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HEADER HYDROLASE 23-NOV-04 1Y37
TITLE STRUCTURE OF FLUOROACETATE DEHALOGENASE FA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA SP.;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: FA1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-21A(+)
KEYWDS DEHALOGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.OMI
REVDAT 1 28-FEB-06 1Y37 0
JRNL AUTH R.OMI,K.JITSUMORI,T.KURIHARA,N.ESAKI,M.GOTO,
JRNL AUTH 2 I.MIYAHARA,K.HIROTSU
JRNL TITL CRYSTAL STRUCTURE OF FLUOROACETATE DEHALOGENASE FA1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1898935.340
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 96934
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) : 0.181
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9697
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 14066
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1647
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4632
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 332
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.86000
REMARK 3 B22 (A**2) : -0.78000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.29
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.620 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.140 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 11.510; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.800 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 46.44
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESOLUTION-DEPENDENT WEIGHTING
REMARK 3 SCHEME OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1Y37 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-2004.
REMARK 100 THE RCSB ID CODE IS RCSB031058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : NW12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96964
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 42.97100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.81550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.97100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 68.81550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 295
REMARK 465 ILE A 296
REMARK 465 HIS A 297
REMARK 465 GLN A 298
REMARK 465 THR A 299
REMARK 465 GLU A 300
REMARK 465 ARG A 301
REMARK 465 ARG A 302
REMARK 465 GLU A 303
REMARK 465 SER A 304
REMARK 465 GLY B 295
REMARK 465 ILE B 296
REMARK 465 HIS B 297
REMARK 465 GLN B 298
REMARK 465 THR B 299
REMARK 465 GLU B 300
REMARK 465 ARG B 301
REMARK 465 ARG B 302
REMARK 465 GLU B 303
REMARK 465 SER B 304
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 6 CG CD OE1 OE2
REMARK 470 THR A 182 OG1 CG2
REMARK 470 THR B 182 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OE1 GLU A 88 O HOH 292 2.09
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 1 SD MET A 1 CE -0.219
REMARK 500 MET A 82 SD MET A 82 CE -0.167
REMARK 500 MET A 262 SD MET A 262 CE -0.134
REMARK 500 MET B 1 SD MET B 1 CE -0.216
REMARK 500 MET B 82 SD MET B 82 CE -0.270
REMARK 500 MET B 251 SD MET B 251 CE -0.119
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 82 CG - SD - CE ANGL. DEV. =-12.2 DEGREES
