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HEADER HYDROLASE 18-OCT-22 8EU1
TITLE ANCESTRAL PETASE 35_442 MUTANT F93L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYETHYLENE TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: ANCESTRAL PETASE 35_442 MUTANT F93L
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 8EU1 0
JRNL AUTH J.SAUNDERS,R.L.FRKIC,C.J.JACKSON
JRNL TITL ANCESTRAL PETASE 35_442 MUTANT F93L
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.23 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) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 14077
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 675
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 63.2700 - 3.8100 1.00 2903 151 0.1421 0.1832
REMARK 3 2 3.8100 - 3.0300 1.00 2794 128 0.1877 0.2791
REMARK 3 3 3.0300 - 2.6400 1.00 2740 140 0.2691 0.3282
REMARK 3 4 2.6400 - 2.4000 0.95 2589 140 0.3755 0.4009
REMARK 3 5 2.4000 - 2.2300 0.87 2376 116 0.5597 0.6017
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) : 0.620
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.29
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 2 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3183 0.1335 6.8277
REMARK 3 T TENSOR
REMARK 3 T11: 0.3042 T22: 0.4614
REMARK 3 T33: 0.2736 T12: -0.0004
REMARK 3 T13: -0.0151 T23: -0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 1.5197 L22: 1.1269
REMARK 3 L33: 1.1299 L12: -0.5943
REMARK 3 L13: 0.0130 L23: -0.3217
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: -0.0365 S13: -0.3816
REMARK 3 S21: -0.3460 S22: -0.0581 S23: 0.0160
REMARK 3 S31: 0.2170 S32: 0.3249 S33: -0.0801
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8416 22.1407 9.3575
REMARK 3 T TENSOR
REMARK 3 T11: 0.2575 T22: 0.3300
REMARK 3 T33: 0.3302 T12: 0.1139
REMARK 3 T13: -0.0539 T23: 0.0850
REMARK 3 L TENSOR
REMARK 3 L11: 1.3319 L22: 1.1587
REMARK 3 L33: 1.1230 L12: 1.0256
REMARK 3 L13: 0.5703 L23: 0.1028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: 0.0906 S13: 0.6281
REMARK 3 S21: -0.2213 S22: -0.0555 S23: 0.1465
REMARK 3 S31: -0.3270 S32: -0.5709 S33: -0.0163
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6110 7.1679 5.7797
REMARK 3 T TENSOR
REMARK 3 T11: 0.2370 T22: 0.2052
REMARK 3 T33: 0.1820 T12: 0.0654
REMARK 3 T13: -0.0256 T23: -0.1131
REMARK 3 L TENSOR
REMARK 3 L11: 0.9251 L22: 2.7512
REMARK 3 L33: 1.2493 L12: 0.3204
REMARK 3 L13: -0.5160 L23: -1.1038
REMARK 3 S TENSOR
REMARK 3 S11: -0.1111 S12: 0.1447 S13: 0.0564
REMARK 3 S21: -0.7121 S22: 0.0864 S23: -0.1836
REMARK 3 S31: 0.2021 S32: -0.2305 S33: 0.0588
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9434 20.7753 11.5228
REMARK 3 T TENSOR
REMARK 3 T11: 0.2761 T22: 0.2679
REMARK 3 T33: 0.2807 T12: 0.0550
REMARK 3 T13: -0.0268 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 0.5981 L22: 0.9556
REMARK 3 L33: 0.5722 L12: 0.3375
REMARK 3 L13: 0.1251 L23: -0.4276
REMARK 3 S TENSOR
REMARK 3 S11: -0.1466 S12: 0.1620 S13: 0.2048
REMARK 3 S21: -0.3112 S22: 0.2453 S23: 0.0920
REMARK 3 S31: -0.0637 S32: 0.2066 S33: 0.0030
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6461 16.6475 19.1610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2645 T22: 0.1529
REMARK 3 T33: 0.3239 T12: 0.0617
REMARK 3 T13: -0.0313 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.6409 L22: 1.3891
REMARK 3 L33: 0.9161 L12: 1.1186
REMARK 3 L13: 0.1949 L23: -0.1962
REMARK 3 S TENSOR
REMARK 3 S11: 0.1591 S12: -0.3551 S13: 0.2111
REMARK 3 S21: 0.3899 S22: -0.0581 S23: 0.2409
REMARK 3 S31: -0.2339 S32: -0.2174 S33: -0.0118
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 248 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1381 13.1083 19.8982
REMARK 3 T TENSOR
REMARK 3 T11: 0.2766 T22: 0.2312
REMARK 3 T33: 0.2380 T12: 0.0014
REMARK 3 T13: -0.0138 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.2640 L22: 0.9876
REMARK 3 L33: 1.2342 L12: -0.0503
REMARK 3 L13: 0.1369 L23: 0.6047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: -0.1356 S13: 0.1167
REMARK 3 S21: 0.1078 S22: 0.1141 S23: 0.0027
REMARK 3 S31: 0.0395 S32: 0.1256 S33: -0.0817
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 249 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9360 -8.1184 19.3798
REMARK 3 T TENSOR
REMARK 3 T11: 0.3064 T22: 0.4559
REMARK 3 T33: 0.2888 T12: 0.1075
REMARK 3 T13: 0.1039 T23: -0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 1.3791 L22: 1.8118
REMARK 3 L33: 1.3682 L12: 0.8257
REMARK 3 L13: 0.6528 L23: 0.7149
REMARK 3 S TENSOR
REMARK 3 S11: 0.1775 S12: -0.1995 S13: 0.2961
REMARK 3 S21: 0.1305 S22: -0.3413 S23: 0.3729
REMARK 3 S31: -0.0671 S32: -0.0201 S33: -0.0634
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 8EU1 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_1000268828.
