HEADER TRANSFERASE 10-JAN-02 1KRV
TITLE GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH COA AND PNP-BETA-GAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALACTOSIDE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: THIOGALACTOSIDE ACETYLTRANSFERASE;
COMPND 5 EC: 2.3.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: LACA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TG1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTAC-85
KEYWDS LEFT-HANDED PARALLEL BETA HELIX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.-G.WANG,L.R.OLSEN,S.L.RODERICK
REVDAT 6 14-FEB-24 1KRV 1 HETSYN
REVDAT 5 29-JUL-20 1KRV 1 COMPND REMARK HETNAM SITE
REVDAT 5 2 1 ATOM
REVDAT 4 11-OCT-17 1KRV 1 REMARK
REVDAT 3 24-FEB-09 1KRV 1 VERSN
REVDAT 2 01-APR-03 1KRV 1 JRNL
REVDAT 1 10-APR-02 1KRV 0
JRNL AUTH X.G.WANG,L.R.OLSEN,S.L.RODERICK
JRNL TITL STRUCTURE OF THE LAC OPERON GALACTOSIDE ACETYLTRANSFERASE.
JRNL REF STRUCTURE V. 10 581 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 11937062
JRNL DOI 10.1016/S0969-2126(02)00741-4
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 17605
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) : 0.174
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 861
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1202
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 59
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4752
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 207
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.30
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
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) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.200 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.320 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.640 ; 2.500
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 : PNP.PAR
REMARK 3 PARAMETER FILE 3 : COA.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : PNP.TOP
REMARK 3 TOPOLOGY FILE 3 : COA.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CONFOCAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-GEN
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17605
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TES, TARTARIC ACID,
REMARK 280 COENZYME A, PNP-BETA-GAL, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 60.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.15000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 91.90000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.15000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 91.90000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.75000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.15000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 91.90000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.75000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.15000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 91.90000
REMARK 290 SMTRY3 8 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 MET A 1
REMARK 465 VAL A 203
REMARK 465 MET B 1
REMARK 465 VAL B 203
