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HEADER HYDROLASE 21-SEP-22 8B4U
TITLE THE CRYSTAL STRUCTURE OF PET46, A PETASE ENZYME FROM CANDIDATUS
TITLE 2 BATHYARCHAEOTA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDATUS BATHYARCHAEOTA ARCHAEON;
SOURCE 3 ORGANISM_TAXID: 2026714;
SOURCE 4 GENE: DRO64_06360;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, PET, ENZYME, HYDROLASE, ESTERASE, PLASTIC, DEGRADATION,
KEYWDS 2 BIOTECH, ENZYME EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.COSTANZI,V.APPLEGATE,J.SCHUMACHER,S.H.J.SMITS
REVDAT 1 23-AUG-23 8B4U 0
JRNL AUTH E.COSTANZI,V.APPLEGATE,J.SCHUMACHER,S.H.J.SMITS
JRNL TITL THE CRYSTAL STRUCTURE OF PET46, A PETASE ENZYME FROM
JRNL TITL 2 CANDIDATUS BATHYARCHAEOTA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 34953
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1725
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 36.3800 - 3.9100 0.96 2957 137 0.1648 0.1817
REMARK 3 2 3.9100 - 3.1100 0.98 2800 164 0.1318 0.1465
REMARK 3 3 3.1100 - 2.7100 0.99 2747 170 0.1343 0.1661
REMARK 3 4 2.7100 - 2.4700 0.99 2751 154 0.1407 0.1644
REMARK 3 5 2.4700 - 2.2900 0.99 2772 139 0.1310 0.1381
REMARK 3 6 2.2900 - 2.1500 0.99 2765 135 0.1388 0.1537
REMARK 3 7 2.1500 - 2.0500 0.99 2752 132 0.1477 0.1958
REMARK 3 8 2.0500 - 1.9600 1.00 2744 141 0.1793 0.2013
REMARK 3 9 1.9600 - 1.8800 1.00 2721 139 0.1736 0.2052
REMARK 3 10 1.8800 - 1.8200 1.00 2744 138 0.1940 0.2636
REMARK 3 11 1.8200 - 1.7600 1.00 2723 133 0.2282 0.2314
REMARK 3 12 1.7600 - 1.7100 1.00 2752 143 0.2863 0.3276
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.187
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.79
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 : 0.011 2308
REMARK 3 ANGLE : 1.013 3087
REMARK 3 CHIRALITY : 0.067 338
REMARK 3 PLANARITY : 0.011 398
REMARK 3 DIHEDRAL : 13.347 860
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 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5255 72.5985 5.8966
REMARK 3 T TENSOR
REMARK 3 T11: 0.1929 T22: 0.2244
REMARK 3 T33: 0.1961 T12: 0.0105
REMARK 3 T13: -0.0054 T23: 0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 2.6161 L22: 2.0313
REMARK 3 L33: 4.4140 L12: -1.4417
REMARK 3 L13: -0.0438 L23: 0.1637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: 0.0681 S13: 0.0818
REMARK 3 S21: -0.0666 S22: -0.0499 S23: 0.0927
REMARK 3 S31: -0.0426 S32: -0.3322 S33: -0.0324
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8667 68.8280 10.7573
REMARK 3 T TENSOR
REMARK 3 T11: 0.2286 T22: 0.1837
REMARK 3 T33: 0.1924 T12: 0.0038
REMARK 3 T13: -0.0159 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.3092 L22: 2.2080
REMARK 3 L33: 2.4465 L12: 0.1667
REMARK 3 L13: -0.2935 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.0144 S13: -0.0399
REMARK 3 S21: 0.0496 S22: 0.0346 S23: 0.1689
REMARK 3 S31: 0.0834 S32: -0.1319 S33: -0.0600
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4286 71.0258 20.8667
REMARK 3 T TENSOR
REMARK 3 T11: 0.3025 T22: 0.1909
REMARK 3 T33: 0.2360 T12: 0.0273
REMARK 3 T13: 0.0290 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 4.9685 L22: 2.1150
REMARK 3 L33: 1.9191 L12: 1.3879
REMARK 3 L13: 0.6977 L23: 0.5567
REMARK 3 S TENSOR
REMARK 3 S11: 0.0391 S12: -0.3578 S13: 0.0431
REMARK 3 S21: 0.2973 S22: -0.0512 S23: 0.2259
REMARK 3 S31: 0.0251 S32: -0.2078 S33: 0.0131
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5089 81.9386 12.6615
REMARK 3 T TENSOR
REMARK 3 T11: 0.2679 T22: 0.2525
REMARK 3 T33: 0.2477 T12: -0.0109
REMARK 3 T13: -0.0245 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 2.7409 L22: 7.9502
REMARK 3 L33: 3.6439 L12: 3.7780
REMARK 3 L13: -1.8853 L23: -4.5518
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: -0.0868 S13: -0.1118
