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HEADER HYDROLASE 18-OCT-22 8ETX
TITLE ANCESTRAL PETASE 55_547
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYETHYLENE TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: ANCESTRAL PETASE 55_547
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 8ETX 0
JRNL AUTH J.SAUNDERS,R.L.FRKIC,C.J.JACKSON
JRNL TITL ANCESTRAL PETASE 55_547
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30209
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1547
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 41.9000 - 3.8900 1.00 2774 133 0.1441 0.1645
REMARK 3 2 3.8900 - 3.0900 1.00 2646 140 0.1439 0.1669
REMARK 3 3 3.0900 - 2.7000 1.00 2624 130 0.1620 0.2131
REMARK 3 4 2.7000 - 2.4500 1.00 2604 150 0.1640 0.1981
REMARK 3 5 2.4500 - 2.2800 1.00 2580 149 0.1579 0.1926
REMARK 3 6 2.2800 - 2.1400 1.00 2584 141 0.1707 0.2053
REMARK 3 7 2.1400 - 2.0300 1.00 2560 153 0.1841 0.2058
REMARK 3 8 2.0300 - 1.9500 1.00 2584 149 0.1968 0.1946
REMARK 3 9 1.9500 - 1.8700 1.00 2591 122 0.2293 0.2433
REMARK 3 10 1.8700 - 1.8100 1.00 2536 146 0.2659 0.3196
REMARK 3 11 1.8100 - 1.7500 1.00 2579 134 0.2937 0.3185
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.50
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): 16.9619 -0.5564 7.0384
REMARK 3 T TENSOR
REMARK 3 T11: 0.2098 T22: 0.1914
REMARK 3 T33: 0.1119 T12: 0.0197
REMARK 3 T13: -0.0108 T23: -0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 5.4910 L22: 3.3549
REMARK 3 L33: 6.1373 L12: 1.2453
REMARK 3 L13: -2.4936 L23: -2.9805
REMARK 3 S TENSOR
REMARK 3 S11: -0.0284 S12: 0.1163 S13: -0.3502
REMARK 3 S21: -0.1284 S22: -0.0302 S23: -0.1224
REMARK 3 S31: 0.1900 S32: 0.2269 S33: 0.0522
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1148 18.0937 9.8103
REMARK 3 T TENSOR
REMARK 3 T11: 0.1972 T22: 0.1945
REMARK 3 T33: 0.2171 T12: 0.0143
REMARK 3 T13: -0.0314 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 0.9990 L22: 3.8666
REMARK 3 L33: 1.7073 L12: 0.7307
REMARK 3 L13: 0.1633 L23: 1.4040
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: 0.0655 S13: 0.2932
REMARK 3 S21: -0.0455 S22: -0.0487 S23: 0.2743
REMARK 3 S31: -0.1507 S32: -0.0814 S33: 0.1086
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5799 15.0117 17.2799
REMARK 3 T TENSOR
REMARK 3 T11: 0.1634 T22: 0.1853
REMARK 3 T33: 0.2309 T12: 0.0046
REMARK 3 T13: 0.0193 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 4.4389 L22: 7.0099
REMARK 3 L33: 1.9772 L12: 3.2914
REMARK 3 L13: 2.1945 L23: 2.1950
REMARK 3 S TENSOR
REMARK 3 S11: -0.1518 S12: -0.2118 S13: 0.5188
REMARK 3 S21: 0.0347 S22: -0.0968 S23: 0.6431
REMARK 3 S31: -0.1981 S32: -0.0566 S33: 0.2870
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4252 18.8748 23.5333
REMARK 3 T TENSOR
REMARK 3 T11: 0.2450 T22: 0.1632
REMARK 3 T33: 0.1752 T12: 0.0037
REMARK 3 T13: -0.0089 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 3.8372 L22: 3.5036
REMARK 3 L33: 1.3240 L12: 1.9834
REMARK 3 L13: 0.2714 L23: 0.2007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0821 S12: -0.1844 S13: 0.2450
REMARK 3 S21: 0.2821 S22: -0.1438 S23: 0.0833
REMARK 3 S31: -0.1723 S32: -0.0210 S33: 0.0515
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3921 13.5461 25.9018
REMARK 3 T TENSOR
REMARK 3 T11: 0.1607 T22: 0.1932
REMARK 3 T33: 0.1665 T12: -0.0145
REMARK 3 T13: -0.0235 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.8033 L22: 5.4578
REMARK 3 L33: 5.1380 L12: 0.0294
REMARK 3 L13: 0.0992 L23: 0.3002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: -0.2894 S13: 0.1083
REMARK 3 S21: 0.3383 S22: -0.1311 S23: -0.1642
REMARK 3 S31: -0.1749 S32: 0.2812 S33: 0.1494
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 206 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9233 13.2035 12.2673
REMARK 3 T TENSOR
REMARK 3 T11: 0.1806 T22: 0.2074
REMARK 3 T33: 0.1541 T12: 0.0024
REMARK 3 T13: -0.0100 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 2.7134 L22: 5.6303
REMARK 3 L33: 1.6532 L12: 2.2119
REMARK 3 L13: -0.4634 L23: -0.7417
REMARK 3 S TENSOR
REMARK 3 S11: -0.0360 S12: 0.1492 S13: 0.2058
REMARK 3 S21: -0.2260 S22: -0.0507 S23: -0.0313
REMARK 3 S31: -0.1079 S32: 0.1183 S33: 0.1023
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1614 -5.3618 17.4350
