HEADER TRANSFERASE 04-JUN-07 2Z3P
TITLE COMPLEX STRUCTURE OF LF-TRANSFERASE AND LEUCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUCYL/PHENYLALANYL-TRNA-PROTEIN TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: L/F-TRANSFERASE, LEUCYLTRANSFERASE, PHENYALANYLTRANSFERASE;
COMPND 5 EC: 2.3.2.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: AAT;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS LF-TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WATANABE,Y.TOH,K.TOMITA
REVDAT 3 01-NOV-23 2Z3P 1 REMARK
REVDAT 2 24-FEB-09 2Z3P 1 VERSN
REVDAT 1 23-OCT-07 2Z3P 0
JRNL AUTH K.WATANABE,Y.TOH,K.SUTO,Y.SHIMIZU,N.OKA,T.WADA,K.TOMITA
JRNL TITL PROTEIN-BASED PEPTIDE-BOND FORMATION BY AMINOACYL-TRNA
JRNL TITL 2 PROTEIN TRANSFERASE
JRNL REF NATURE V. 449 867 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17891155
JRNL DOI 10.1038/NATURE06167
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1193407.670
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 20821
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) : 0.229
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1054
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2438
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 120
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3703
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.67000
REMARK 3 B22 (A**2) : 23.88000
REMARK 3 B33 (A**2) : -21.21000
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) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.42
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
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) : 4.020 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.290 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.850 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 42.42
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 5 : TAR.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : TAR.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Z3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000027481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-06
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21192
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 55.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.15900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2DPS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES-NA, 0.7M TRI-SODIUM
REMARK 280 TARTRATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 57.83950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.83950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.60000
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 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, 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 GLU A 234
REMARK 465 GLN B 233
REMARK 465 GLU B 234
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 3 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 3 120.05 -7.27
