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HEADER HYDROLASE 25-FEB-16 5IE5
TITLE CRYSTAL STRUCTURE OF A LACTONASE DOUBLE MUTANT IN COMPLEX WITH
TITLE 2 SUBSTRATE A
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)
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 5IE5 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. 2.39 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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 40427
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2046
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) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2895
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5301
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 301
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : 0.83000
REMARK 3 B33 (A**2) : -2.70000
REMARK 3 B12 (A**2) : 0.42000
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): 0.294
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.563
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5477 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5140 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7466 ; 1.525 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11851 ; 0.990 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 679 ; 8.936 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;36.472 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 841 ;19.582 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.758 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 851 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6106 ; 0.018 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1190 ; 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): 2755 ; 3.028 ; 3.107
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2754 ; 3.027 ; 3.107
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3421 ; 4.274 ; 4.639
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3422 ; 4.274 ; 4.639
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2722 ; 3.913 ; 3.480
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2722 ; 3.913 ; 3.480
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4046 ; 5.673 ; 5.067
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6344 ; 7.857 ;26.095
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6286 ; 7.855 ;25.886
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 30120 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 5IE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218712.
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 : BL13B1
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 : 42998
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
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: 3XZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.96
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 157.28733
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 314.57467
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 235.93100
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 393.21833
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 78.64367
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 157.28733
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 314.57467
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 393.21833
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 235.93100
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 78.64367
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 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 THR C 54
REMARK 465 THR C 55
REMARK 465 PRO C 59
REMARK 465 GLY C 60
REMARK 465 MET C 61
REMARK 465 SER C 62
REMARK 465 ARG C 63
REMARK 465 SER C 64
REMARK 465 ALA C 65
REMARK 465 LYS C 66
REMARK 465 HIS C 125
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 PRO C 181
REMARK 465 VAL C 182
REMARK 465 TRP C 210
REMARK 465 THR C 211
REMARK 465 VAL C 212
REMARK 465 GLY C 213
REMARK 465 PRO C 217
REMARK 465 THR C 218
REMARK 465 GLU C 219
REMARK 465 SER C 220
REMARK 465 ILE C 225
REMARK 465 VAL C 226
REMARK 465 THR C 229
REMARK 465 LYS C 230
REMARK 465 ILE C 235
REMARK 465 GLY C 236
REMARK 465 LEU C 237
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 O LEU C 88 O ASP C 92 1.88
REMARK 500 OD1 ASP C 209 ND2 ASN C 234 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 491 O HOH B 482 6555 2.09
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 2 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 120 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 2 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 120 NE - CZ - NH2 ANGL. DEV. = -3.8 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 31 -177.09 -66.18
REMARK 500 SER A 62 -127.80 45.48
REMARK 500 TYR A 72 21.94 -140.25
REMARK 500 ALA A 102 -124.62 60.57
REMARK 500 THR A 129 -2.54 -145.28
REMARK 500 PRO A 196 44.08 -83.17
REMARK 500 MET A 241 -116.13 -132.41
REMARK 500 ASP B 31 -176.65 -60.67
