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HEADER HYDROLASE 25-FEB-16 5IE7
TITLE CRYSTAL STRUCTURE OF A LACTONASE DOUBLE MUTANT IN COMPLEX WITH
TITLE 2 SUBSTRATE B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: LACTONASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;
SOURCE 3 ORGANISM_TAXID: 29856;
SOURCE 4 GENE: ZHD101;
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-46 EK/LIC
KEYWDS ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHENG,Z.X.XU,W.D.LIU,C.C.CHEN,R.T.GUO
REVDAT 1 04-JAN-17 5IE7 0
JRNL AUTH Z.X.XU,W.D.LIU,C.C.CHEN,Q.LI,J.W.HUANG,T.P.KO,G.LIU,W.LIU,
JRNL AUTH 2 W.PENG,Y.S.CHENG,Y.CHEN,J.JIN,H.LI,Y.Y.ZHENG,R.T.GUO
JRNL TITL ENHANCED ALPH-ZEARALENOL HYDROLYZING ACTIVITY OF A
JRNL TITL 2 MYCOESTROGEN-DETOXIFYING LACTONASE BY STRUCTURE-BASED
JRNL TITL 3 ENGINEERING
JRNL REF ACS CATALYSIS V. 6 7657 2016
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.6B01826
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 35550
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 + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1870
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2537
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 384
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.62000
REMARK 3 B22 (A**2) : 0.62000
REMARK 3 B33 (A**2) : -2.01000
REMARK 3 B12 (A**2) : 0.31000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.349
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.289
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.202
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.966
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5204 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4878 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7093 ; 1.513 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11262 ; 1.002 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 8.877 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 209 ;37.113 ;24.115
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 803 ;20.193 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;13.833 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 809 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5797 ; 0.017 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1121 ; 0.008 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2617 ; 3.500 ; 3.420
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2616 ; 3.501 ; 3.420
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3252 ; 5.275 ; 5.095
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3253 ; 5.274 ; 5.096
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2587 ; 3.867 ; 3.700
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2587 ; 3.865 ; 3.700
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3842 ; 5.857 ; 5.426
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6115 ; 8.501 ;27.736
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6036 ; 8.500 ;27.486
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 264 B 1 264 30428 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5IE7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13C1
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 : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37570
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35700
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3WZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 2000 MME, 0.1M BIS-TRIS, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 156.81633
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 313.63267
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 235.22450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 392.04083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.40817
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 156.81633
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 313.63267
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 392.04083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 235.22450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 78.40817
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, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 C 1
REMARK 465 ARG C 2
REMARK 465 THR C 3
REMARK 465 ARG C 4
REMARK 465 SER C 5
REMARK 465 THR C 6
REMARK 465 ILE C 7
REMARK 465 SER C 8
REMARK 465 THR C 9
REMARK 465 PRO C 10
REMARK 465 ASN C 11
REMARK 465 GLY C 12
REMARK 465 ILE C 13