REMARK 500 GLY A 183 N - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 GLY A 240 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ILE B 130 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 MET B 251 CG - SD - CE ANGL. DEV. =-16.0 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 316 DISTANCE = 7.86 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS NO SUITABLE SEQUENCE DATABASE
REMARK 999 REFERENCE AT THE TIME OF PROCESSING.
REMARK 999 THE MUTATION Q297H IS PRESENT
REMARK 999 IN THE POLYPEPTIDE SEQUENCE
REMARK 999 IN COMPARISON TO THE PUBLISHED
REMARK 999 SEQUENCE IN JRNL OF MOLECULAR CATALYSIS
REMARK 999 B:ENZYMATIC 23(2003) 347-355.
SEQRES 1 A 304 MET PHE GLU GLY PHE GLU ARG ARG LEU VAL ASP VAL GLY
SEQRES 2 A 304 ASP VAL THR ILE ASN CYS VAL VAL GLY GLY SER GLY PRO
SEQRES 3 A 304 ALA LEU LEU LEU LEU HIS GLY PHE PRO GLN ASN LEU HIS
SEQRES 4 A 304 MET TRP ALA ARG VAL ALA PRO LEU LEU ALA ASN GLU TYR
SEQRES 5 A 304 THR VAL VAL CYS ALA ASP LEU ARG GLY TYR GLY GLY SER
SEQRES 6 A 304 SER LYS PRO VAL GLY ALA PRO ASP HIS ALA ASN TYR SER
SEQRES 7 A 304 PHE ARG ALA MET ALA SER ASP GLN ARG GLU LEU MET ARG
SEQRES 8 A 304 THR LEU GLY PHE GLU ARG PHE HIS LEU VAL GLY HIS ASP
SEQRES 9 A 304 ARG GLY GLY ARG THR GLY HIS ARG MET ALA LEU ASP HIS
SEQRES 10 A 304 PRO ASP SER VAL LEU SER LEU ALA VAL LEU ASP ILE ILE
SEQRES 11 A 304 PRO THR TYR VAL MET PHE GLU GLU VAL ASP ARG PHE VAL
SEQRES 12 A 304 ALA ARG ALA TYR TRP HIS TRP TYR PHE LEU GLN GLN PRO
SEQRES 13 A 304 ALA PRO TYR PRO GLU LYS VAL ILE GLY ALA ASP PRO ASP
SEQRES 14 A 304 THR PHE TYR GLU GLY CYS LEU PHE GLY TRP GLY ALA THR
SEQRES 15 A 304 GLY ALA ASP GLY PHE ASP PRO GLU GLN LEU GLU GLU TYR
SEQRES 16 A 304 ARG LYS GLN TRP ARG ASP PRO ALA ALA ILE HIS GLY SER
SEQRES 17 A 304 CYS CYS ASP TYR ARG ALA GLY GLY THR ILE ASP PHE GLU
SEQRES 18 A 304 LEU ASP HIS GLY ASP LEU GLY ARG GLN VAL GLN CYS PRO
SEQRES 19 A 304 ALA LEU VAL PHE SER GLY SER ALA GLY LEU MET HIS SER
SEQRES 20 A 304 LEU PHE GLU MET GLN VAL VAL TRP ALA PRO ARG LEU ALA
SEQRES 21 A 304 ASN MET ARG PHE ALA SER LEU PRO GLY GLY HIS PHE PHE
SEQRES 22 A 304 VAL ASP ARG PHE PRO ASP ASP THR ALA ARG ILE LEU ARG
SEQRES 23 A 304 GLU PHE LEU SER ASP ALA ARG SER GLY ILE HIS GLN THR
SEQRES 24 A 304 GLU ARG ARG GLU SER
SEQRES 1 B 304 MET PHE GLU GLY PHE GLU ARG ARG LEU VAL ASP VAL GLY
SEQRES 2 B 304 ASP VAL THR ILE ASN CYS VAL VAL GLY GLY SER GLY PRO
SEQRES 3 B 304 ALA LEU LEU LEU LEU HIS GLY PHE PRO GLN ASN LEU HIS
SEQRES 4 B 304 MET TRP ALA ARG VAL ALA PRO LEU LEU ALA ASN GLU TYR
SEQRES 5 B 304 THR VAL VAL CYS ALA ASP LEU ARG GLY TYR GLY GLY SER
SEQRES 6 B 304 SER LYS PRO VAL GLY ALA PRO ASP HIS ALA ASN TYR SER
SEQRES 7 B 304 PHE ARG ALA MET ALA SER ASP GLN ARG GLU LEU MET ARG
SEQRES 8 B 304 THR LEU GLY PHE GLU ARG PHE HIS LEU VAL GLY HIS ASP
SEQRES 9 B 304 ARG GLY GLY ARG THR GLY HIS ARG MET ALA LEU ASP HIS
SEQRES 10 B 304 PRO ASP SER VAL LEU SER LEU ALA VAL LEU ASP ILE ILE
SEQRES 11 B 304 PRO THR TYR VAL MET PHE GLU GLU VAL ASP ARG PHE VAL
SEQRES 12 B 304 ALA ARG ALA TYR TRP HIS TRP TYR PHE LEU GLN GLN PRO
SEQRES 13 B 304 ALA PRO TYR PRO GLU LYS VAL ILE GLY ALA ASP PRO ASP
SEQRES 14 B 304 THR PHE TYR GLU GLY CYS LEU PHE GLY TRP GLY ALA THR
