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HEADER HYDROLASE 18-OCT-22 8ETZ
TITLE ANCESTRAL PETASE 35_442 MUTANT E13D
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 E13D
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 8ETZ 0
JRNL AUTH J.SAUNDERS,R.L.FRKIC,C.J.JACKSON
JRNL TITL ANCESTRAL PETASE 35_442 MUTANT E13D
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.68 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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 33465
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1659
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 41.7100 - 3.8500 1.00 2799 169 0.1477 0.1466
REMARK 3 2 3.8400 - 3.0500 1.00 2707 125 0.1342 0.1414
REMARK 3 3 3.0500 - 2.6700 1.00 2687 119 0.1423 0.1844
REMARK 3 4 2.6700 - 2.4200 1.00 2654 141 0.1401 0.1681
REMARK 3 5 2.4200 - 2.2500 1.00 2677 123 0.1372 0.1723
REMARK 3 6 2.2500 - 2.1200 1.00 2594 148 0.1408 0.1767
REMARK 3 7 2.1200 - 2.0100 1.00 2677 126 0.1544 0.1575
REMARK 3 8 2.0100 - 1.9200 1.00 2589 145 0.1684 0.2176
REMARK 3 9 1.9200 - 1.8500 1.00 2616 142 0.1946 0.2251
REMARK 3 10 1.8500 - 1.7900 1.00 2610 142 0.2364 0.2920
REMARK 3 11 1.7900 - 1.7300 1.00 2605 145 0.2680 0.2912
REMARK 3 12 1.7300 - 1.6800 1.00 2591 134 0.3020 0.3099
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.39
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 : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8039 -0.5102 7.0563
REMARK 3 T TENSOR
REMARK 3 T11: 0.1910 T22: 0.1786
REMARK 3 T33: 0.1358 T12: 0.0106
REMARK 3 T13: -0.0392 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 4.6794 L22: 1.9340
REMARK 3 L33: 4.8225 L12: 0.5558
REMARK 3 L13: -2.2142 L23: -1.7675
REMARK 3 S TENSOR
REMARK 3 S11: -0.0272 S12: 0.1516 S13: -0.1542
REMARK 3 S21: -0.1955 S22: -0.0778 S23: 0.0386
REMARK 3 S31: -0.0130 S32: 0.0867 S33: 0.1137
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8673 17.9212 9.9216
REMARK 3 T TENSOR
REMARK 3 T11: 0.2016 T22: 0.2223
REMARK 3 T33: 0.2473 T12: 0.0088
REMARK 3 T13: -0.0439 T23: 0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.9607 L22: 3.1264
REMARK 3 L33: 2.0067 L12: 0.3544
REMARK 3 L13: 0.0065 L23: 0.8970
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: 0.0830 S13: 0.1979
REMARK 3 S21: -0.1343 S22: -0.0056 S23: 0.2521
REMARK 3 S31: -0.1018 S32: -0.1057 S33: 0.0789
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2760 14.5726 16.9758
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.1958
REMARK 3 T33: 0.2342 T12: 0.0048
REMARK 3 T13: 0.0023 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 3.8474 L22: 5.2499
REMARK 3 L33: 1.7399 L12: 1.8943
REMARK 3 L13: 1.6284 L23: 1.7762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0884 S12: -0.1088 S13: 0.3294
REMARK 3 S21: -0.0487 S22: -0.0707 S23: 0.5825
REMARK 3 S31: -0.1452 S32: -0.1101 S33: 0.1830
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3488 16.3847 21.3317
REMARK 3 T TENSOR
REMARK 3 T11: 0.1732 T22: 0.1742
REMARK 3 T33: 0.1644 T12: -0.0063
REMARK 3 T13: -0.0165 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.6178 L22: 2.2906
REMARK 3 L33: 1.2150 L12: 0.2136
REMARK 3 L13: 0.1532 L23: -0.3454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.0764 S13: 0.1992
REMARK 3 S21: 0.1186 S22: -0.0541 S23: -0.0322
REMARK 3 S31: -0.1667 S32: 0.0696 S33: 0.0676
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5126 -4.7309 17.0454
REMARK 3 T TENSOR
REMARK 3 T11: 0.2081 T22: 0.2575
REMARK 3 T33: 0.1917 T12: -0.0089
REMARK 3 T13: 0.0037 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 3.3429 L22: 0.1413
REMARK 3 L33: 0.2932 L12: -0.5500
REMARK 3 L13: 0.9825 L23: -0.1771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.1102 S13: -0.1407
REMARK 3 S21: -0.0096 S22: 0.0310 S23: 0.0282
REMARK 3 S31: -0.0405 S32: 0.0553 S33: -0.0359
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 8ETZ 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_1000269073.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-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 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33515
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 41.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.17800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : 4.61200
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 (%): 48.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M SODIUM CITRATE,
REMARK 280 VAPOR DIFFUSION, SITTING 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 34.76650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.74400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.76650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.74400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.76650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.74400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.76650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.74400
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 C1 EDO A 304 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 536 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 612 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 620 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 648 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 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 HH TYR A 255 O HOH A 404 1.58
REMARK 500 O HOH A 514 O HOH A 627 1.96
REMARK 500 O HOH A 615 O HOH A 646 2.05
REMARK 500 O HOH A 402 O HOH A 616 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 609 O HOH A 609 3656 2.00
REMARK 500 O HOH A 587 O HOH A 587 3555 2.07
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 65 -0.33 71.94
REMARK 500 SER A 132 -122.22 66.16
REMARK 500 THR A 155 62.02 33.03
REMARK 500 HIS A 186 -84.45 -124.03
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 311 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 247 O
REMARK 620 2 ASP A 249 O 90.3
REMARK 620 3 ILE A 252 O 95.8 84.6
REMARK 620 4 HOH A 573 O 170.7 99.0 85.4
REMARK 620 5 HOH A 606 O 86.2 174.1 100.5 84.5
REMARK 620 6 HOH A 610 O 86.3 90.7 174.8 93.2 84.4
REMARK 620 N 1 2 3 4 5
DBREF 8ETZ A -19 261 PDB 8ETZ 8ETZ -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 ASP 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 PHE 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 PEG A 301 17
HET P6G A 302 45
HET EDO A 303 10
HET EDO A 304 10
HET EDO A 305 10
HET EDO A 306 10
HET EDO A 307 10
HET EDO A 308 10
HET GOL A 309 14
HET EDO A 310 10
HET NA A 311 1
HET PEG A 312 17
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN P6G POLYETHYLENE GLYCOL PEG400
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 PEG 2(C4 H10 O3)
FORMUL 3 P6G C12 H26 O7
FORMUL 4 EDO 7(C2 H6 O2)
FORMUL 10 GOL C3 H8 O3
FORMUL 12 NA NA 1+
FORMUL 14 HOH *258(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 2.02
LINK O HIS A 247 NA NA A 311 1555 1555 2.33
LINK O ASP A 249 NA NA A 311 1555 1555 2.43
LINK O ILE A 252 NA NA A 311 1555 1555 2.31
LINK NA NA A 311 O HOH A 573 1555 1555 2.42
LINK NA NA A 311 O HOH A 606 1555 1555 2.38
LINK NA NA A 311 O HOH A 610 1555 1555 2.40
CISPEP 1 CYS A 259 PRO A 260 0 2.64
CRYST1 69.533 149.488 55.634 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 0.014382 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006690 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017975 0.00000
TER 3919 TYR A 261
MASTER 397 0 12 12 8 0 0 6 2294 1 171 22
END |