REMARK 500 ASN A 24 105.92 -54.38
REMARK 500 LEU A 26 109.95 -57.07
REMARK 500 SER A 60 85.01 -155.41
REMARK 500 ALA A 94 68.57 -151.14
REMARK 500 GLU A 107 -66.80 -100.14
REMARK 500 GLU A 137 -120.14 58.84
REMARK 500 GLN A 188 -82.79 65.57
REMARK 500 ASP A 192 -52.97 -22.63
REMARK 500 PRO A 232 -165.78 -64.36
REMARK 500 LEU B 3 89.90 22.19
REMARK 500 ALA B 19 151.48 -49.34
REMARK 500 SER B 60 73.62 -167.26
REMARK 500 ASP B 105 -12.75 -172.17
REMARK 500 GLU B 107 -113.20 -153.90
REMARK 500 GLU B 137 -125.86 69.71
REMARK 500 GLN B 188 -76.17 66.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z3K RELATED DB: PDB
REMARK 900 RELATED ID: 2Z3L RELATED DB: PDB
REMARK 900 RELATED ID: 2Z3M RELATED DB: PDB
REMARK 900 RELATED ID: 2Z3N RELATED DB: PDB
REMARK 900 RELATED ID: 2Z3O RELATED DB: PDB
DBREF 2Z3P A 2 234 UNP P0A8P1 LFTR_ECOLI 2 234
DBREF 2Z3P B 2 234 UNP P0A8P1 LFTR_ECOLI 2 234
SEQRES 1 A 233 ARG LEU VAL GLN LEU SER ARG HIS SER ILE ALA PHE PRO
SEQRES 2 A 233 SER PRO GLU GLY ALA LEU ARG GLU PRO ASN GLY LEU LEU
SEQRES 3 A 233 ALA LEU GLY GLY ASP LEU SER PRO ALA ARG LEU LEU MET
SEQRES 4 A 233 ALA TYR GLN ARG GLY ILE PHE PRO TRP PHE SER PRO GLY
SEQRES 5 A 233 ASP PRO ILE LEU TRP TRP SER PRO ASP PRO ARG ALA VAL
SEQRES 6 A 233 LEU TRP PRO GLU SER LEU HIS ILE SER ARG SER MET LYS
SEQRES 7 A 233 ARG PHE HIS LYS ARG SER PRO TYR ARG VAL THR MET ASN
SEQRES 8 A 233 TYR ALA PHE GLY GLN VAL ILE GLU GLY CYS ALA SER ASP
SEQRES 9 A 233 ARG GLU GLU GLY THR TRP ILE THR ARG GLY VAL VAL GLU
SEQRES 10 A 233 ALA TYR HIS ARG LEU HIS GLU LEU GLY HIS ALA HIS SER
SEQRES 11 A 233 ILE GLU VAL TRP ARG GLU ASP GLU LEU VAL GLY GLY MET
SEQRES 12 A 233 TYR GLY VAL ALA GLN GLY THR LEU PHE CYS GLY GLU SER
SEQRES 13 A 233 MET PHE SER ARG MET GLU ASN ALA SER LYS THR ALA LEU
SEQRES 14 A 233 LEU VAL PHE CYS GLU GLU PHE ILE GLY HIS GLY GLY LYS
SEQRES 15 A 233 LEU ILE ASP CYS GLN VAL LEU ASN ASP HIS THR ALA SER
SEQRES 16 A 233 LEU GLY ALA CYS GLU ILE PRO ARG ARG ASP TYR LEU ASN
SEQRES 17 A 233 TYR LEU ASN GLN MET ARG LEU GLY ARG LEU PRO ASN ASN
SEQRES 18 A 233 PHE TRP VAL PRO ARG CYS LEU PHE SER PRO GLN GLU
SEQRES 1 B 233 ARG LEU VAL GLN LEU SER ARG HIS SER ILE ALA PHE PRO
SEQRES 2 B 233 SER PRO GLU GLY ALA LEU ARG GLU PRO ASN GLY LEU LEU
SEQRES 3 B 233 ALA LEU GLY GLY ASP LEU SER PRO ALA ARG LEU LEU MET
SEQRES 4 B 233 ALA TYR GLN ARG GLY ILE PHE PRO TRP PHE SER PRO GLY
SEQRES 5 B 233 ASP PRO ILE LEU TRP TRP SER PRO ASP PRO ARG ALA VAL
SEQRES 6 B 233 LEU TRP PRO GLU SER LEU HIS ILE SER ARG SER MET LYS
SEQRES 7 B 233 ARG PHE HIS LYS ARG SER PRO TYR ARG VAL THR MET ASN
SEQRES 8 B 233 TYR ALA PHE GLY GLN VAL ILE GLU GLY CYS ALA SER ASP
SEQRES 9 B 233 ARG GLU GLU GLY THR TRP ILE THR ARG GLY VAL VAL GLU
SEQRES 10 B 233 ALA TYR HIS ARG LEU HIS GLU LEU GLY HIS ALA HIS SER
SEQRES 11 B 233 ILE GLU VAL TRP ARG GLU ASP GLU LEU VAL GLY GLY MET
SEQRES 12 B 233 TYR GLY VAL ALA GLN GLY THR LEU PHE CYS GLY GLU SER
