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HEADER HYDROLASE 21-NOV-07 3BF8
TITLE 1.1 RESOLUTION STRUCTURE OF YBFF, A NEW ESTERASE FROM
TITLE 2 ESCHERICHIA COLI: A UNIQUE SUBSTRATE-BINDING CREVICE
TITLE 3 GENERATED BY DOMAIN ARRANGEMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE YBFF;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 GENE: K12;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET21A
KEYWDS ESTERASE, THIOESTERASE, YBFF, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.PARK,J.S.KIM
REVDAT 1 15-JAN-08 3BF8 0
JRNL AUTH S.Y.PARK,S.H.LEE,J.LEE,N.KOSUKE,Y.S.KIM,C.H.JUNG,
JRNL AUTH 2 J.S.KIM
JRNL TITL 1.1 RESOLUTION STRUCTURE OF YBFF, A NEW ESTERASE
JRNL TITL 2 FROM ESCHERICHIA COLI: A UNIQUE SUBSTRATE-BINDING
JRNL TITL 3 CREVICE GENERATED BY DOMAIN ARRANGEMENT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.68 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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : -1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 116381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 11536
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 176
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 : 4027
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 825
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) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.18
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: THE FILE CONTAINS FRIEDEL PAIRS
REMARK 4
REMARK 4 3BF8 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB045445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.20
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123112
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.15900
REMARK 200 FOR SHELL : 12.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM MALONATE, PH7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 33.10800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.62650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.53050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.62650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.10800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.53050
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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 HIS B 255
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 ASP A 42 15.75 -140.18
REMARK 500 SER A 89 -117.26 49.33
REMARK 500 ASP A 107 -83.54 -96.23
REMARK 500 ASP A 113 63.30 37.78
REMARK 500 ASP A 254 56.61 37.24
REMARK 500 SER B 89 -116.58 51.39
REMARK 500 ASP B 107 -82.04 -91.20
REMARK 500 ASP B 113 64.74 37.94
