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HEADER HYDROLASE 18-OCT-22 8ETY
TITLE ANCESTRAL PETASE 35_442
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYETHYLENE TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: ANCESTRAL PETASE 35_442
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET, PETASE, PLASTIC DEGRADATION, ANCESTRAL SEQUENCE RECONSTRUCTION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SAUNDERS,R.L.FRKIC,C.J.JACKSON
REVDAT 1 01-NOV-23 8ETY 0
JRNL AUTH J.SAUNDERS,R.L.FRKIC,C.J.JACKSON
JRNL TITL ANCESTRAL PETASE 35_442
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.54 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) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 43071
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2102
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 40.3700 - 3.8000 1.00 2910 156 0.1490 0.1673
REMARK 3 2 3.8000 - 3.0100 1.00 2792 143 0.1474 0.1777
REMARK 3 3 3.0100 - 2.6300 1.00 2738 156 0.1698 0.1944
REMARK 3 4 2.6300 - 2.3900 1.00 2766 131 0.1597 0.2239
REMARK 3 5 2.3900 - 2.2200 1.00 2719 150 0.1563 0.1801
REMARK 3 6 2.2200 - 2.0900 1.00 2744 120 0.1589 0.2018
REMARK 3 7 2.0900 - 1.9900 1.00 2724 135 0.1696 0.1901
REMARK 3 8 1.9900 - 1.9000 1.00 2726 133 0.1739 0.2022
REMARK 3 9 1.9000 - 1.8300 1.00 2692 152 0.1836 0.2399
REMARK 3 10 1.8300 - 1.7600 1.00 2732 131 0.2085 0.2415
REMARK 3 11 1.7600 - 1.7100 1.00 2667 143 0.2493 0.2858
REMARK 3 12 1.7100 - 1.6600 1.00 2713 141 0.2482 0.2870
REMARK 3 13 1.6600 - 1.6200 1.00 2680 146 0.2551 0.2765
REMARK 3 14 1.6200 - 1.5800 1.00 2700 141 0.2592 0.2610
REMARK 3 15 1.5800 - 1.5400 0.99 2666 124 0.2823 0.2968
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.15
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6175 -0.9597 7.0608
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.1338
REMARK 3 T33: 0.1087 T12: -0.0088
REMARK 3 T13: -0.0219 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 3.9740 L22: 1.7847
REMARK 3 L33: 5.6200 L12: -0.8529
REMARK 3 L13: -1.4432 L23: -1.2445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: 0.0560 S13: -0.2720
REMARK 3 S21: -0.1193 S22: -0.0546 S23: 0.0814
REMARK 3 S31: 0.1994 S32: 0.0892 S33: 0.0479
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7639 22.0591 9.3047
REMARK 3 T TENSOR
REMARK 3 T11: 0.2475 T22: 0.2115
REMARK 3 T33: 0.3518 T12: 0.0367
REMARK 3 T13: -0.0683 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.0193 L22: 2.1811
REMARK 3 L33: 3.8126 L12: -0.8869
REMARK 3 L13: -0.1145 L23: 2.4135
REMARK 3 S TENSOR
REMARK 3 S11: 0.0690 S12: 0.1633 S13: 0.2277
REMARK 3 S21: -0.5999 S22: -0.3839 S23: 0.3358
REMARK 3 S31: -0.5876 S32: -0.5357 S33: 0.2017
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4609 6.3391 5.6905
REMARK 3 T TENSOR
REMARK 3 T11: 0.1657 T22: 0.1764
REMARK 3 T33: 0.1658 T12: -0.0213
REMARK 3 T13: -0.0064 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 2.3323 L22: 2.8804
REMARK 3 L33: 3.5191 L12: 1.2032
REMARK 3 L13: 0.1722 L23: -0.4854
REMARK 3 S TENSOR
REMARK 3 S11: -0.1271 S12: 0.1386 S13: 0.0723
REMARK 3 S21: -0.3180 S22: -0.0141 S23: -0.0056
REMARK 3 S31: 0.2563 S32: -0.0898 S33: 0.1294
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8693 21.0870 11.5232
REMARK 3 T TENSOR
REMARK 3 T11: 0.1733 T22: 0.1350
REMARK 3 T33: 0.2056 T12: -0.0111
REMARK 3 T13: -0.0495 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.2469 L22: 2.9327
REMARK 3 L33: 1.8180 L12: 0.6514
REMARK 3 L13: 0.1104 L23: 0.6439
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: 0.0394 S13: 0.3237
REMARK 3 S21: -0.0327 S22: -0.0682 S23: 0.2647
REMARK 3 S31: -0.3132 S32: 0.0293 S33: 0.0879
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2037 14.6105 16.8753
REMARK 3 T TENSOR