REMARK 465 MET C 1
REMARK 465 VAL C 203
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 LYS A 198 CG CD CE NZ
REMARK 470 SER A 202 O
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 SER B 202 O
REMARK 470 LYS C 198 CG CD CE NZ
REMARK 470 SER C 202 O
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 SER C 201 N - CA - C ANGL. DEV. = 21.3 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 ASP A 92 71.01 -114.36
REMARK 500 ASN A 107 72.55 55.02
REMARK 500 HIS A 119 -16.73 -48.44
REMARK 500 HIS A 143 19.08 58.88
REMARK 500 ARG A 183 164.53 178.14
REMARK 500 ASN A 186 -147.63 -97.72
REMARK 500 LYS A 195 -110.32 41.49
REMARK 500 GLU A 200 97.34 -52.77
REMARK 500 MET B 18 40.03 -100.08
REMARK 500 GLU B 43 58.14 -60.01
REMARK 500 TYR B 72 -53.40 -128.91
REMARK 500 ASP B 92 65.47 -106.81
REMARK 500 HIS B 119 -17.90 -48.54
REMARK 500 GLU B 126 150.92 -43.62
REMARK 500 ASN B 155 7.03 59.16
REMARK 500 ARG B 183 160.21 178.93
REMARK 500 LYS B 195 -113.02 52.84
REMARK 500 SER B 201 -81.83 -8.22
REMARK 500 ASP C 92 60.19 -103.72
REMARK 500 PRO C 131 158.73 -43.20
REMARK 500 LYS C 195 -112.68 52.67
REMARK 500 SER C 201 -39.40 -39.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KQA RELATED DB: PDB
REMARK 900 GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A
REMARK 900 RELATED ID: 1KRR RELATED DB: PDB
REMARK 900 GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH ACETYL-COENZYME A
REMARK 900 RELATED ID: 1KRU RELATED DB: PDB
REMARK 900 GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH IPTG AND COENZYME A
DBREF 1KRV A 1 203 UNP P07464 THGA_ECOLI 1 203
DBREF 1KRV B 1 203 UNP P07464 THGA_ECOLI 1 203
DBREF 1KRV C 1 203 UNP P07464 THGA_ECOLI 1 203
SEQRES 1 A 203 MET ASN MET PRO MET THR GLU ARG ILE ARG ALA GLY LYS
SEQRES 2 A 203 LEU PHE THR ASP MET CYS GLU GLY LEU PRO GLU LYS ARG
SEQRES 3 A 203 LEU ARG GLY LYS THR LEU MET TYR GLU PHE ASN HIS SER
SEQRES 4 A 203 HIS PRO SER GLU VAL GLU LYS ARG GLU SER LEU ILE LYS
SEQRES 5 A 203 GLU MET PHE ALA THR VAL GLY GLU ASN ALA TRP VAL GLU
SEQRES 6 A 203 PRO PRO VAL TYR PHE SER TYR GLY SER ASN ILE HIS ILE
SEQRES 7 A 203 GLY ARG ASN PHE TYR ALA ASN PHE ASN LEU THR ILE VAL
SEQRES 8 A 203 ASP ASP TYR THR VAL THR ILE GLY ASP ASN VAL LEU ILE
SEQRES 9 A 203 ALA PRO ASN VAL THR LEU SER VAL THR GLY HIS PRO VAL
SEQRES 10 A 203 HIS HIS GLU LEU ARG LYS ASN GLY GLU MET TYR SER PHE
SEQRES 11 A 203 PRO ILE THR ILE GLY ASN ASN VAL TRP ILE GLY SER HIS
SEQRES 12 A 203 VAL VAL ILE ASN PRO GLY VAL THR ILE GLY ASP ASN SER
SEQRES 13 A 203 VAL ILE GLY ALA GLY SER ILE VAL THR LYS ASP ILE PRO
SEQRES 14 A 203 PRO ASN VAL VAL ALA ALA GLY VAL PRO CYS ARG VAL ILE
SEQRES 15 A 203 ARG GLU ILE ASN ASP ARG ASP LYS HIS TYR TYR PHE LYS
SEQRES 16 A 203 ASP TYR LYS VAL GLU SER SER VAL
SEQRES 1 B 203 MET ASN MET PRO MET THR GLU ARG ILE ARG ALA GLY LYS
SEQRES 2 B 203 LEU PHE THR ASP MET CYS GLU GLY LEU PRO GLU LYS ARG
SEQRES 3 B 203 LEU ARG GLY LYS THR LEU MET TYR GLU PHE ASN HIS SER
SEQRES 4 B 203 HIS PRO SER GLU VAL GLU LYS ARG GLU SER LEU ILE LYS
SEQRES 5 B 203 GLU MET PHE ALA THR VAL GLY GLU ASN ALA TRP VAL GLU