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 A5143 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A5190 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A5215 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH B5427 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH A5238 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH A5241 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH A5276 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH B5482 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A5285 DISTANCE = 5.75 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BF7 RELATED DB: PDB
DBREF 3BF8 A 1 254 UNP A7ZXU7 A7ZXU7_ECOLX 1 254
DBREF 3BF8 B 1 254 UNP A7ZXU7 A7ZXU7_ECOLX 1 254
SEQADV 3BF8 VAL A 50 UNP A7ZXU7 MET 50 ENGINEERED
SEQADV 3BF8 GLN A 78 UNP A7ZXU7 LEU 78 ENGINEERED
SEQADV 3BF8 HIS A 255 UNP A7ZXU7 EXPRESSION TAG
SEQADV 3BF8 VAL B 50 UNP A7ZXU7 MET 50 ENGINEERED
SEQADV 3BF8 GLN B 78 UNP A7ZXU7 LEU 78 ENGINEERED
SEQADV 3BF8 HIS B 255 UNP A7ZXU7 EXPRESSION TAG
SEQRES 1 A 255 MET LYS LEU ASN ILE ARG ALA GLN THR ALA GLN ASN GLN
SEQRES 2 A 255 HIS ASN ASN SER PRO ILE VAL LEU VAL HIS GLY LEU PHE
SEQRES 3 A 255 GLY SER LEU ASP ASN LEU GLY VAL LEU ALA ARG ASP LEU
SEQRES 4 A 255 VAL ASN ASP HIS ASN ILE ILE GLN VAL ASP VAL ARG ASN
SEQRES 5 A 255 HIS GLY LEU SER PRO ARG GLU PRO VAL MET ASN TYR PRO
SEQRES 6 A 255 ALA MET ALA GLN ASP LEU VAL ASP THR LEU ASP ALA GLN
SEQRES 7 A 255 GLN ILE ASP LYS ALA THR PHE ILE GLY HIS SER MET GLY
SEQRES 8 A 255 GLY LYS ALA VAL MET ALA LEU THR ALA LEU ALA PRO ASP
SEQRES 9 A 255 ARG ILE ASP LYS LEU VAL ALA ILE ASP ILE ALA PRO VAL
SEQRES 10 A 255 ASP TYR HIS VAL ARG ARG HIS ASP GLU ILE PHE ALA ALA
SEQRES 11 A 255 ILE ASN ALA VAL SER GLU SER ASP ALA GLN THR ARG GLN
SEQRES 12 A 255 GLN ALA ALA ALA ILE MET ARG GLN HIS LEU ASN GLU GLU
SEQRES 13 A 255 GLY VAL ILE GLN PHE LEU LEU LYS SER PHE VAL ASP GLY
SEQRES 14 A 255 GLU TRP ARG PHE ASN VAL PRO VAL LEU TRP ASP GLN TYR
SEQRES 15 A 255 PRO HIS ILE VAL GLY TRP GLU LYS ILE PRO ALA TRP ASP
SEQRES 16 A 255 HIS PRO ALA LEU PHE ILE PRO GLY GLY ASN SER PRO TYR
SEQRES 17 A 255 VAL SER GLU GLN TYR ARG ASP ASP LEU LEU ALA GLN PHE
SEQRES 18 A 255 PRO GLN ALA ARG ALA HIS VAL ILE ALA GLY ALA GLY HIS
SEQRES 19 A 255 TRP VAL HIS ALA GLU LYS PRO ASP ALA VAL LEU ARG ALA
SEQRES 20 A 255 ILE ARG ARG TYR LEU ASN ASP HIS
SEQRES 1 B 255 MET LYS LEU ASN ILE ARG ALA GLN THR ALA GLN ASN GLN
SEQRES 2 B 255 HIS ASN ASN SER PRO ILE VAL LEU VAL HIS GLY LEU PHE
SEQRES 3 B 255 GLY SER LEU ASP ASN LEU GLY VAL LEU ALA ARG ASP LEU
SEQRES 4 B 255 VAL ASN ASP HIS ASN ILE ILE GLN VAL ASP VAL ARG ASN
SEQRES 5 B 255 HIS GLY LEU SER PRO ARG GLU PRO VAL MET ASN TYR PRO
SEQRES 6 B 255 ALA MET ALA GLN ASP LEU VAL ASP THR LEU ASP ALA GLN
SEQRES 7 B 255 GLN ILE ASP LYS ALA THR PHE ILE GLY HIS SER MET GLY
SEQRES 8 B 255 GLY LYS ALA VAL MET ALA LEU THR ALA LEU ALA PRO ASP
SEQRES 9 B 255 ARG ILE ASP LYS LEU VAL ALA ILE ASP ILE ALA PRO VAL
SEQRES 10 B 255 ASP TYR HIS VAL ARG ARG HIS ASP GLU ILE PHE ALA ALA
SEQRES 11 B 255 ILE ASN ALA VAL SER GLU SER ASP ALA GLN THR ARG GLN
SEQRES 12 B 255 GLN ALA ALA ALA ILE MET ARG GLN HIS LEU ASN GLU GLU
