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HEADER HYDROLASE 09-OCT-23 8QRJ
TITLE LCC-ICCG PETASE MUTANT H218Y
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEAF-BRANCH COMPOST CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LCC, PETASE, HYDROLASE, DIRECT ENZYME EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.ORR,Y.NIV,M.BARAKAT,A.BOGINYA,M.DESSAU,L.AFRIAT-JURNOU
REVDAT 1 18-SEP-24 8QRJ 0
JRNL AUTH G.ORR,Y.NIV,M.BARAKAT,A.BOGINYA,M.DESSAU,L.AFRIAT-JURNOU
JRNL TITL STREAMLINED SCREENING OF EXTRACELLULARLY EXPRESSED PETASE
JRNL TITL 2 LIBRARIES FOR IMPROVED POLYETHYLENE TEREPHTHALATE
JRNL TITL 3 DEGRADATION.
JRNL REF BIOTECHNOL J V. 19 00021 2024
JRNL REFN ESSN 1860-7314
JRNL PMID 38987219
JRNL DOI 10.1002/BIOT.202400021
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 56565
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1700 - 3.8500 0.95 2851 146 0.1377 0.1273
REMARK 3 2 3.8500 - 3.0600 0.93 2716 125 0.1398 0.1426
REMARK 3 3 3.0600 - 2.6700 0.95 2701 154 0.1506 0.1793
REMARK 3 4 2.6700 - 2.4300 0.94 2658 162 0.1498 0.1732
REMARK 3 5 2.4300 - 2.2500 0.96 2710 153 0.1442 0.1456
REMARK 3 6 2.2500 - 2.1200 0.96 2724 136 0.1373 0.1564
REMARK 3 7 2.1200 - 2.0200 0.96 2714 146 0.1459 0.1744
REMARK 3 8 2.0100 - 1.9300 0.96 2701 148 0.1615 0.1850
REMARK 3 9 1.9300 - 1.8500 0.97 2724 144 0.1713 0.2018
REMARK 3 10 1.8500 - 1.7900 0.96 2698 132 0.1718 0.1797
REMARK 3 11 1.7900 - 1.7300 0.97 2729 142 0.1814 0.2217
REMARK 3 12 1.7300 - 1.6800 0.97 2704 149 0.1977 0.2056
REMARK 3 13 1.6800 - 1.6400 0.94 2625 150 0.2174 0.2567
REMARK 3 14 1.6400 - 1.6000 0.95 2653 140 0.2352 0.2693
REMARK 3 15 1.6000 - 1.5600 0.96 2693 143 0.2447 0.2669
REMARK 3 16 1.5600 - 1.5300 0.94 2628 144 0.2480 0.2592
REMARK 3 17 1.5300 - 1.5000 0.93 2601 137 0.2588 0.2631
REMARK 3 18 1.5000 - 1.4700 0.93 2599 153 0.2696 0.3125
REMARK 3 19 1.4400 - 1.4200 0.95 2631 134 0.3076 0.3559
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2046
REMARK 3 ANGLE : 0.826 2799
REMARK 3 CHIRALITY : 0.078 315
REMARK 3 PLANARITY : 0.010 365
REMARK 3 DIHEDRAL : 11.490 738
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4305 25.6475 23.3517
REMARK 3 T TENSOR
REMARK 3 T11: 0.0916 T22: 0.1026
REMARK 3 T33: 0.0922 T12: 0.0099
REMARK 3 T13: 0.0005 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.1431 L22: 1.7911
REMARK 3 L33: 1.4497 L12: -0.1389
REMARK 3 L13: -0.0013 L23: 0.3859
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: 0.0169 S13: 0.0950
REMARK 3 S21: -0.0649 S22: -0.0028 S23: 0.0721
REMARK 3 S31: -0.0448 S32: -0.0395 S33: -0.0060
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8365 16.4551 29.2542
REMARK 3 T TENSOR
REMARK 3 T11: 0.1120 T22: 0.1214
REMARK 3 T33: 0.1059 T12: 0.0020
REMARK 3 T13: 0.0006 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.7378 L22: 2.7892
REMARK 3 L33: 0.8028 L12: -0.3049
REMARK 3 L13: 0.2825 L23: -0.9622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0170 S12: 0.0114 S13: -0.0037
REMARK 3 S21: 0.0319 S22: 0.0609 S23: 0.1670
REMARK 3 S31: 0.0269 S32: -0.1076 S33: -0.0797
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3844 10.0078 26.5078
REMARK 3 T TENSOR
REMARK 3 T11: 0.1143 T22: 0.1100
REMARK 3 T33: 0.1129 T12: 0.0002
REMARK 3 T13: 0.0013 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.2354 L22: 7.8782
REMARK 3 L33: 1.3097 L12: -0.1130
REMARK 3 L13: 0.2802 L23: -2.0080
REMARK 3 S TENSOR
REMARK 3 S11: 0.0377 S12: -0.0196 S13: -0.0468
REMARK 3 S21: -0.1029 S22: 0.0308 S23: 0.2383
REMARK 3 S31: 0.1546 S32: -0.0633 S33: -0.0794
