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HEADER HYDROLASE 18-OCT-22 8EU0
TITLE ANCESTRAL PETASE 35_442 MUTANT E27Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYETHYLENE TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: ANCESTRAL PETASE 35_442 MUTANT E27Q
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 8EU0 0
JRNL AUTH J.SAUNDERS,R.L.FRKIC,C.J.JACKSON
JRNL TITL ANCESTRAL PETASE 35_442 MUTANT E27Q
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.06 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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36856
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1912
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 57.0700 - 4.9600 1.00 2729 132 0.1476 0.1980
REMARK 3 2 4.9600 - 3.9400 1.00 2558 142 0.1388 0.1597
REMARK 3 3 3.9400 - 3.4400 1.00 2508 160 0.1518 0.2000
REMARK 3 4 3.4400 - 3.1300 1.00 2509 134 0.1955 0.1822
REMARK 3 5 3.1300 - 2.9000 1.00 2505 140 0.2113 0.2722
REMARK 3 6 2.9000 - 2.7300 1.00 2442 157 0.2332 0.2836
REMARK 3 7 2.7300 - 2.6000 1.00 2492 131 0.2303 0.2747
REMARK 3 8 2.6000 - 2.4800 1.00 2494 130 0.2474 0.2956
REMARK 3 9 2.4800 - 2.3900 1.00 2465 116 0.2524 0.3323
REMARK 3 10 2.3900 - 2.3000 1.00 2483 120 0.2670 0.2921
REMARK 3 11 2.3000 - 2.2300 1.00 2447 148 0.2812 0.2901
REMARK 3 12 2.2300 - 2.1700 1.00 2475 121 0.2946 0.3387
REMARK 3 13 2.1700 - 2.1100 1.00 2432 131 0.2978 0.3453
REMARK 3 14 2.1100 - 2.0600 1.00 2405 150 0.3138 0.3971
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.81
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 : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8449 -27.5862 -16.7150
REMARK 3 T TENSOR
REMARK 3 T11: 0.5923 T22: 0.4366
REMARK 3 T33: 0.3666 T12: 0.0044
REMARK 3 T13: -0.0837 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 8.4181 L22: 4.6022
REMARK 3 L33: 5.9117 L12: 3.0538
REMARK 3 L13: -6.0837 L23: -2.3110
REMARK 3 S TENSOR
REMARK 3 S11: -0.4088 S12: -0.5785 S13: -0.1613
REMARK 3 S21: -0.7316 S22: 0.0404 S23: -0.0609
REMARK 3 S31: 0.8048 S32: 0.2354 S33: 0.3551
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0147 -7.7220 -23.3171
REMARK 3 T TENSOR
REMARK 3 T11: 0.4618 T22: 0.4561
REMARK 3 T33: 0.3889 T12: 0.0641
REMARK 3 T13: -0.1026 T23: 0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 3.6463 L22: 5.9580
REMARK 3 L33: 5.4665 L12: 1.0207
REMARK 3 L13: -0.0767 L23: -1.4629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: 0.4302 S13: -0.1480
REMARK 3 S21: -0.9566 S22: 0.1833 S23: 0.1992
REMARK 3 S31: 0.0459 S32: -0.0485 S33: -0.1244
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1604 -9.4978 -6.4809
REMARK 3 T TENSOR
REMARK 3 T11: 0.3172 T22: 0.2975
REMARK 3 T33: 0.3691 T12: 0.0057
REMARK 3 T13: -0.0051 T23: 0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 1.4257 L22: 2.1307
REMARK 3 L33: 2.7428 L12: 0.3759
REMARK 3 L13: 0.2685 L23: 0.1488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0685 S12: 0.0433 S13: 0.0908
REMARK 3 S21: -0.0627 S22: 0.0032 S23: 0.0803
REMARK 3 S31: -0.1123 S32: -0.0751 S33: -0.0684
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1145 -26.4295 -1.9041
REMARK 3 T TENSOR
REMARK 3 T11: 0.4008 T22: 0.2818
REMARK 3 T33: 0.4330 T12: -0.0309
REMARK 3 T13: 0.0036 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 6.3331 L22: 3.8746