REMARK 465 THR C 14
REMARK 465 TRP C 15
REMARK 465 ASP C 31
REMARK 465 GLY C 32
REMARK 465 LEU C 33
REMARK 465 GLY C 34
REMARK 465 GLU C 35
REMARK 465 CYS C 36
REMARK 465 GLN C 37
REMARK 465 MET C 38
REMARK 465 PHE C 39
REMARK 465 ASP C 40
REMARK 465 THR C 54
REMARK 465 THR C 55
REMARK 465 PHE C 56
REMARK 465 ARG C 63
REMARK 465 SER C 64
REMARK 465 ALA C 65
REMARK 465 LYS C 66
REMARK 465 ALA C 67
REMARK 465 PRO C 68
REMARK 465 PRO C 69
REMARK 465 THR C 76
REMARK 465 ALA C 77
REMARK 465 GLN C 78
REMARK 465 LYS C 79
REMARK 465 LEU C 80
REMARK 465 ALA C 81
REMARK 465 GLU C 126
REMARK 465 LEU C 127
REMARK 465 PRO C 128
REMARK 465 THR C 129
REMARK 465 LYS C 130
REMARK 465 LEU C 131
REMARK 465 LEU C 132
REMARK 465 ASP C 133
REMARK 465 HIS C 134
REMARK 465 LEU C 135
REMARK 465 SER C 136
REMARK 465 ASN C 137
REMARK 465 THR C 138
REMARK 465 ALA C 139
REMARK 465 VAL C 140
REMARK 465 LEU C 141
REMARK 465 GLU C 142
REMARK 465 ASP C 143
REMARK 465 GLU C 144
REMARK 465 GLU C 145
REMARK 465 ILE C 146
REMARK 465 SER C 147
REMARK 465 LYS C 148
REMARK 465 ILE C 149
REMARK 465 LEU C 150
REMARK 465 ALA C 151
REMARK 465 ASN C 152
REMARK 465 HIS C 153
REMARK 465 MET C 154
REMARK 465 LEU C 155
REMARK 465 ASN C 156
REMARK 465 ASP C 157
REMARK 465 VAL C 158
REMARK 465 SER C 159
REMARK 465 GLY C 160
REMARK 465 GLY C 161
REMARK 465 SER C 162
REMARK 465 GLU C 163
REMARK 465 ALA C 164
REMARK 465 TRP C 165
REMARK 465 GLN C 166
REMARK 465 ALA C 167
REMARK 465 MET C 168
REMARK 465 GLY C 169
REMARK 465 ASP C 170
REMARK 465 GLU C 171
REMARK 465 VAL C 172
REMARK 465 HIS C 173
REMARK 465 ALA C 174
REMARK 465 ARG C 175
REMARK 465 LEU C 176
REMARK 465 HIS C 177
REMARK 465 LYS C 178
REMARK 465 ASN C 179
REMARK 465 TYR C 180
REMARK 465 ARG C 185
REMARK 465 GLY C 186
REMARK 465 TYR C 187
REMARK 465 PRO C 188
REMARK 465 ARG C 189
REMARK 465 THR C 190
REMARK 465 ILE C 191
REMARK 465 TRP C 210
REMARK 465 THR C 211
REMARK 465 VAL C 212
REMARK 465 GLY C 213
REMARK 465 ALA C 214
REMARK 465 ALA C 215
REMARK 465 THR C 216
REMARK 465 ILE C 225
REMARK 465 VAL C 226
REMARK 465 THR C 227
REMARK 465 ALA C 228
REMARK 465 THR C 229
REMARK 465 LYS C 230
REMARK 465 ALA C 231
REMARK 465 GLY C 232
REMARK 465 VAL C 233
REMARK 465 ASN C 234
REMARK 465 ILE C 235
REMARK 465 GLY C 236
REMARK 465 LEU C 237
REMARK 465 LEU C 238
REMARK 465 PRO C 239
REMARK 465 GLY C 240
REMARK 465 MET C 241
REMARK 465 HIS C 242
REMARK 465 PHE C 243
REMARK 465 PRO C 244
REMARK 465 TYR C 245
REMARK 465 VAL C 246
REMARK 465 SER C 247
REMARK 465 HIS C 248
REMARK 465 PRO C 249
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 DISTANCE
REMARK 500 OH TYR C 255 O HOH C 301 2.06
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 SER A 5 -177.53 -172.39
REMARK 500 SER A 62 -129.90 46.18
REMARK 500 ALA A 102 -122.63 56.71
REMARK 500 GLU A 126 70.41 53.21
REMARK 500 PRO A 196 40.15 -91.98
REMARK 500 MET A 241 -112.39 -129.11
REMARK 500 ASP B 31 -172.92 -66.93
REMARK 500 SER B 62 -129.73 46.09
REMARK 500 ALA B 102 -122.86 57.48
REMARK 500 GLU B 126 71.47 49.17
REMARK 500 PRO B 196 47.11 -93.58
REMARK 500 MET B 241 -112.31 -129.39
REMARK 500 GLN C 19 98.34 -171.70
REMARK 500 THR C 71 -61.96 -25.59
REMARK 500 GLU C 74 74.66 49.39
REMARK 500 ASP C 92 68.63 36.34
REMARK 500 CYS C 101 -67.65 -99.28
REMARK 500 ALA C 102 -110.77 -93.19
REMARK 500 PRO C 196 48.83 -69.53
REMARK 500 PRO C 207 80.83 -60.70
REMARK 500 GLU C 219 -22.60 -142.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 157 VAL B 158 -146.49
REMARK 500 ALA C 48 GLN C 49 148.73
REMARK 500 ASP C 57 MET C 58 -134.41
REMARK 500 PRO C 181 VAL C 182 144.33
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 546 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 547 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 548 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH A 549 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A 550 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH A 551 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH A 552 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH A 553 DISTANCE = 8.38 ANGSTROMS