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 128 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4081 16.6967 21.7311
REMARK 3 T TENSOR
REMARK 3 T11: 0.1066 T22: 0.1292
REMARK 3 T33: 0.1137 T12: 0.0060
REMARK 3 T13: -0.0038 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.2709 L22: 1.2247
REMARK 3 L33: 0.5514 L12: 0.3191
REMARK 3 L13: -0.3830 L23: -0.3555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0281 S12: 0.0165 S13: -0.0150
REMARK 3 S21: -0.0723 S22: -0.0359 S23: -0.0251
REMARK 3 S31: 0.0208 S32: 0.0186 S33: 0.0257
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2367 14.4275 42.0210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0958 T22: 0.0993
REMARK 3 T33: 0.1077 T12: 0.0044
REMARK 3 T13: -0.0046 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.9619 L22: 0.8518
REMARK 3 L33: 1.5944 L12: 0.0529
REMARK 3 L13: -0.5955 L23: -0.0637
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0673 S13: -0.0189
REMARK 3 S21: 0.0612 S22: -0.0036 S23: -0.0332
REMARK 3 S31: 0.0685 S32: 0.0955 S33: 0.0139
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0059 15.9893 40.8143
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.1128
REMARK 3 T33: 0.1320 T12: -0.0113
REMARK 3 T13: 0.0107 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.7408 L22: 1.8108
REMARK 3 L33: 2.6709 L12: 0.3195
REMARK 3 L13: 0.3545 L23: -0.0077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: -0.0575 S13: 0.1307
REMARK 3 S21: -0.0309 S22: -0.0217 S23: 0.1116
REMARK 3 S31: 0.0836 S32: -0.2210 S33: -0.0054
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 250 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5148 29.2065 41.9501
REMARK 3 T TENSOR
REMARK 3 T11: 0.1162 T22: 0.1074
REMARK 3 T33: 0.1169 T12: -0.0062
REMARK 3 T13: 0.0120 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.6051 L22: 0.8719
REMARK 3 L33: 2.2565 L12: 0.2911
REMARK 3 L13: -0.7132 L23: -0.6465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0861 S12: -0.0962 S13: 0.1067
REMARK 3 S21: 0.0920 S22: -0.0367 S23: -0.0190
REMARK 3 S31: -0.2223 S32: 0.1221 S33: -0.0578
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8QRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1292133744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8731
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93953
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
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 (%) : 82.0
REMARK 200 DATA REDUNDANCY : 1.770
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.6500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.89400
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M NA-FORMATE PH=7.3,
REMARK 280 PH 7.3, VAPOR DIFFUSION, TEMPERATURE 289K
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 40.47500
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 40.47500
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 40.95000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.25500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.95000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.25500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.47500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.95000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.25500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.47500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.95000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.25500
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 682 LIES ON A SPECIAL POSITION.