REMARK 3 T11: 0.1752 T22: 0.1733
REMARK 3 T33: 0.2658 T12: 0.0121
REMARK 3 T13: 0.0006 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 3.1779 L22: 4.4212
REMARK 3 L33: 1.1464 L12: 2.1861
REMARK 3 L13: 0.9524 L23: 1.2348
REMARK 3 S TENSOR
REMARK 3 S11: -0.1586 S12: -0.0367 S13: 0.3494
REMARK 3 S21: 0.0241 S22: -0.0113 S23: 0.6651
REMARK 3 S31: -0.1118 S32: -0.0716 S33: 0.2119
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 248 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5033 13.9498 20.3502
REMARK 3 T TENSOR
REMARK 3 T11: 0.1451 T22: 0.1577
REMARK 3 T33: 0.1143 T12: -0.0312
REMARK 3 T13: -0.0154 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.0408 L22: 2.0930
REMARK 3 L33: 0.9823 L12: 0.0760
REMARK 3 L13: 0.1904 L23: 0.0666
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: -0.0308 S13: 0.1091
REMARK 3 S21: 0.0982 S22: -0.0595 S23: 0.0187
REMARK 3 S31: -0.1149 S32: 0.1054 S33: 0.0665
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 249 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5271 -8.5859 19.3217
REMARK 3 T TENSOR
REMARK 3 T11: 0.1759 T22: 0.2913
REMARK 3 T33: 0.1818 T12: -0.0211
REMARK 3 T13: 0.0319 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 2.5984 L22: 2.9222
REMARK 3 L33: 8.6814 L12: 1.6170
REMARK 3 L13: 4.4016 L23: 4.2009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: -0.0233 S13: 0.1240
REMARK 3 S21: -0.1726 S22: -0.0302 S23: 0.1071
REMARK 3 S31: -0.3404 S32: -0.3889 S33: -0.0463
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 8ETY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1000269071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43143
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 40.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.18800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.40
REMARK 200 R MERGE FOR SHELL (I) : 5.98800
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: 6QGC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M BIS TRIS PROPANE PH
REMARK 280 6.5, 0.2M SODIUM MALONATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
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
REMARK 290 7555 -X+1/2,Y+1/2,-Z
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 0.00000
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 0.00000
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 34.87950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.24900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.87950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.24900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.87950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.24900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.87950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.24900
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 416 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 523 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 594 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 595 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 596 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 629 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 641 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 643 O HOH A 686 2.16
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 132 -122.17 65.00
REMARK 500 THR A 155 60.56 33.71
REMARK 500 HIS A 186 -86.35 -127.27
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 718 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A 719 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A 720 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 721 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 722 DISTANCE = 7.64 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 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 33 O