SEQRES 6 B 203 PRO PRO VAL TYR PHE SER TYR GLY SER ASN ILE HIS ILE
SEQRES 7 B 203 GLY ARG ASN PHE TYR ALA ASN PHE ASN LEU THR ILE VAL
SEQRES 8 B 203 ASP ASP TYR THR VAL THR ILE GLY ASP ASN VAL LEU ILE
SEQRES 9 B 203 ALA PRO ASN VAL THR LEU SER VAL THR GLY HIS PRO VAL
SEQRES 10 B 203 HIS HIS GLU LEU ARG LYS ASN GLY GLU MET TYR SER PHE
SEQRES 11 B 203 PRO ILE THR ILE GLY ASN ASN VAL TRP ILE GLY SER HIS
SEQRES 12 B 203 VAL VAL ILE ASN PRO GLY VAL THR ILE GLY ASP ASN SER
SEQRES 13 B 203 VAL ILE GLY ALA GLY SER ILE VAL THR LYS ASP ILE PRO
SEQRES 14 B 203 PRO ASN VAL VAL ALA ALA GLY VAL PRO CYS ARG VAL ILE
SEQRES 15 B 203 ARG GLU ILE ASN ASP ARG ASP LYS HIS TYR TYR PHE LYS
SEQRES 16 B 203 ASP TYR LYS VAL GLU SER SER VAL
SEQRES 1 C 203 MET ASN MET PRO MET THR GLU ARG ILE ARG ALA GLY LYS
SEQRES 2 C 203 LEU PHE THR ASP MET CYS GLU GLY LEU PRO GLU LYS ARG
SEQRES 3 C 203 LEU ARG GLY LYS THR LEU MET TYR GLU PHE ASN HIS SER
SEQRES 4 C 203 HIS PRO SER GLU VAL GLU LYS ARG GLU SER LEU ILE LYS
SEQRES 5 C 203 GLU MET PHE ALA THR VAL GLY GLU ASN ALA TRP VAL GLU
SEQRES 6 C 203 PRO PRO VAL TYR PHE SER TYR GLY SER ASN ILE HIS ILE
SEQRES 7 C 203 GLY ARG ASN PHE TYR ALA ASN PHE ASN LEU THR ILE VAL
SEQRES 8 C 203 ASP ASP TYR THR VAL THR ILE GLY ASP ASN VAL LEU ILE
SEQRES 9 C 203 ALA PRO ASN VAL THR LEU SER VAL THR GLY HIS PRO VAL
SEQRES 10 C 203 HIS HIS GLU LEU ARG LYS ASN GLY GLU MET TYR SER PHE
SEQRES 11 C 203 PRO ILE THR ILE GLY ASN ASN VAL TRP ILE GLY SER HIS
SEQRES 12 C 203 VAL VAL ILE ASN PRO GLY VAL THR ILE GLY ASP ASN SER
SEQRES 13 C 203 VAL ILE GLY ALA GLY SER ILE VAL THR LYS ASP ILE PRO
SEQRES 14 C 203 PRO ASN VAL VAL ALA ALA GLY VAL PRO CYS ARG VAL ILE
SEQRES 15 C 203 ARG GLU ILE ASN ASP ARG ASP LYS HIS TYR TYR PHE LYS
SEQRES 16 C 203 ASP TYR LYS VAL GLU SER SER VAL
HET 147 A 206 21
HET COA A 207 48
HET 147 B 204 21
HET COA B 208 48
HET 147 C 205 21
HET COA C 209 48
HETNAM 147 4-NITROPHENYL BETA-D-GALACTOPYRANOSIDE
HETNAM COA COENZYME A
HETSYN 147 1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE; 4-
HETSYN 2 147 NITROPHENYL BETA-D-GALACTOSIDE; 4-NITROPHENYL D-
HETSYN 3 147 GALACTOSIDE; 4-NITROPHENYL GALACTOSIDE
FORMUL 4 147 3(C12 H15 N O8)
FORMUL 5 COA 3(C21 H36 N7 O16 P3 S)
FORMUL 10 HOH *70(H2 O)
HELIX 1 1 PRO A 4 GLY A 12 1 9
HELIX 2 2 GLY A 21 SER A 39 1 19
HELIX 3 3 GLU A 43 PHE A 55 1 13
HELIX 4 4 ASP A 187 LYS A 190 5 4
HELIX 5 5 PRO B 4 GLY B 12 1 9
HELIX 6 6 GLY B 21 HIS B 38 1 18
HELIX 7 7 GLU B 43 PHE B 55 1 13
HELIX 8 8 ASN B 186 LYS B 190 5 5
HELIX 9 9 PRO C 4 ALA C 11 1 8
HELIX 10 10 GLY C 21 SER C 39 1 19
HELIX 11 11 GLU C 43 PHE C 55 1 13
HELIX 12 12 ASP C 187 LYS C 190 5 4
SHEET 1 A 7 TRP A 63 VAL A 64 0
SHEET 2 A 7 TYR A 83 ALA A 84 1 O ALA A 84 N TRP A 63
SHEET 3 A 7 LEU A 103 ILE A 104 1 O ILE A 104 N TYR A 83
SHEET 4 A 7 TRP A 139 ILE A 140 1 O ILE A 140 N LEU A 103
SHEET 5 A 7 VAL A 157 ILE A 158 1 O ILE A 158 N TRP A 139
SHEET 6 A 7 VAL A 172 ALA A 175 1 O ALA A 174 N VAL A 157
SHEET 7 A 7 ARG A 180 GLU A 184 -1 O ARG A 180 N ALA A 175
SHEET 1 B 5 VAL A 68 PHE A 70 0