REMARK 3 L33: 8.2144 L12: 2.0246
REMARK 3 L13: 4.3009 L23: -0.9694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0391 S12: -0.0814 S13: -0.3454
REMARK 3 S21: 0.0678 S22: 0.2414 S23: -0.0965
REMARK 3 S31: 0.0371 S32: -0.1709 S33: -0.2695
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7152 -0.8975 -20.6404
REMARK 3 T TENSOR
REMARK 3 T11: 0.3165 T22: 0.3827
REMARK 3 T33: 0.3416 T12: 0.0162
REMARK 3 T13: -0.0529 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 2.2755 L22: 6.3461
REMARK 3 L33: 3.1334 L12: -0.7291
REMARK 3 L13: 0.0704 L23: 0.7448
REMARK 3 S TENSOR
REMARK 3 S11: 0.1162 S12: 0.0567 S13: -0.0247
REMARK 3 S21: 0.4152 S22: -0.1176 S23: -0.4812
REMARK 3 S31: 0.3479 S32: 0.2440 S33: 0.0068
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 56 THROUGH 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6642 7.7719 -29.9586
REMARK 3 T TENSOR
REMARK 3 T11: 0.4144 T22: 0.2967
REMARK 3 T33: 0.3534 T12: 0.0038
REMARK 3 T13: 0.0608 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 3.4799 L22: 2.5509
REMARK 3 L33: 2.3650 L12: -0.4716
REMARK 3 L13: 0.8237 L23: -0.1034
REMARK 3 S TENSOR
REMARK 3 S11: 0.1634 S12: 0.0734 S13: 0.3585
REMARK 3 S21: -0.1729 S22: -0.0350 S23: -0.2453
REMARK 3 S31: -0.2170 S32: 0.1207 S33: -0.1205
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 155 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6934 -3.4030 -35.7290
REMARK 3 T TENSOR
REMARK 3 T11: 0.5169 T22: 0.3431
REMARK 3 T33: 0.3562 T12: 0.0583
REMARK 3 T13: -0.0044 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.8071 L22: 1.0440
REMARK 3 L33: 1.4563 L12: -0.0576
REMARK 3 L13: 0.1570 L23: 0.2327
REMARK 3 S TENSOR
REMARK 3 S11: 0.1926 S12: 0.1528 S13: 0.0255
REMARK 3 S21: -0.1216 S22: -0.0349 S23: -0.0143
REMARK 3 S31: 0.0195 S32: 0.0449 S33: -0.1576
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 242 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2006 -14.4903 -34.9733
REMARK 3 T TENSOR
REMARK 3 T11: 0.6517 T22: 0.3234
REMARK 3 T33: 0.3689 T12: 0.0619
REMARK 3 T13: 0.0060 T23: 0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 7.6512 L22: 2.0293
REMARK 3 L33: 4.3916 L12: 0.9730
REMARK 3 L13: -2.3047 L23: 0.6174
REMARK 3 S TENSOR
REMARK 3 S11: -0.2128 S12: -0.0758 S13: -0.0360
REMARK 3 S21: 0.0673 S22: -0.0609 S23: -0.2032
REMARK 3 S31: 0.2320 S32: -0.1319 S33: 0.3063
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 8EU0 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_1000269155.
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) : 0.9536
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 : 36969
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 59.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.90
REMARK 200 R MERGE (I) : 0.22300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.70
REMARK 200 R MERGE FOR SHELL (I) : 3.43400
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 (%): 48.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M SODIUM FLUORIDE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 142.67600
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 71.33800
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 71.33800