REMARK 620 2 ALA A 36 O 94.2
REMARK 620 3 PHE A 39 O 107.4 82.9
REMARK 620 4 HOH A 574 O 171.4 91.6 79.7
REMARK 620 5 HOH A 605 O 79.8 81.9 163.6 94.7
REMARK 620 6 HOH A 618 O 100.0 157.9 76.8 76.5 117.1
REMARK 620 N 1 2 3 4 5
DBREF 8ETY A -20 261 PDB 8ETY 8ETY -20 261
SEQRES 1 A 282 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 282 LEU VAL PRO ARG GLY SER HIS MET MET ALA ALA ASN PRO
SEQRES 3 A 282 TYR GLU ARG GLY PRO ASP PRO THR GLU SER SER LEU GLU
SEQRES 4 A 282 ALA SER SER GLY PRO PHE SER VAL SER GLU THR SER VAL
SEQRES 5 A 282 SER ARG LEU SER ALA SER GLY PHE GLY GLY GLY THR ILE
SEQRES 6 A 282 TYR TYR PRO THR THR THR SER GLU GLY THR TYR GLY ALA
SEQRES 7 A 282 VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER SER
SEQRES 8 A 282 ILE ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 9 A 282 VAL VAL ILE THR ILE ASP THR ASN THR THR PHE ASP GLN
SEQRES 10 A 282 PRO ASP SER ARG ALA ARG GLN LEU MET ALA ALA LEU ASN
SEQRES 11 A 282 TYR LEU VAL ASN ARG SER SER VAL ARG SER ARG ILE ASP
SEQRES 12 A 282 SER SER ARG LEU ALA VAL MET GLY HIS SER MET GLY GLY
SEQRES 13 A 282 GLY GLY THR LEU ARG ALA ALA GLU ASP ASN PRO SER LEU
SEQRES 14 A 282 LYS ALA ALA ILE PRO LEU THR PRO TRP HIS THR ASN LYS
SEQRES 15 A 282 ASN TRP SER SER VAL ARG VAL PRO THR LEU ILE ILE GLY
SEQRES 16 A 282 ALA GLU ASN ASP THR ILE ALA PRO VAL SER SER HIS ALA
SEQRES 17 A 282 LYS PRO PHE TYR ASN SER LEU PRO SER SER THR PRO LYS
SEQRES 18 A 282 ALA TYR LEU GLU LEU ASN GLY ALA SER HIS PHE ALA PRO
SEQRES 19 A 282 ASN SER SER ASN THR THR ILE GLY LYS TYR SER ILE ALA
SEQRES 20 A 282 TRP LEU LYS ARG PHE VAL ASP ASN ASP THR ARG TYR SER
SEQRES 21 A 282 GLN PHE LEU CYS PRO ALA PRO HIS ASP ASP SER ALA ILE
SEQRES 22 A 282 SER GLU TYR ARG SER THR CYS PRO TYR
HET NA A 301 1
HET PEG A 302 7
HET PEG A 303 7
HET EDO A 304 4
HET 1PE A 305 16
HET GOL A 306 6
HET EDO A 307 4
HET EDO A 308 4
HET EDO A 309 4
HET SO4 A 310 5
HET EDO A 311 4
HET EDO A 312 4
HET EDO A 313 4
HET EDO A 314 4
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN 1PE PEG400
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NA NA 1+
FORMUL 3 PEG 2(C4 H10 O3)
FORMUL 5 EDO 8(C2 H6 O2)
FORMUL 6 1PE C10 H22 O6
FORMUL 7 GOL C3 H8 O3
FORMUL 11 SO4 O4 S 2-
FORMUL 16 HOH *322(H2 O)
HELIX 1 AA1 THR A 13 ALA A 19 1 7
HELIX 2 AA2 THR A 67 ALA A 72 5 6
HELIX 3 AA3 TRP A 73 SER A 80 1 8
HELIX 4 AA4 GLN A 96 ARG A 114 1 19
HELIX 5 AA5 VAL A 117 SER A 119 5 3
HELIX 6 AA6 SER A 132 ASN A 145 1 14
HELIX 7 AA7 HIS A 186 LEU A 194 1 9
HELIX 8 AA8 PHE A 211 SER A 215 5 5
HELIX 9 AA9 ASN A 217 ASP A 233 1 17
HELIX 10 AB1 ASP A 235 ARG A 237 5 3
HELIX 11 AB2 TYR A 238 CYS A 243 1 6
HELIX 12 AB3 ALA A 245 ASP A 249 5 5
SHEET 1 AA1 6 VAL A 26 VAL A 31 0
SHEET 2 AA1 6 GLY A 42 PRO A 47 -1 O ILE A 44 N THR A 29
SHEET 3 AA1 6 VAL A 84 ILE A 88 -1 O VAL A 85 N TYR A 45
SHEET 4 AA1 6 TYR A 55 SER A 61 1 N VAL A 58 O VAL A 84
SHEET 5 AA1 6 ILE A 121 HIS A 131 1 O ASP A 122 N TYR A 55
SHEET 6 AA1 6 ALA A 150 LEU A 154 1 O LEU A 154 N GLY A 130
SHEET 1 AA2 2 THR A 170 ALA A 175 0
SHEET 2 AA2 2 LYS A 200 LEU A 205 1 O LEU A 205 N GLY A 174
SSBOND 1 CYS A 243 CYS A 259 1555 2655 2.05
LINK O ARG A 33 NA NA A 301 1555 1555 2.46
LINK O ALA A 36 NA NA A 301 1555 1555 2.24
LINK O PHE A 39 NA NA A 301 1555 1555 2.31
LINK NA NA A 301 O HOH A 574 1555 1555 2.66
LINK NA NA A 301 O HOH A 605 1555 1555 2.50
LINK NA NA A 301 O HOH A 618 1555 1555 2.76
CISPEP 1 CYS A 259 PRO A 260 0 3.21
CRYST1 69.759 148.498 55.554 90.00 90.00 90.00 C 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006734 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018001 0.00000
TER 2074 TYR A 261
MASTER 427 0 14 12 8 0 0 6 2365 1 81 22
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