SEQRES 15 B 304 GLY ALA ASP GLY PHE ASP PRO GLU GLN LEU GLU GLU TYR
SEQRES 16 B 304 ARG LYS GLN TRP ARG ASP PRO ALA ALA ILE HIS GLY SER
SEQRES 17 B 304 CYS CYS ASP TYR ARG ALA GLY GLY THR ILE ASP PHE GLU
SEQRES 18 B 304 LEU ASP HIS GLY ASP LEU GLY ARG GLN VAL GLN CYS PRO
SEQRES 19 B 304 ALA LEU VAL PHE SER GLY SER ALA GLY LEU MET HIS SER
SEQRES 20 B 304 LEU PHE GLU MET GLN VAL VAL TRP ALA PRO ARG LEU ALA
SEQRES 21 B 304 ASN MET ARG PHE ALA SER LEU PRO GLY GLY HIS PHE PHE
SEQRES 22 B 304 VAL ASP ARG PHE PRO ASP ASP THR ALA ARG ILE LEU ARG
SEQRES 23 B 304 GLU PHE LEU SER ASP ALA ARG SER GLY ILE HIS GLN THR
SEQRES 24 B 304 GLU ARG ARG GLU SER
HET MG 501 1
HET MG 502 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 2(MG1 2+)
FORMUL 5 HOH *332(H2 O1)
HELIX 1 1 ASN A 37 ALA A 42 5 6
HELIX 2 2 ARG A 43 ALA A 49 1 7
HELIX 3 3 HIS A 74 TYR A 77 5 4
HELIX 4 4 SER A 78 LEU A 93 1 16
HELIX 5 5 ASP A 104 HIS A 117 1 14
HELIX 6 6 PRO A 131 GLU A 138 1 8
HELIX 7 7 ASP A 140 TYR A 147 1 8
HELIX 8 8 TRP A 148 LEU A 153 1 6
HELIX 9 9 PRO A 158 ASP A 167 1 10
HELIX 10 10 ASP A 167 GLY A 178 1 12
HELIX 11 11 ASP A 188 ARG A 200 1 13
HELIX 12 12 ASP A 201 GLY A 216 1 16
HELIX 13 13 THR A 217 ASP A 226 1 10
HELIX 14 14 GLY A 243 PHE A 249 1 7
HELIX 15 15 GLU A 250 ALA A 256 1 7
HELIX 16 16 PHE A 272 PHE A 277 1 6
HELIX 17 17 PHE A 277 SER A 294 1 18
HELIX 18 18 ASN B 37 ALA B 42 5 6
HELIX 19 19 ARG B 43 ALA B 49 1 7
HELIX 20 20 HIS B 74 TYR B 77 5 4
HELIX 21 21 SER B 78 LEU B 93 1 16
HELIX 22 22 ASP B 104 HIS B 117 1 14
HELIX 23 23 PRO B 131 GLU B 138 1 8
HELIX 24 24 ASP B 140 TYR B 147 1 8
HELIX 25 25 TRP B 148 LEU B 153 1 6
HELIX 26 26 PRO B 158 ALA B 166 1 9
HELIX 27 27 ASP B 167 GLY B 178 1 12
HELIX 28 28 ASP B 188 ARG B 200 1 13
HELIX 29 29 ASP B 201 GLY B 216 1 16
HELIX 30 30 THR B 217 ASP B 226 1 10
HELIX 31 31 GLY B 243 PHE B 249 1 7
HELIX 32 32 GLU B 250 ALA B 256 1 7
HELIX 33 33 PHE B 272 PHE B 277 1 6
HELIX 34 34 PHE B 277 SER B 294 1 18
SHEET 1 A 8 ARG A 8 VAL A 12 0
SHEET 2 A 8 VAL A 15 GLY A 23 -1 O VAL A 15 N VAL A 12
SHEET 3 A 8 THR A 53 ALA A 57 -1 O VAL A 54 N GLY A 22
SHEET 4 A 8 ALA A 27 LEU A 31 1 N LEU A 28 O VAL A 55
SHEET 5 A 8 PHE A 98 HIS A 103 1 O VAL A 101 N LEU A 31
SHEET 6 A 8 VAL A 121 LEU A 127 1 O LEU A 127 N GLY A 102
SHEET 7 A 8 ALA A 235 GLY A 240 1 O LEU A 236 N VAL A 126
SHEET 8 A 8 MET A 262 LEU A 267 1 O ARG A 263 N VAL A 237
SHEET 1 B 8 GLU B 6 ASP B 11 0
SHEET 2 B 8 THR B 16 GLY B 23 -1 O VAL B 21 N GLU B 6
SHEET 3 B 8 THR B 53 ALA B 57 -1 O VAL B 54 N GLY B 22
SHEET 4 B 8 ALA B 27 LEU B 31 1 N LEU B 30 O VAL B 55
SHEET 5 B 8 PHE B 98 HIS B 103 1 O HIS B 99 N LEU B 29
SHEET 6 B 8 VAL B 121 LEU B 127 1 O LEU B 127 N GLY B 102
SHEET 7 B 8 ALA B 235 GLY B 240 1 O LEU B 236 N VAL B 126
SHEET 8 B 8 MET B 262 LEU B 267 1 O ARG B 263 N VAL B 237
CISPEP 1 PHE A 34 PRO A 35 0 -0.09
CISPEP 2 ALA A 157 PRO A 158 0 0.64
CISPEP 3 PHE B 34 PRO B 35 0 -0.10
CISPEP 4 ALA B 157 PRO B 158 0 0.80
CRYST1 85.942 137.631 52.920 90.00 95.09 90.00 C 1 2 1 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 0.011636 0.000000 0.001036 0.00000
SCALE2 0.000000 0.007266 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018971 0.00000 |