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 142.67600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 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 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -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 OE2 GLU B 254 NH2 ARG B 256 2.18
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 PRO A 62 -169.39 -79.09
REMARK 500 SER A 132 -117.12 60.90
REMARK 500 HIS A 186 -82.17 -128.07
REMARK 500 THR B 67 -166.21 -119.10
REMARK 500 SER B 132 -116.67 60.03
REMARK 500 ASN B 177 33.88 -98.74
REMARK 500 HIS B 186 -80.84 -125.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CYS A 243 -11.71
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 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 33 O
REMARK 620 2 ALA A 36 O 90.4
REMARK 620 3 PHE A 39 O 104.8 80.0
REMARK 620 4 HOH A 503 O 167.3 88.4 87.4
REMARK 620 5 HOH A 512 O 86.5 86.4 162.2 80.8
REMARK 620 N 1 2 3 4
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 PRO A 246 O
REMARK 620 2 ASP A 249 O 78.7
REMARK 620 3 ILE A 252 O 89.5 79.6
REMARK 620 4 HOH A 475 O 78.8 157.1 96.0
REMARK 620 5 HOH A 485 O 176.7 104.0 89.0 98.3
REMARK 620 6 HOH A 504 O 86.7 90.1 169.6 92.8 95.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 466 O
REMARK 620 2 PRO B 246 O 92.9
REMARK 620 3 ASP B 249 O 94.1 78.8
REMARK 620 4 ILE B 252 O 172.6 83.7 78.8
REMARK 620 5 HOH B 463 O 97.7 168.1 105.6 86.3
REMARK 620 6 HOH B 486 O 93.3 78.3 156.3 92.4 95.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 33 O
REMARK 620 2 ALA B 36 O 95.1
REMARK 620 3 PHE B 39 O 100.4 71.5
REMARK 620 4 HOH B 499 O 133.4 68.4 113.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 231 O
REMARK 620 2 ASN B 234 OD1 79.3
REMARK 620 3 HOH B 472 O 79.8 138.8
REMARK 620 4 HOH B 476 O 73.0 80.1 126.1
REMARK 620 N 1 2 3
DBREF 8EU0 A -19 261 PDB 8EU0 8EU0 -19 261
DBREF 8EU0 B -19 261 PDB 8EU0 8EU0 -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 GLN 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 CSO PRO TYR
SEQRES 1 B 281 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 281 LEU VAL PRO ARG GLY SER HIS MET ALA ALA ASN PRO TYR
SEQRES 3 B 281 GLU ARG GLY PRO ASP PRO THR GLU SER SER LEU GLU ALA
SEQRES 4 B 281 SER SER GLY PRO PHE SER VAL SER GLN THR SER VAL SER
SEQRES 5 B 281 ARG LEU SER ALA SER GLY PHE GLY GLY GLY THR ILE TYR
SEQRES 6 B 281 TYR PRO THR THR THR SER GLU GLY THR TYR GLY ALA VAL
SEQRES 7 B 281 ALA ILE SER PRO GLY TYR THR ALA THR GLN SER SER ILE
SEQRES 8 B 281 ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 9 B 281 VAL ILE THR ILE ASP THR ASN THR THR PHE ASP GLN PRO
SEQRES 10 B 281 ASP SER ARG ALA ARG GLN LEU MET ALA ALA LEU ASN TYR
SEQRES 11 B 281 LEU VAL ASN ARG SER SER VAL ARG SER ARG ILE ASP SER
SEQRES 12 B 281 SER ARG LEU ALA VAL MET GLY HIS SER MET GLY GLY GLY
SEQRES 13 B 281 GLY THR LEU ARG ALA ALA GLU ASP ASN PRO SER LEU LYS
SEQRES 14 B 281 ALA ALA ILE PRO LEU THR PRO TRP HIS THR ASN LYS ASN
SEQRES 15 B 281 TRP SER SER VAL ARG VAL PRO THR LEU ILE ILE GLY ALA
SEQRES 16 B 281 GLU ASN ASP THR ILE ALA PRO VAL SER SER HIS ALA LYS
SEQRES 17 B 281 PRO PHE TYR ASN SER LEU PRO SER SER THR PRO LYS ALA
SEQRES 18 B 281 TYR LEU GLU LEU ASN GLY ALA SER HIS PHE ALA PRO ASN
SEQRES 19 B 281 SER SER ASN THR THR ILE GLY LYS TYR SER ILE ALA TRP
SEQRES 20 B 281 LEU LYS ARG PHE VAL ASP ASN ASP THR ARG TYR SER GLN
SEQRES 21 B 281 PHE LEU CYS PRO ALA PRO HIS ASP ASP SER ALA ILE SER