REMARK 525 HOH B 519 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH C 394 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH C 395 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH C 396 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH C 397 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C 398 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH C 399 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH C 400 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH C 401 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH C 402 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH C 403 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH C 404 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH C 405 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH C 406 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH C 407 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH C 408 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH C 409 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH C 410 DISTANCE = 8.21 ANGSTROMS
REMARK 525 HOH C 411 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH C 412 DISTANCE = 8.49 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZHB A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZHB B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IE4 RELATED DB: PDB
REMARK 900 RELATED ID: 5IE5 RELATED DB: PDB
REMARK 900 RELATED ID: 5IE6 RELATED DB: PDB
DBREF 5IE7 A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5IE7 B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5IE7 C 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 5IE7 ALA A 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 5IE7 HIS A 153 UNP Q8NKB0 VAL 153 ENGINEERED MUTATION
SEQADV 5IE7 ALA B 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 5IE7 HIS B 153 UNP Q8NKB0 VAL 153 ENGINEERED MUTATION
SEQADV 5IE7 ALA C 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 5IE7 HIS C 153 UNP Q8NKB0 VAL 153 ENGINEERED MUTATION
SEQRES 1 A 264 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 A 264 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP VAL
SEQRES 3 A 264 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 A 264 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 A 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 A 264 LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 A 264 LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA LEU
SEQRES 8 A 264 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER GLY
SEQRES 9 A 264 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 A 264 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 A 264 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 A 264 GLU GLU ILE SER LYS ILE LEU ALA ASN HIS MET LEU ASN
SEQRES 13 A 264 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET GLY
SEQRES 14 A 264 ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 A 264 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 A 264 PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 A 264 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 A 264 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 A 264 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 A 264 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 A 264 GLN LYS HIS LEU
SEQRES 1 B 264 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 B 264 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP VAL
SEQRES 3 B 264 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 B 264 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 B 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 B 264 LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 B 264 LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA LEU
SEQRES 8 B 264 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER GLY
SEQRES 9 B 264 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 B 264 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 B 264 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 B 264 GLU GLU ILE SER LYS ILE LEU ALA ASN HIS MET LEU ASN
SEQRES 13 B 264 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET GLY
SEQRES 14 B 264 ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 B 264 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 B 264 PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 B 264 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 B 264 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 B 264 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 B 264 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 B 264 GLN LYS HIS LEU
SEQRES 1 C 264 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 C 264 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP VAL