REMARK 3 S21: 0.0161 S22: -0.3135 S23: -0.6110
REMARK 3 S31: -0.1423 S32: 0.4853 S33: 0.3706
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 162 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6179 80.5208 14.9893
REMARK 3 T TENSOR
REMARK 3 T11: 0.2721 T22: 0.2202
REMARK 3 T33: 0.2738 T12: 0.0116
REMARK 3 T13: -0.0282 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.4119 L22: 1.8262
REMARK 3 L33: 2.3424 L12: 0.6800
REMARK 3 L13: -0.3772 L23: -1.4250
REMARK 3 S TENSOR
REMARK 3 S11: 0.0362 S12: -0.0027 S13: 0.0832
REMARK 3 S21: 0.2213 S22: 0.0247 S23: -0.0038
REMARK 3 S31: -0.2588 S32: 0.1377 S33: -0.0949
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6479 64.7044 22.6877
REMARK 3 T TENSOR
REMARK 3 T11: 0.2623 T22: 0.2117
REMARK 3 T33: 0.2679 T12: 0.0611
REMARK 3 T13: -0.0701 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 3.0023 L22: 1.9092
REMARK 3 L33: 6.8210 L12: -0.1283
REMARK 3 L13: -1.9558 L23: 0.3516
REMARK 3 S TENSOR
REMARK 3 S11: -0.0307 S12: -0.0821 S13: -0.0948
REMARK 3 S21: 0.3279 S22: 0.0885 S23: -0.1995
REMARK 3 S31: 0.1702 S32: 0.3831 S33: -0.0280
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7469 54.3407 20.7097
REMARK 3 T TENSOR
REMARK 3 T11: 0.4989 T22: 0.2544
REMARK 3 T33: 0.3844 T12: -0.0298
REMARK 3 T13: 0.0070 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 3.2256 L22: 2.6377
REMARK 3 L33: 4.7998 L12: -0.6446
REMARK 3 L13: -0.6602 L23: 0.6397
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: -0.0683 S13: -0.5531
REMARK 3 S21: 0.4749 S22: 0.0204 S23: 0.4015
REMARK 3 S31: 0.8480 S32: -0.4746 S33: 0.2084
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 8B4U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1292125752.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-21
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34960
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 68.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: ALPHAFOLD MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 325 MM (NH4)H2PO4, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 285K
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 57.18200
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 114.36400
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 85.77300
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 142.95500
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 28.59100
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 57.18200
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 114.36400
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 142.95500
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 85.77300
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 28.59100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 KCAL/MOL
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 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 LEU A 270
REMARK 465 GLU A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 HIS A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
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 GLU A 45 178.83 59.93
REMARK 500 SER A 115 -111.35 55.85
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8B4U A 1 262 UNP A0A497NK85_9ARCH
DBREF2 8B4U A A0A497NK85 1 262
SEQADV 8B4U VAL A 263 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U ASP A 264 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U LYS A 265 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U LEU A 266 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U ALA A 267 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U ALA A 268 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U ALA A 269 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U LEU A 270 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U GLU A 271 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U HIS A 272 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U HIS A 273 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U HIS A 274 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U HIS A 275 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U HIS A 276 UNP A0A497NK8 EXPRESSION TAG