SHEET 2 B 5 LEU A 88 VAL A 91 1 O LEU A 88 N TYR A 69
SHEET 3 B 5 VAL A 108 SER A 111 1 O LEU A 110 N VAL A 91
SHEET 4 B 5 VAL A 145 ILE A 146 1 O ILE A 146 N THR A 109
SHEET 5 B 5 ILE A 163 VAL A 164 1 O VAL A 164 N VAL A 145
SHEET 1 C 4 ILE A 76 ILE A 78 0
SHEET 2 C 4 VAL A 96 ILE A 98 1 O ILE A 98 N HIS A 77
SHEET 3 C 4 ILE A 132 ILE A 134 1 O ILE A 134 N THR A 97
SHEET 4 C 4 THR A 151 ILE A 152 1 O ILE A 152 N THR A 133
SHEET 1 D 2 THR A 113 GLY A 114 0
SHEET 2 D 2 TYR A 128 SER A 129 -1 O TYR A 128 N GLY A 114
SHEET 1 E 2 TYR A 192 PHE A 194 0
SHEET 2 E 2 TYR A 197 LYS A 198 -1 O TYR A 197 N PHE A 194
SHEET 1 F 7 TRP B 63 VAL B 64 0
SHEET 2 F 7 TYR B 83 ALA B 84 1 O ALA B 84 N TRP B 63
SHEET 3 F 7 LEU B 103 ILE B 104 1 O ILE B 104 N TYR B 83
SHEET 4 F 7 TRP B 139 ILE B 140 1 O ILE B 140 N LEU B 103
SHEET 5 F 7 VAL B 157 ILE B 158 1 O ILE B 158 N TRP B 139
SHEET 6 F 7 VAL B 172 ALA B 175 1 O ALA B 174 N VAL B 157
SHEET 7 F 7 ARG B 180 GLU B 184 -1 O ARG B 180 N ALA B 175
SHEET 1 G 5 VAL B 68 PHE B 70 0
SHEET 2 G 5 LEU B 88 VAL B 91 1 O ILE B 90 N TYR B 69
SHEET 3 G 5 THR B 109 SER B 111 1 O LEU B 110 N VAL B 91
SHEET 4 G 5 VAL B 145 ILE B 146 1 O ILE B 146 N THR B 109
SHEET 5 G 5 ILE B 163 VAL B 164 1 O VAL B 164 N VAL B 145
SHEET 1 H 4 ILE B 76 ILE B 78 0
SHEET 2 H 4 VAL B 96 ILE B 98 1 O ILE B 98 N HIS B 77
SHEET 3 H 4 ILE B 132 ILE B 134 1 O ILE B 134 N THR B 97
SHEET 4 H 4 THR B 151 ILE B 152 1 O ILE B 152 N THR B 133
SHEET 1 I 2 THR B 113 GLY B 114 0
SHEET 2 I 2 TYR B 128 SER B 129 -1 O TYR B 128 N GLY B 114
SHEET 1 J 2 TYR B 192 PHE B 194 0
SHEET 2 J 2 TYR B 197 LYS B 198 -1 O TYR B 197 N PHE B 194
SHEET 1 K 7 TRP C 63 VAL C 64 0
SHEET 2 K 7 TYR C 83 ALA C 84 1 O ALA C 84 N TRP C 63
SHEET 3 K 7 LEU C 103 ILE C 104 1 O ILE C 104 N TYR C 83
SHEET 4 K 7 TRP C 139 ILE C 140 1 O ILE C 140 N LEU C 103
SHEET 5 K 7 VAL C 157 ILE C 158 1 O ILE C 158 N TRP C 139
SHEET 6 K 7 VAL C 172 ALA C 175 1 O ALA C 174 N VAL C 157
SHEET 7 K 7 ARG C 180 GLU C 184 -1 O ARG C 183 N VAL C 173
SHEET 1 L 5 VAL C 68 PHE C 70 0
SHEET 2 L 5 LEU C 88 VAL C 91 1 O ILE C 90 N TYR C 69
SHEET 3 L 5 THR C 109 SER C 111 1 O LEU C 110 N THR C 89
SHEET 4 L 5 VAL C 145 ILE C 146 1 O ILE C 146 N THR C 109
SHEET 5 L 5 ILE C 163 VAL C 164 1 O VAL C 164 N VAL C 145
SHEET 1 M 4 ILE C 76 ILE C 78 0
SHEET 2 M 4 VAL C 96 ILE C 98 1 O VAL C 96 N HIS C 77
SHEET 3 M 4 ILE C 132 ILE C 134 1 O ILE C 132 N THR C 97
SHEET 4 M 4 THR C 151 ILE C 152 1 O ILE C 152 N THR C 133
SHEET 1 N 2 THR C 113 GLY C 114 0
SHEET 2 N 2 TYR C 128 SER C 129 -1 O TYR C 128 N GLY C 114
SHEET 1 O 2 TYR C 192 PHE C 194 0
SHEET 2 O 2 TYR C 197 LYS C 198 -1 O TYR C 197 N PHE C 194
CISPEP 1 PRO A 66 PRO A 67 0 -0.10
CISPEP 2 VAL A 177 PRO A 178 0 0.54
CISPEP 3 PRO B 66 PRO B 67 0 0.36
CISPEP 4 VAL B 177 PRO B 178 0 0.01
CISPEP 5 PRO C 66 PRO C 67 0 -0.28
CISPEP 6 VAL C 177 PRO C 178 0 0.18
CRYST1 66.300 183.800 121.500 90.00 90.00 90.00 C 2 2 21 24
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 0.015083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005441 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