SEQRES 3 C 264 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 C 264 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 C 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 C 264 LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 C 264 LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA LEU
SEQRES 8 C 264 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER GLY
SEQRES 9 C 264 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 C 264 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 C 264 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 C 264 GLU GLU ILE SER LYS ILE LEU ALA ASN HIS MET LEU ASN
SEQRES 13 C 264 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET GLY
SEQRES 14 C 264 ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 C 264 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 C 264 PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 C 264 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 C 264 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 C 264 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 C 264 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 C 264 GLN LYS HIS LEU
HET ZHB A 300 23
HET ZHB B 301 23
HETNAM ZHB (3S,7S,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,
HETNAM 2 ZHB 10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE
FORMUL 4 ZHB 2(C18 H24 O5)
FORMUL 6 HOH *384(H2 O)
HELIX 1 AA1 GLU A 35 MET A 38 5 4
HELIX 2 AA2 PHE A 39 GLN A 49 1 11
HELIX 3 AA3 MET A 61 ALA A 65 5 5
HELIX 4 AA4 PRO A 68 TYR A 72 5 5
HELIX 5 AA5 THR A 76 LEU A 91 1 16
HELIX 6 AA6 ALA A 102 TYR A 115 1 14
HELIX 7 AA7 LEU A 132 ASN A 137 1 6
HELIX 8 AA8 THR A 138 LEU A 141 5 4
HELIX 9 AA9 GLU A 142 ASP A 157 1 16
HELIX 10 AB1 GLY A 161 MET A 168 1 8
HELIX 11 AB2 GLY A 169 TYR A 187 1 19
HELIX 12 AB3 ILE A 191 ALA A 195 5 5
HELIX 13 AB4 ASP A 199 ARG A 204 1 6
HELIX 14 AB5 PHE A 221 GLY A 232 1 12
HELIX 15 AB6 PHE A 243 HIS A 248 1 6
HELIX 16 AB7 HIS A 248 LYS A 262 1 15
HELIX 17 AB8 GLU B 35 MET B 38 5 4
HELIX 18 AB9 PHE B 39 GLN B 49 1 11
HELIX 19 AC1 MET B 61 ALA B 65 5 5
HELIX 20 AC2 PRO B 68 TYR B 72 5 5
HELIX 21 AC3 THR B 76 LEU B 91 1 16
HELIX 22 AC4 ALA B 102 TYR B 115 1 14
HELIX 23 AC5 LEU B 132 ASN B 137 1 6
HELIX 24 AC6 THR B 138 LEU B 141 5 4
HELIX 25 AC7 GLU B 142 ASP B 157 1 16
HELIX 26 AC8 GLY B 161 MET B 168 1 8
HELIX 27 AC9 GLY B 169 TYR B 187 1 19
HELIX 28 AD1 ILE B 191 ALA B 195 5 5
HELIX 29 AD2 ASP B 199 ARG B 204 1 6
HELIX 30 AD3 PRO B 217 GLY B 232 1 16
HELIX 31 AD4 PHE B 243 HIS B 248 1 6
HELIX 32 AD5 HIS B 248 LYS B 262 1 15
HELIX 33 AD6 SER C 42 ALA C 48 1 7
HELIX 34 AD7 TYR C 83 ASP C 89 1 7
HELIX 35 AD8 ALA C 102 TYR C 115 1 14
HELIX 36 AD9 ASP C 199 ARG C 204 1 6
HELIX 37 AE1 VAL C 251 LYS C 262 1 12
SHEET 1 AA1 8 THR A 3 THR A 9 0
SHEET 2 AA1 8 ILE A 13 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA1 8 ARG A 52 PHE A 56 -1 O VAL A 53 N GLU A 20
SHEET 4 AA1 8 ASP A 25 VAL A 29 1 N VAL A 26 O ARG A 52
SHEET 5 AA1 8 ALA A 96 CYS A 101 1 O THR A 97 N VAL A 27
SHEET 6 AA1 8 ILE A 119 HIS A 125 1 O ASN A 121 N VAL A 98
SHEET 7 AA1 8 LEU A 208 GLY A 213 1 O THR A 211 N CYS A 124
SHEET 8 AA1 8 ASN A 234 LEU A 238 1 O ASN A 234 N TRP A 210
SHEET 1 AA2 8 THR B 3 SER B 8 0
SHEET 2 AA2 8 THR B 14 GLU B 20 -1 O TRP B 15 N ILE B 7
SHEET 3 AA2 8 ARG B 52 PHE B 56 -1 O VAL B 53 N GLU B 20
SHEET 4 AA2 8 ASP B 25 VAL B 29 1 N VAL B 26 O ARG B 52
SHEET 5 AA2 8 ALA B 96 CYS B 101 1 O THR B 97 N VAL B 27
SHEET 6 AA2 8 ILE B 119 HIS B 125 1 O MET B 123 N VAL B 98
SHEET 7 AA2 8 LEU B 208 GLY B 213 1 O THR B 211 N CYS B 124
SHEET 8 AA2 8 ASN B 234 LEU B 238 1 O ASN B 234 N TRP B 210
SHEET 1 AA3 2 ASP C 25 LEU C 28 0
SHEET 2 AA3 2 ALA C 96 TRP C 99 1 O THR C 97 N VAL C 27
SITE 1 AC1 14 GLY A 32 ALA A 102 SER A 103 PRO A 128
SITE 2 AC1 14 LEU A 135 HIS A 153 VAL A 158 TRP A 183
SITE 3 AC1 14 TYR A 187 PRO A 188 ILE A 191 PRO A 192
SITE 4 AC1 14 HIS A 242 HOH A 463
SITE 1 AC2 12 GLY B 32 ALA B 102 SER B 103 HIS B 153
SITE 2 AC2 12 MET B 154 VAL B 158 TRP B 183 TYR B 187
SITE 3 AC2 12 PRO B 188 PRO B 192 HIS B 242 HOH B 445
CRYST1 86.408 86.408 470.449 90.00 90.00 120.00 P 61 2 2 36
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 0.011573 0.006682 0.000000 0.00000
SCALE2 0.000000 0.013363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002126 0.00000
TER 2024 LEU A 264
TER 4048 LEU B 264
TER 5037 LEU C 264
MASTER 538 0 2 37 18 0 7 6 5464 3 46 63
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