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) : 0.9536
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 0.7.7
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14586
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 63.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 1.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 6.66300
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 (%): 49.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M BIS TRIS PROPANE PH
REMARK 280 6.5, 0.2M SODIUM POTASSIUM PHOSPHATE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, 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 34.96000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.31200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.31200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.31200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.96000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.31200
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 426 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 464 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 478 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER 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 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
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 461 O HOH A 477 2.11
REMARK 500 O HOH A 469 O HOH A 473 2.13
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 -124.66 63.46
REMARK 500 PRO A 146 -7.88 -58.67
REMARK 500 THR A 155 62.27 27.21
REMARK 500 HIS A 158 144.18 -173.86
REMARK 500 HIS A 186 -85.60 -130.81
REMARK 500 THR A 258 31.19 -93.43
REMARK 500
REMARK 500 REMARK: NULL
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 75.5
REMARK 620 3 PHE A 39 O 105.3 77.4
REMARK 620 4 HOH A 433 O 117.6 160.5 84.9
REMARK 620 5 HOH A 445 O 149.1 77.8 83.5 92.4
REMARK 620 6 HOH A 458 O 81.6 77.3 151.0 117.5 77.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 247 O
REMARK 620 2 ASP A 249 O 87.0
REMARK 620 3 ILE A 252 O 82.7 72.9
REMARK 620 4 HOH A 446 O 100.4 82.1 154.6
REMARK 620 5 HOH A 455 O 162.4 94.1 80.8 97.1
REMARK 620 6 HOH A 461 O 83.4 160.1 88.7 116.7 90.1
REMARK 620 N 1 2 3 4 5
DBREF 8EU1 A -19 261 PDB 8EU1 8EU1 -19 261
SEQRES 1 A 281 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 281 LEU VAL PRO ARG GLY SER HIS MET ALA ALA ASN PRO TYR
SEQRES 3 A 281 GLU ARG GLY PRO ASP PRO THR GLU SER SER LEU GLU ALA
SEQRES 4 A 281 SER SER GLY PRO PHE SER VAL SER GLU THR SER VAL SER
SEQRES 5 A 281 ARG LEU SER ALA SER GLY PHE GLY GLY GLY THR ILE TYR
SEQRES 6 A 281 TYR PRO THR THR THR SER GLU GLY THR TYR GLY ALA VAL
SEQRES 7 A 281 ALA ILE SER PRO GLY TYR THR ALA THR GLN SER SER ILE
SEQRES 8 A 281 ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 9 A 281 VAL ILE THR ILE ASP THR ASN THR THR LEU ASP GLN PRO
SEQRES 10 A 281 ASP SER ARG ALA ARG GLN LEU MET ALA ALA LEU ASN TYR
SEQRES 11 A 281 LEU VAL ASN ARG SER SER VAL ARG SER ARG ILE ASP SER
SEQRES 12 A 281 SER ARG LEU ALA VAL MET GLY HIS SER MET GLY GLY GLY
SEQRES 13 A 281 GLY THR LEU ARG ALA ALA GLU ASP ASN PRO SER LEU LYS
SEQRES 14 A 281 ALA ALA ILE PRO LEU THR PRO TRP HIS THR ASN LYS ASN
SEQRES 15 A 281 TRP SER SER VAL ARG VAL PRO THR LEU ILE ILE GLY ALA
SEQRES 16 A 281 GLU ASN ASP THR ILE ALA PRO VAL SER SER HIS ALA LYS
SEQRES 17 A 281 PRO PHE TYR ASN SER LEU PRO SER SER THR PRO LYS ALA
SEQRES 18 A 281 TYR LEU GLU LEU ASN GLY ALA SER HIS PHE ALA PRO ASN
SEQRES 19 A 281 SER SER ASN THR THR ILE GLY LYS TYR SER ILE ALA TRP
SEQRES 20 A 281 LEU LYS ARG PHE VAL ASP ASN ASP THR ARG TYR SER GLN
SEQRES 21 A 281 PHE LEU CYS PRO ALA PRO HIS ASP ASP SER ALA ILE SER
SEQRES 22 A 281 GLU TYR ARG SER THR CYS PRO TYR
HET NA A 301 1
HET NA A 302 1
HET PEG A 303 7
HET PEG A 304 7
HET PEG A 305 7
HET EDO A 306 4
HET EDO A 307 4
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NA 2(NA 1+)
FORMUL 4 PEG 3(C4 H10 O3)
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 HOH *78(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 PHE A 83 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 ALA A 201 N ILE A 172
SSBOND 1 CYS A 243 CYS A 259 1555 2655 2.05
LINK O ARG A 33 NA NA A 301 1555 1555 2.63
LINK O ALA A 36 NA NA A 301 1555 1555 2.86
LINK O PHE A 39 NA NA A 301 1555 1555 2.41
LINK O HIS A 247 NA NA A 302 1555 1555 2.41
LINK O ASP A 249 NA NA A 302 1555 1555 2.65
LINK O ILE A 252 NA NA A 302 1555 1555 2.68
LINK NA NA A 301 O HOH A 433 1555 1555 2.60
LINK NA NA A 301 O HOH A 445 1555 1555 2.93
LINK NA NA A 301 O HOH A 458 1555 1555 2.28
LINK NA NA A 302 O HOH A 446 1555 1555 2.41
LINK NA NA A 302 O HOH A 455 1555 1555 2.21
LINK NA NA A 302 O HOH A 461 1555 1555 2.61
CISPEP 1 CYS A 259 PRO A 260 0 2.64
CRYST1 69.920 148.624 55.893 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 0.014302 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017891 0.00000
TER 1959 TYR A 261
MASTER 412 0 7 12 8 0 0 6 2067 1 45 22
END |