REMARK 500 SER B 62 -127.97 49.08
REMARK 500 ALA B 102 -123.98 60.19
REMARK 500 GLU B 126 70.01 52.28
REMARK 500 PRO B 196 40.84 -81.28
REMARK 500 MET B 241 -110.58 -127.29
REMARK 500 GLN C 19 106.43 -160.46
REMARK 500 GLN C 37 31.27 -71.36
REMARK 500 ASP C 92 -125.12 25.07
REMARK 500 ILE C 93 84.24 69.38
REMARK 500 ALA C 102 -128.32 67.26
REMARK 500 PRO C 196 40.09 -78.65
REMARK 500 MET C 241 -82.04 -122.08
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 LEU C 91 ASP C 92 -140.46
REMARK 500 ALA C 214 ALA C 215 -135.63
REMARK 500 ASP C 223 ASN C 224 143.57
REMARK 500 LEU C 238 PRO C 239 -147.36
REMARK 500 ASP C 250 VAL C 251 124.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 120 0.10 SIDE CHAIN
REMARK 500 ARG B 120 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 197 -11.95
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 512 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 513 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 514 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A 515 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH A 516 DISTANCE = 8.07 ANGSTROMS
REMARK 525 HOH B 512 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 513 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B 514 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH C 360 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH C 361 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C 362 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH C 363 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH C 364 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH C 365 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH C 366 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH C 367 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH C 368 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH C 369 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH C 370 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH C 371 DISTANCE = 7.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IE4 RELATED DB: PDB
REMARK 900 RELATED ID: 5IE6 RELATED DB: PDB
REMARK 900 RELATED ID: 5IE7 RELATED DB: PDB
DBREF 5IE5 A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5IE5 B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5IE5 C 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 5IE5 ALA A 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 5IE5 HIS A 153 UNP Q8NKB0 VAL 153 ENGINEERED MUTATION
SEQADV 5IE5 ALA B 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 5IE5 HIS B 153 UNP Q8NKB0 VAL 153 ENGINEERED MUTATION
SEQADV 5IE5 ALA C 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 5IE5 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 36J A 300 23
HET 36J B 301 23
HETNAM 36J (3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,
HETNAM 2 36J 10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE
FORMUL 4 36J 2(C18 H24 O5)
FORMUL 6 HOH *301(H2 O)
HELIX 1 AA1 GLU A 35 MET A 38 5 4
HELIX 2 AA2 PHE A 39 ALA A 48 1 10
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 ALA A 167 1 7
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 PRO A 217 ALA A 231 1 15
HELIX 15 AB6 PHE A 243 HIS A 248 1 6
HELIX 16 AB7 HIS A 248 HIS A 263 1 16
HELIX 17 AB8 GLU B 35 MET B 38 5 4
HELIX 18 AB9 PHE B 39 ALA B 48 1 10
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 ALA B 167 1 7
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 ALA B 231 1 15
HELIX 31 AD4 PHE B 243 HIS B 248 1 6
HELIX 32 AD5 HIS B 248 LEU B 264 1 17
HELIX 33 AD6 SER C 41 ILE C 46 1 6
HELIX 34 AD7 ALA C 47 GLY C 50 5 4
HELIX 35 AD8 PRO C 68 TYR C 72 5 5
HELIX 36 AD9 THR C 76 LEU C 91 1 16
HELIX 37 AE1 ALA C 102 TYR C 115 1 14
HELIX 38 AE2 ILE C 191 ALA C 195 5 5
HELIX 39 AE3 ASP C 199 ARG C 204 1 6
HELIX 40 AE4 PHE C 252 HIS C 263 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 MET A 123 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 GLN B 19 N THR B 3
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 4 ASP C 25 VAL C 29 0
SHEET 2 AA3 4 ALA C 96 GLY C 100 1 O TRP C 99 N VAL C 29
SHEET 3 AA3 4 ILE C 119 MET C 123 1 O ASN C 121 N VAL C 98
SHEET 4 AA3 4 LEU C 208 ASP C 209 1 O ASP C 209 N ALA C 122
SITE 1 AC1 14 GLY A 32 ALA A 102 SER A 103 LEU A 135
SITE 2 AC1 14 HIS A 153 MET A 154 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 PHE A 221 HIS A 242
SITE 1 AC2 15 GLY B 32 LEU B 33 ALA B 102 SER B 103
SITE 2 AC2 15 PRO B 128 LEU B 135 HIS B 153 MET B 154
SITE 3 AC2 15 TRP B 183 TYR B 187 PRO B 188 ILE B 191
SITE 4 AC2 15 PRO B 192 PHE B 221 HIS B 242
CRYST1 86.164 86.164 471.862 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 0.011606 0.006701 0.000000 0.00000
SCALE2 0.000000 0.013401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002119 0.00000
TER 2024 LEU A 264
TER 4048 LEU B 264
TER 5304 LEU C 264
MASTER 568 0 2 40 20 0 8 6 5648 3 46 63
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