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 ASP A 2
REMARK 465 GLY A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 TRP A 6
REMARK 465 ARG A 7
REMARK 465 VAL A 8
REMARK 465 ARG A 9
REMARK 465 THR A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 LEU A 13
REMARK 465 MET A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 LEU A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 TRP A 23
REMARK 465 ALA A 24
REMARK 465 LEU A 25
REMARK 465 VAL A 26
REMARK 465 TRP A 27
REMARK 465 ALA A 28
REMARK 465 SER A 29
REMARK 465 PRO A 30
REMARK 465 SER A 31
REMARK 465 VAL A 32
REMARK 465 GLU A 33
REMARK 465 ALA A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 293
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 HOH A 808 O HOH A 827 1.87
REMARK 500 O HOH A 769 O HOH A 804 1.91
REMARK 500 O HOH A 414 O HOH A 441 1.93
REMARK 500 O HOH A 575 O HOH A 615 1.99
REMARK 500 O HOH A 703 O HOH A 753 2.01
REMARK 500 O HOH A 686 O HOH A 721 2.04
REMARK 500 O HOH A 683 O HOH A 821 2.06
REMARK 500 O HOH A 516 O HOH A 768 2.06
REMARK 500 O HOH A 618 O HOH A 641 2.07
REMARK 500 O HOH A 602 O HOH A 805 2.09
REMARK 500 O HOH A 528 O HOH A 553 2.12
REMARK 500 O HOH A 441 O HOH A 732 2.13
REMARK 500 NH1 ARG A 107 O HOH A 401 2.16
REMARK 500 O HOH A 702 O HOH A 706 2.16
REMARK 500 O HOH A 738 O HOH A 769 2.16
REMARK 500 O HOH A 760 O HOH A 834 2.17
REMARK 500 O HOH A 571 O HOH A 707 2.18
REMARK 500 O HOH A 777 O HOH A 794 2.18
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 599 O HOH A 599 4556 1.94
REMARK 500 O HOH A 618 O HOH A 781 6554 2.17
REMARK 500 O HOH A 545 O HOH A 687 4556 2.18
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 THR A 96 -3.80 71.35
REMARK 500 SER A 165 -122.52 64.27
REMARK 500 THR A 188 58.28 33.65
REMARK 500 TYR A 218 -82.35 -124.24
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 837 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A 842 DISTANCE = 6.28 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 65 O
REMARK 620 2 VAL A 68 O 83.0
REMARK 620 3 PHE A 71 O 106.8 96.4
REMARK 620 4 HOH A 516 O 177.9 95.9 71.5
REMARK 620 5 HOH A 542 O 108.1 166.4 73.2 72.7
REMARK 620 6 HOH A 702 O 112.6 78.8 139.2 68.8 103.2
REMARK 620 7 HOH A 706 O 81.7 106.9 156.1 100.3 82.9 45.2
REMARK 620 N 1 2 3 4 5 6
DBREF 8QRJ A 1 293 UNP G9BY57 PETH_UNKP 1 293
SEQADV 8QRJ GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 8QRJ TYR A 218 UNP G9BY57 HIS 218 ENGINEERED MUTATION
SEQADV 8QRJ CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 8QRJ ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 8QRJ CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQRES 1 A 293 MET ASP GLY VAL LEU TRP ARG VAL ARG THR ALA ALA LEU
SEQRES 2 A 293 MET ALA ALA LEU LEU ALA LEU ALA ALA TRP ALA LEU VAL
SEQRES 3 A 293 TRP ALA SER PRO SER VAL GLU ALA GLN SER ASN PRO TYR
SEQRES 4 A 293 GLN ARG GLY PRO ASN PRO THR ARG SER ALA LEU THR ALA
SEQRES 5 A 293 ASP GLY PRO PHE SER VAL ALA THR TYR THR VAL SER ARG