SEQADV 8B4U HIS A 277 UNP A0A497NK8 EXPRESSION TAG
SEQRES 1 A 277 MET ILE LYS PRO VAL THR PHE MET SER GLU GLY GLU GLN
SEQRES 2 A 277 ILE ILE GLY VAL LEU HIS VAL PRO ASP ASP LEU ARG GLY
SEQRES 3 A 277 ASP LYS ARG ALA PRO ALA ILE ALA MET PHE HIS GLY PHE
SEQRES 4 A 277 THR GLY ASN LYS SER GLU ALA HIS ARG LEU PHE VAL HIS
SEQRES 5 A 277 VAL ALA ARG SER LEU CYS ASN ASP GLY PHE VAL VAL LEU
SEQRES 6 A 277 ARG PHE ASP PHE ARG GLY SER GLY ASP SER ASP GLY GLU
SEQRES 7 A 277 PHE GLU ASP MET THR VAL PRO GLY GLU VAL CYS ASP ALA
SEQRES 8 A 277 SER ARG SER ILE ASP PHE LEU SER GLU LEU ASN PHE VAL
SEQRES 9 A 277 ASP SER GLU ARG ILE GLY VAL LEU GLY LEU SER MET GLY
SEQRES 10 A 277 GLY ARG VAL ALA ALA ILE LEU ALA SER LYS ASP ARG ARG
SEQRES 11 A 277 ILE LYS PHE VAL ILE LEU TYR SER ALA ALA LEU THR PRO
SEQRES 12 A 277 LEU ARG ARG LYS PHE LEU GLU GLY LEU GLU LYS GLU SER
SEQRES 13 A 277 ILE ARG ARG LEU GLU MET GLY GLU ALA VAL HIS VAL GLY
SEQRES 14 A 277 ASN GLY TRP TYR LEU LYS LYS GLY PHE PHE GLU THR VAL
SEQRES 15 A 277 ASP SER ILE VAL PRO LEU ASP VAL LEU ASP ARG ILE ARG
SEQRES 16 A 277 VAL PRO VAL LEU ILE ILE HIS GLY ASP SER ASP SER VAL
SEQRES 17 A 277 ILE PRO LEU ASP GLY ALA LEU LYS GLY TYR GLU ILE ILE
SEQRES 18 A 277 ARG ASP LEU ASN ASP LYS ASN GLU LEU TYR ILE VAL ARG
SEQRES 19 A 277 GLY GLY ASP HIS VAL PHE THR ARG ARG GLU HIS THR ILE
SEQRES 20 A 277 GLU VAL ILE GLU ARG THR LEU ASP TRP LEU ARG SER LEU
SEQRES 21 A 277 ASN LEU VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS
SEQRES 22 A 277 HIS HIS HIS HIS
HET EDO A 301 10
HET EDO A 302 10
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 EDO A 309 10
HET EDO A 310 10
HET EDO A 311 10
HET EDO A 312 10
HET EDO A 313 10
HET EDO A 314 10
HET EDO A 315 10
HET EDO A 316 10
HET EDO A 317 10
HET EDO A 318 10
HET EDO A 319 10
HET EDO A 320 10
HET PO4 A 321 5
HET PO4 A 322 5
HET PO4 A 323 5
HET PO4 A 324 5
HET CL A 325 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 20(C2 H6 O2)
FORMUL 22 PO4 4(O4 P 3-)
FORMUL 26 CL CL 1-
FORMUL 27 HOH *194(H2 O)
HELIX 1 AA1 GLU A 45 HIS A 47 5 3
HELIX 2 AA2 ARG A 48 ASP A 60 1 13
HELIX 3 AA3 GLU A 78 MET A 82 5 5
HELIX 4 AA4 THR A 83 GLU A 100 1 18
HELIX 5 AA5 SER A 115 ASP A 128 1 14
HELIX 6 AA6 LEU A 144 GLY A 151 1 8
HELIX 7 AA7 GLU A 153 MET A 162 1 10
HELIX 8 AA8 LYS A 175 VAL A 182 1 8
HELIX 9 AA9 VAL A 186 LEU A 191 1 6
HELIX 10 AB1 ASP A 192 ILE A 194 5 3
HELIX 11 AB2 PRO A 210 ARG A 222 1 13
HELIX 12 AB3 ARG A 242 LEU A 260 1 19
HELIX 13 AB4 ASP A 264 ALA A 269 1 6
SHEET 1 AA1 8 ILE A 2 SER A 9 0
SHEET 2 AA1 8 GLU A 12 HIS A 19 -1 O ILE A 14 N PHE A 7
SHEET 3 AA1 8 VAL A 63 PHE A 67 -1 O ARG A 66 N VAL A 17
SHEET 4 AA1 8 ALA A 30 PHE A 36 1 N ILE A 33 O LEU A 65
SHEET 5 AA1 8 VAL A 104 LEU A 114 1 O ASP A 105 N ALA A 30
SHEET 6 AA1 8 ILE A 131 TYR A 137 1 O LYS A 132 N ILE A 109
SHEET 7 AA1 8 VAL A 198 GLY A 203 1 O ILE A 201 N LEU A 136
SHEET 8 AA1 8 GLU A 229 VAL A 233 1 O GLU A 229 N ILE A 200
SHEET 1 AA2 2 VAL A 166 GLY A 169 0
SHEET 2 AA2 2 TRP A 172 LEU A 174 -1 O TRP A 172 N VAL A 168
SSBOND 1 CYS A 89 CYS A 89 1555 12575 2.13
CRYST1 79.292 79.292 171.546 90.00 90.00 120.00 P 61 2 2 12
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 0.012612 0.007281 0.000000 0.00000
SCALE2 0.000000 0.014563 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005829 0.00000
TER 4357 ALA A 269
MASTER 373 0 25 13 10 0 0 6 2414 1 220 22
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