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.2588
REMARK 3 T33: 0.1933 T12: -0.0151
REMARK 3 T13: 0.0100 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 4.3649 L22: 0.2367
REMARK 3 L33: 0.8421 L12: -0.8932
REMARK 3 L13: 1.9014 L23: -0.3334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: 0.0831 S13: -0.1722
REMARK 3 S21: -0.0311 S22: 0.0632 S23: -0.0263
REMARK 3 S31: -0.0155 S32: 0.0756 S33: -0.0584
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 8ETX 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_1000269126.
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30223
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 41.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : 2.42200
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 (%): 49.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M BIS TRIS PROPANE PH
REMARK 280 7.5, 0.2M POTASSIUM SODIUM TARTRATE, 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 35.08300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.28700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.08300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.28700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.08300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.28700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.08300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.28700
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 NA NA A 306 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL A 308 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 566 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 572 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 581 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 634 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 O HOH A 600 O HOH A 646 2.07
REMARK 500 O HOH A 519 O HOH A 670 2.16
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 444 O HOH A 444 2555 2.02
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 -122.80 63.81
REMARK 500 THR A 155 60.64 33.93
REMARK 500 HIS A 186 -83.82 -128.55
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 84.6
REMARK 620 3 PHE A 39 O 102.8 78.7
REMARK 620 4 HOH A 564 O 113.0 150.0 73.9
REMARK 620 5 HOH A 579 O 175.9 98.9 79.9 64.7
REMARK 620 6 HOH A 624 O 88.4 104.3 168.6 100.4 88.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 306 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 258 O
REMARK 620 2 THR A 258 O 0.0
REMARK 620 3 PRO A 260 O 96.5 96.5
REMARK 620 4 PRO A 260 O 96.5 96.5 0.0
REMARK 620 5 HOH A 634 O 109.7 109.7 82.3 82.3
REMARK 620 6 HOH A 634 O 109.7 109.7 82.2 82.2 0.0
REMARK 620 N 1 2 3 4 5
DBREF 8ETX A -19 261 PDB 8ETX 8ETX -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 ALA 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 SER 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 VAL SER 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 PG4 A 302 31
HET EDO A 303 10
HET SO4 A 304 5
HET EDO A 305 10
HET NA A 306 1
HET SO4 A 307 5
HET CL A 308 1
HETNAM NA SODIUM ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NA 2(NA 1+)
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 9 CL CL 1-
FORMUL 10 HOH *278(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 LEU A 205 N GLY A 174
SSBOND 1 CYS A 243 CYS A 259 1555 2655 2.07
LINK O ARG A 33 NA NA A 301 1555 1555 2.49
LINK O ALA A 36 NA NA A 301 1555 1555 2.44
LINK O PHE A 39 NA NA A 301 1555 1555 2.59
LINK O THR A 258 NA NA A 306 1555 1555 2.61
LINK O THR A 258 NA NA A 306 1555 4556 2.61
LINK O PRO A 260 NA NA A 306 1555 1555 2.70
LINK O PRO A 260 NA NA A 306 1555 4556 2.70
LINK NA NA A 301 O HOH A 564 1555 1555 2.80
LINK NA NA A 301 O HOH A 579 1555 1555 2.57
LINK NA NA A 301 O HOH A 624 1555 1555 2.46
LINK NA NA A 306 O HOH A 634 1555 1555 2.82
LINK NA NA A 306 O HOH A 634 1555 4556 2.82
CISPEP 1 CYS A 259 PRO A 260 0 1.61
CRYST1 70.166 150.574 55.691 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 0.014252 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006641 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017956 0.00000
TER 3928 TYR A 261
MASTER 435 0 8 12 8 0 0 6 2277 1 73 22
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