SEQRES 13 B 255 GLY VAL ILE GLN PHE LEU LEU LYS SER PHE VAL ASP GLY
SEQRES 14 B 255 GLU TRP ARG PHE ASN VAL PRO VAL LEU TRP ASP GLN TYR
SEQRES 15 B 255 PRO HIS ILE VAL GLY TRP GLU LYS ILE PRO ALA TRP ASP
SEQRES 16 B 255 HIS PRO ALA LEU PHE ILE PRO GLY GLY ASN SER PRO TYR
SEQRES 17 B 255 VAL SER GLU GLN TYR ARG ASP ASP LEU LEU ALA GLN PHE
SEQRES 18 B 255 PRO GLN ALA ARG ALA HIS VAL ILE ALA GLY ALA GLY HIS
SEQRES 19 B 255 TRP VAL HIS ALA GLU LYS PRO ASP ALA VAL LEU ARG ALA
SEQRES 20 B 255 ILE ARG ARG TYR LEU ASN ASP HIS
HET MLA A4892 7
HET MLA B4892 7
HETNAM MLA MALONIC ACID
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METAHNEDICARBOXYLIC ACID
FORMUL 3 MLA 2(C3 H4 O4)
FORMUL 5 HOH *825(H2 O)
HELIX 1 1 LEU A 32 VAL A 40 1 9
HELIX 2 2 ASN A 63 GLN A 79 1 17
HELIX 3 3 SER A 89 ALA A 102 1 14
HELIX 4 4 HIS A 124 SER A 137 1 14
HELIX 5 5 THR A 141 ARG A 150 1 10
HELIX 6 6 GLU A 155 LYS A 164 1 10
HELIX 7 7 ASN A 174 GLN A 181 1 8
HELIX 8 8 GLN A 181 GLY A 187 1 7
HELIX 9 9 SER A 210 GLN A 212 5 3
HELIX 10 10 TYR A 213 PHE A 221 1 9
HELIX 11 11 TRP A 235 LYS A 240 1 6
HELIX 12 12 LYS A 240 ASP A 254 1 15
HELIX 13 13 SER B 28 ASN B 31 5 4
HELIX 14 14 LEU B 32 VAL B 40 1 9
HELIX 15 15 ASN B 63 GLN B 78 1 16
HELIX 16 16 SER B 89 ALA B 102 1 14
HELIX 17 17 HIS B 124 SER B 137 1 14
HELIX 18 18 THR B 141 ARG B 150 1 10
HELIX 19 19 GLU B 155 LYS B 164 1 10
HELIX 20 20 ASN B 174 GLY B 187 1 14
HELIX 21 21 SER B 210 GLN B 212 5 3
HELIX 22 22 TYR B 213 PHE B 221 1 9
HELIX 23 23 TRP B 235 LYS B 240 1 6
HELIX 24 24 LYS B 240 ASP B 254 1 15
SHEET 1 A 7 ILE A 5 GLN A 8 0
SHEET 2 A 7 ILE A 45 VAL A 48 -1 O ILE A 45 N GLN A 8
SHEET 3 A 7 ILE A 19 VAL A 22 1 N LEU A 21 O ILE A 46
SHEET 4 A 7 ALA A 83 HIS A 88 1 O THR A 84 N VAL A 20
SHEET 5 A 7 ILE A 106 ILE A 112 1 O ILE A 112 N GLY A 87
SHEET 6 A 7 ALA A 198 ILE A 201 1 O LEU A 199 N ALA A 111
SHEET 7 A 7 ALA A 224 ALA A 226 1 O ARG A 225 N PHE A 200
SHEET 1 B 2 PHE A 166 VAL A 167 0
SHEET 2 B 2 GLU A 170 TRP A 171 -1 O GLU A 170 N VAL A 167
SHEET 1 C 7 ILE B 5 GLN B 8 0
SHEET 2 C 7 ILE B 45 VAL B 48 -1 O ILE B 45 N GLN B 8
SHEET 3 C 7 ILE B 19 VAL B 22 1 N LEU B 21 O ILE B 46
SHEET 4 C 7 ALA B 83 HIS B 88 1 O THR B 84 N VAL B 20
SHEET 5 C 7 ILE B 106 ILE B 112 1 O ILE B 112 N GLY B 87
SHEET 6 C 7 ALA B 198 ILE B 201 1 O LEU B 199 N ALA B 111
SHEET 7 C 7 ALA B 224 ALA B 226 1 O ARG B 225 N PHE B 200
SHEET 1 D 2 PHE B 166 VAL B 167 0
SHEET 2 D 2 GLU B 170 TRP B 171 -1 O GLU B 170 N VAL B 167
CRYST1 66.216 91.061 93.253 90.00 90.00 90.00 P 21 21 21 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 0.015102 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010982 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010724 0.00000
TER 2020 HIS A 255
TER 4029 ASP B 254
MASTER 277 0 2 24 18 0 0 6 4866 2 14 40
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