SEQRES 6 A 293 LEU SER VAL SER GLY PHE GLY GLY GLY VAL ILE TYR TYR
SEQRES 7 A 293 PRO THR GLY THR SER LEU THR PHE GLY GLY ILE ALA MET
SEQRES 8 A 293 SER PRO GLY TYR THR ALA ASP ALA SER SER LEU ALA TRP
SEQRES 9 A 293 LEU GLY ARG ARG LEU ALA SER HIS GLY PHE VAL VAL LEU
SEQRES 10 A 293 VAL ILE ASN THR ASN SER ARG PHE ASP GLY PRO ASP SER
SEQRES 11 A 293 ARG ALA SER GLN LEU SER ALA ALA LEU ASN TYR LEU ARG
SEQRES 12 A 293 THR SER SER PRO SER ALA VAL ARG ALA ARG LEU ASP ALA
SEQRES 13 A 293 ASN ARG LEU ALA VAL ALA GLY HIS SER MET GLY GLY GLY
SEQRES 14 A 293 GLY THR LEU ARG ILE ALA GLU GLN ASN PRO SER LEU LYS
SEQRES 15 A 293 ALA ALA VAL PRO LEU THR PRO TRP HIS THR ASP LYS THR
SEQRES 16 A 293 PHE ASN THR SER VAL PRO VAL LEU ILE VAL GLY ALA GLU
SEQRES 17 A 293 ALA ASP THR VAL ALA PRO VAL SER GLN TYR ALA ILE PRO
SEQRES 18 A 293 PHE TYR GLN ASN LEU PRO SER THR THR PRO LYS VAL TYR
SEQRES 19 A 293 VAL GLU LEU CYS ASN ALA SER HIS ILE ALA PRO ASN SER
SEQRES 20 A 293 ASN ASN ALA ALA ILE SER VAL TYR THR ILE SER TRP MET
SEQRES 21 A 293 LYS LEU TRP VAL ASP ASN ASP THR ARG TYR ARG GLN PHE
SEQRES 22 A 293 LEU CYS ASN VAL ASN ASP PRO ALA LEU CYS ASP PHE ARG
SEQRES 23 A 293 THR ASN ASN ARG HIS CYS GLN
HET EDO A 301 4
HET P33 A 302 22
HET CA A 303 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN P33 HEPTAETHYLENE GLYCOL; PEG330
FORMUL 2 EDO C2 H6 O2
FORMUL 3 P33 C14 H30 O8
FORMUL 4 CA CA 2+
FORMUL 5 HOH *442(H2 O)
HELIX 1 AA1 ARG A 47 ALA A 52 5 6
HELIX 2 AA2 SER A 64 VAL A 68 5 5
HELIX 3 AA3 ASP A 98 SER A 101 5 4
HELIX 4 AA4 LEU A 102 HIS A 112 1 11
HELIX 5 AA5 GLY A 127 SER A 145 1 19
HELIX 6 AA6 PRO A 147 ARG A 153 1 7
HELIX 7 AA7 SER A 165 ASN A 178 1 14
HELIX 8 AA8 TYR A 218 LEU A 226 1 9
HELIX 9 AA9 ILE A 243 SER A 247 5 5
HELIX 10 AB1 ASN A 249 ASP A 265 1 17
HELIX 11 AB2 ASP A 267 LEU A 274 5 8
SHEET 1 AA1 6 SER A 57 VAL A 63 0
SHEET 2 AA1 6 GLY A 74 THR A 80 -1 O ILE A 76 N TYR A 61
SHEET 3 AA1 6 VAL A 115 ILE A 119 -1 O VAL A 116 N TYR A 77
SHEET 4 AA1 6 PHE A 86 SER A 92 1 N ILE A 89 O LEU A 117
SHEET 5 AA1 6 LEU A 154 HIS A 164 1 O ASP A 155 N PHE A 86
SHEET 6 AA1 6 ALA A 184 LEU A 187 1 O LEU A 187 N GLY A 163
SHEET 1 AA2 3 VAL A 202 ALA A 207 0
SHEET 2 AA2 3 LYS A 232 LEU A 237 1 O VAL A 235 N GLY A 206
SHEET 3 AA2 3 LEU A 282 THR A 287 -1 O CYS A 283 N GLU A 236
SSBOND 1 CYS A 238 CYS A 283 1555 1555 2.07
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.05
LINK O ARG A 65 CA CA A 303 1555 1555 2.65
LINK O VAL A 68 CA CA A 303 1555 1555 2.69
LINK O PHE A 71 CA CA A 303 1555 1555 2.77
LINK CA CA A 303 O HOH A 516 1555 1555 2.92
LINK CA CA A 303 O HOH A 542 1555 1555 2.84
LINK CA CA A 303 O HOH A 702 1555 1555 2.80
LINK CA CA A 303 O HOH A 706 1555 1555 2.82
CRYST1 81.900 94.510 80.950 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012210 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012353 0.00000
TER 1967 CYS A 292
MASTER 480 0 3 11 9 0 0 6 2410 1 39 23
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