SEQRES 13 B 233 MET PHE SER ARG MET GLU ASN ALA SER LYS THR ALA LEU
SEQRES 14 B 233 LEU VAL PHE CYS GLU GLU PHE ILE GLY HIS GLY GLY LYS
SEQRES 15 B 233 LEU ILE ASP CYS GLN VAL LEU ASN ASP HIS THR ALA SER
SEQRES 16 B 233 LEU GLY ALA CYS GLU ILE PRO ARG ARG ASP TYR LEU ASN
SEQRES 17 B 233 TYR LEU ASN GLN MET ARG LEU GLY ARG LEU PRO ASN ASN
SEQRES 18 B 233 PHE TRP VAL PRO ARG CYS LEU PHE SER PRO GLN GLU
HET LEU A 301 9
HET TAR A 501 10
HET LEU B 401 9
HET TAR B 502 10
HETNAM LEU LEUCINE
HETNAM TAR D(-)-TARTARIC ACID
FORMUL 3 LEU 2(C6 H13 N O2)
FORMUL 4 TAR 2(C4 H6 O6)
FORMUL 7 HOH *20(H2 O)
HELIX 1 1 SER A 15 ALA A 19 5 5
HELIX 2 2 SER A 34 ARG A 44 1 11
HELIX 3 3 TRP A 68 LEU A 72 5 5
HELIX 4 4 SER A 75 ARG A 84 1 10
HELIX 5 5 ALA A 94 SER A 104 1 11
HELIX 6 6 GLU A 108 ILE A 112 5 5
HELIX 7 7 THR A 113 LEU A 126 1 14
HELIX 8 8 ASN A 164 HIS A 180 1 17
HELIX 9 9 ASN A 191 LEU A 197 1 7
HELIX 10 10 PRO A 203 ARG A 215 1 13
HELIX 11 11 SER B 15 ALA B 19 5 5
HELIX 12 12 SER B 34 ARG B 44 1 11
HELIX 13 13 TRP B 68 LEU B 72 5 5
HELIX 14 14 SER B 75 ARG B 84 1 10
HELIX 15 15 ALA B 94 SER B 104 1 11
HELIX 16 16 GLU B 107 ILE B 112 5 6
HELIX 17 17 THR B 113 LEU B 126 1 14
HELIX 18 18 ASN B 164 HIS B 180 1 17
HELIX 19 19 ASN B 191 LEU B 197 1 7
HELIX 20 20 PRO B 203 ARG B 215 1 13
SHEET 1 A 4 VAL A 4 LEU A 6 0
SHEET 2 A 4 LEU A 26 GLY A 30 1 O LEU A 29 N LEU A 6
SHEET 3 A 4 LEU A 57 TRP A 59 -1 O TRP A 58 N ALA A 28
SHEET 4 A 4 PHE A 47 PRO A 48 -1 N PHE A 47 O TRP A 59
SHEET 1 B 8 CYS A 200 ILE A 202 0
SHEET 2 B 8 ARG A 64 LEU A 67 -1 N VAL A 66 O CYS A 200
SHEET 3 B 8 LEU A 184 GLN A 188 -1 O ILE A 185 N LEU A 67
SHEET 4 B 8 LEU A 152 SER A 160 1 N PHE A 153 O ASP A 186
SHEET 5 B 8 GLU A 139 GLN A 149 -1 N GLN A 149 O LEU A 152
SHEET 6 B 8 ALA A 129 ARG A 136 -1 N ARG A 136 O GLU A 139
SHEET 7 B 8 TYR A 87 MET A 91 -1 N ARG A 88 O TRP A 135
SHEET 8 B 8 ARG A 227 PHE A 230 -1 O ARG A 227 N MET A 91
SHEET 1 C 4 VAL B 4 GLN B 5 0
SHEET 2 C 4 LEU B 26 LEU B 29 1 O LEU B 29 N VAL B 4
SHEET 3 C 4 LEU B 57 TRP B 59 -1 O TRP B 58 N ALA B 28
SHEET 4 C 4 PHE B 47 PRO B 48 -1 N PHE B 47 O TRP B 59
SHEET 1 D 8 CYS B 200 ILE B 202 0
SHEET 2 D 8 ARG B 64 LEU B 67 -1 N ARG B 64 O ILE B 202
SHEET 3 D 8 LEU B 184 GLN B 188 -1 O ILE B 185 N LEU B 67
SHEET 4 D 8 LEU B 152 SER B 160 1 N PHE B 153 O ASP B 186
SHEET 5 D 8 GLU B 139 GLN B 149 -1 N GLN B 149 O LEU B 152
SHEET 6 D 8 ALA B 129 ARG B 136 -1 N ILE B 132 O MET B 144
SHEET 7 D 8 ARG B 88 MET B 91 -1 N ARG B 88 O TRP B 135
SHEET 8 D 8 ARG B 227 PHE B 230 -1 O LEU B 229 N VAL B 89
CISPEP 1 GLU A 22 PRO A 23 0 0.61
CISPEP 2 ASP A 62 PRO A 63 0 -0.66
CISPEP 3 GLU B 22 PRO B 23 0 -0.04
CISPEP 4 ASP B 62 PRO B 63 0 0.19
CRYST1 115.679 129.200 38.797 90.00 90.00 90.00 P 21 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 0.008645 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007740 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025775 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