SEQRES 22 B 281 GLU TYR ARG SER THR CSO PRO TYR
HET CSO A 259 7
HET CSO B 259 7
HET PEG A 301 7
HET NA A 302 1
HET NA A 303 1
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HET PEG B 301 7
HET NA B 302 1
HET NA B 303 1
HET NA B 304 1
HET SO4 B 305 5
HET EDO B 306 4
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 3 PEG 2(C4 H10 O3)
FORMUL 4 NA 5(NA 1+)
FORMUL 6 EDO 4(C2 H6 O2)
FORMUL 13 SO4 O4 S 2-
FORMUL 15 HOH *266(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 LEU A 242 5 8
HELIX 11 AB2 ALA A 245 ASP A 249 5 5
HELIX 12 AB3 THR B 13 ALA B 19 1 7
HELIX 13 AB4 THR B 67 ALA B 72 5 6
HELIX 14 AB5 TRP B 73 SER B 80 1 8
HELIX 15 AB6 GLN B 96 ARG B 114 1 19
HELIX 16 AB7 VAL B 117 SER B 119 5 3
HELIX 17 AB8 SER B 132 ASN B 145 1 14
HELIX 18 AB9 HIS B 186 LEU B 194 1 9
HELIX 19 AC1 PHE B 211 SER B 215 5 5
HELIX 20 AC2 ASN B 217 VAL B 232 1 16
HELIX 21 AC3 ASP B 235 LEU B 242 5 8
HELIX 22 AC4 ALA B 245 ASP B 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 GLY A 56 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 3 THR A 170 ALA A 175 0
SHEET 2 AA2 3 LYS A 200 LEU A 205 1 O LEU A 203 N GLY A 174
SHEET 3 AA2 3 ILE A 252 THR A 258 -1 O ARG A 256 N TYR A 202
SHEET 1 AA3 6 VAL B 26 VAL B 31 0
SHEET 2 AA3 6 GLY B 42 PRO B 47 -1 O ILE B 44 N THR B 29
SHEET 3 AA3 6 PHE B 83 ILE B 88 -1 O VAL B 85 N TYR B 45
SHEET 4 AA3 6 TYR B 55 SER B 61 1 N GLY B 56 O VAL B 84
SHEET 5 AA3 6 ILE B 121 HIS B 131 1 O ASP B 122 N TYR B 55
SHEET 6 AA3 6 ALA B 150 LEU B 154 1 O LEU B 154 N GLY B 130
SHEET 1 AA4 3 THR B 170 ALA B 175 0
SHEET 2 AA4 3 LYS B 200 LEU B 205 1 O LEU B 205 N GLY B 174
SHEET 3 AA4 3 ILE B 252 THR B 258 -1 O ARG B 256 N TYR B 202
LINK C THR A 258 N CSO A 259 1555 1555 1.33
LINK C CSO A 259 N PRO A 260 1555 1555 1.34
LINK C THR B 258 N CSO B 259 1555 1555 1.33
LINK C CSO B 259 N PRO B 260 1555 1555 1.34
LINK O ARG A 33 NA NA A 303 1555 1555 2.35
LINK O ALA A 36 NA NA A 303 1555 1555 2.54
LINK O PHE A 39 NA NA A 303 1555 1555 2.44
LINK O PRO A 246 NA NA A 302 1555 1555 2.24
LINK O ASP A 249 NA NA A 302 1555 1555 2.35
LINK O ILE A 252 NA NA A 302 1555 1555 2.31
LINK NA NA A 302 O HOH A 475 1555 1555 2.35
LINK NA NA A 302 O HOH A 485 1555 1555 2.46
LINK NA NA A 302 O HOH A 504 1555 1555 2.46
LINK NA NA A 303 O HOH A 503 1555 1555 2.42
LINK NA NA A 303 O HOH A 512 1555 1555 2.58
LINK O HOH A 466 NA NA B 302 1555 1555 2.59
LINK O ARG B 33 NA NA B 303 1555 1555 2.35
LINK O ALA B 36 NA NA B 303 1555 1555 2.39
LINK O PHE B 39 NA NA B 303 1555 1555 2.56
LINK O PHE B 231 NA NA B 304 1555 1555 2.55
LINK OD1 ASN B 234 NA NA B 304 1555 1555 2.66
LINK O PRO B 246 NA NA B 302 1555 1555 2.29
LINK O ASP B 249 NA NA B 302 1555 1555 2.30
LINK O ILE B 252 NA NA B 302 1555 1555 2.49
LINK NA NA B 302 O HOH B 463 1555 1555 2.44
LINK NA NA B 302 O HOH B 486 1555 1555 2.36
LINK NA NA B 303 O HOH B 499 1555 1555 2.89
LINK NA NA B 304 O HOH B 472 1555 1555 2.40
LINK NA NA B 304 O HOH B 476 1555 1555 2.97
CRYST1 68.372 68.372 214.014 90.00 90.00 120.00 P 32 2 1 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 0.014626 0.008444 0.000000 0.00000
SCALE2 0.000000 0.016889 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004673 0.00000
TER 1997 TYR A 261
TER 3994 TYR B 261
MASTER 482 0 14 22 18 0 0 6 4266 2 86 44
END |