A 337
SITE 1 AC2 3 ARG A 63 GLU A 81 THR A 176
SITE 1 AC3 6 HIS A 153 ASP A 166 ALA A 169 TYR A 272
SITE 2 AC3 6 ASP A 276 HOH A 367
SITE 1 AC4 9 PHE A 36 ASP A 104 TRP A 105 ILE A 137
SITE 2 AC4 9 TYR A 164 LEU A 189 TYR A 272 HIS A 333
SITE 3 AC4 9 TRP A 334
CRYST1 66.415 66.415 156.829 90.10 90.10 90.10 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 0.015057 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015057 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006376 0.00000
TER 2709 PRO A 356
MASTER 323 0 4 22 10 0 8 6 2856 1 28 28
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