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HEADER HYDROLASE 26-JUN-19 6S42
TITLE THE DOUBLE MUTANT(ILE44LEU+GLN102HIS) OF HALOALKANE DEHALOGENASE DBEA
TITLE 2 FROM BRADYRHIZOBIUM ELKANII USDA94 WITH AN ELIMINATED HALIDE-BINDING
TITLE 3 SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: CHAIN A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM ELKANII;
SOURCE 3 ORGANISM_TAXID: 29448;
SOURCE 4 GENE: DBEA, DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-21B
KEYWDS HALOALKANE DEHALOGENASE, HALIDE-BINDING SITE, DOUBLE MUTANT, RANDOM
KEYWDS 2 MICROSEEDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PUDNIKOVA,J.R.MESTERS,I.KUTA SMATANOVA
REVDAT 1 05-FEB-20 6S42 0
JRNL AUTH T.PRUDNIKOVA,I.KUTA SMATANOVA
JRNL TITL CRYSTALLIZATION AND CRYSTALLOGRAPHIC ANALYSIS OF A
JRNL TITL 2 BRADYRHIZOBIUM ELKANII USDA94 HALOALKANE DEHALOGENASE
JRNL TITL 3 VARIANT WITH AN ELIMINATED HALIDE-BINDING SITE
JRNL REF CRYSTALS 2019
JRNL REFN ESSN 2073-4352
JRNL DOI 10.3390/CRYST9070375
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 68322
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3417
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 4.1980 - 4.0305 0.98 2831 150 0.1315 0.1533
REMARK 3 2 4.0305 - 3.1995 0.97 2770 145 0.1308 0.1315
REMARK 3 3 3.1995 - 2.7951 0.97 2734 144 0.1315 0.1443
REMARK 3 4 2.7951 - 2.5396 0.97 2751 145 0.1315 0.1769
REMARK 3 5 2.5396 - 2.3576 0.97 2756 145 0.1315 0.1623
REMARK 3 6 2.3576 - 2.2186 0.98 2742 144 0.1315 0.1319
REMARK 3 7 2.2186 - 2.1075 0.97 2727 144 0.1315 0.1451
REMARK 3 8 2.1075 - 2.0158 0.97 2726 143 0.1315 0.1601
REMARK 3 9 2.0158 - 1.9382 0.97 2718 143 0.1315 0.1667
REMARK 3 10 1.9382 - 1.8713 0.97 2738 144 0.1315 0.1555
REMARK 3 11 1.8713 - 1.8128 0.97 2713 143 0.1315 0.1626
REMARK 3 12 1.8128 - 1.7610 0.97 2690 142 0.1315 0.1528
REMARK 3 13 1.7610 - 1.7146 0.97 2712 143 0.1296 0.1393
REMARK 3 14 1.7146 - 1.6728 0.96 2675 140 0.1310 0.1412
REMARK 3 15 1.6728 - 1.6347 0.96 2682 142 0.1315 0.1564
REMARK 3 16 1.6347 - 1.5999 0.96 2716 142 0.1297 0.1542
REMARK 3 17 1.5999 - 1.5679 0.95 2692 142 0.1315 0.1430
REMARK 3 18 1.5679 - 1.5384 0.96 2670 141 0.1315 0.1549
REMARK 3 19 1.5384 - 1.5109 0.95 2689 141 0.1315 0.1363
REMARK 3 20 1.5109 - 1.4853 0.96 2653 140 0.1315 0.1550
REMARK 3 21 1.4853 - 1.4613 0.95 2672 141 0.1315 0.1666
REMARK 3 22 1.4613 - 1.4388 0.96 2656 139 0.1315 0.1813
REMARK 3 23 1.4388 - 1.4177 0.94 2652 140 0.1315 0.2113
REMARK 3 24 1.4177 - 1.4000 0.90 2540 134 0.1315 0.2070
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.42
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 : 0.006 2414
REMARK 3 ANGLE : 0.873 3293
REMARK 3 CHIRALITY : 0.080 353
REMARK 3 PLANARITY : 0.006 436
REMARK 3 DIHEDRAL : 8.987 1352
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2900 2.0645 23.8297
REMARK 3 T TENSOR
REMARK 3 T11: 0.0754 T22: 0.1439
REMARK 3 T33: 0.0400 T12: 0.0222
REMARK 3 T13: 0.0234 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.8904 L22: 1.5137
REMARK 3 L33: 0.7337 L12: 0.2958
REMARK 3 L13: -0.3770 L23: -0.0100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: -0.3123 S13: 0.0262
REMARK 3 S21: 0.2410 S22: 0.0093 S23: 0.0647
REMARK 3 S31: -0.0204 S32: -0.1973 S33: 0.0238
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7294 8.8778 15.3399
REMARK 3 T TENSOR
REMARK 3 T11: 0.0938 T22: 0.0977
REMARK 3 T33: 0.0846 T12: 0.0186
REMARK 3 T13: -0.0052 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.9183 L22: 0.6521
REMARK 3 L33: 0.4173 L12: -0.4787
REMARK 3 L13: 0.0561 L23: -0.4220
REMARK 3 S TENSOR
REMARK 3 S11: -0.1151 S12: -0.0589 S13: 0.1193
REMARK 3 S21: 0.0931 S22: 0.1044 S23: -0.0580
REMARK 3 S31: -0.1380 S32: -0.0099 S33: -0.0456
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 214 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3737 -8.4148 5.4932
REMARK 3 T TENSOR
REMARK 3 T11: 0.0653 T22: 0.0590
REMARK 3 T33: 0.0474 T12: -0.0186
REMARK 3 T13: 0.0185 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.4266 L22: 1.6886
REMARK 3 L33: 0.8910 L12: 0.1708
REMARK 3 L13: 0.7251 L23: 0.5255
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.0284 S13: -0.1256
REMARK 3 S21: -0.2232 S22: 0.0315 S23: -0.0287
REMARK 3 S31: 0.0314 S32: -0.0422 S33: 0.0339
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5202 4.6989 11.6554
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: 0.0765
REMARK 3 T33: 0.1090 T12: 0.0029
REMARK 3 T13: 0.0134 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.9640 L22: 1.3649
REMARK 3 L33: 0.6985 L12: 0.2343
REMARK 3 L13: 0.3841 L23: -0.1766
REMARK 3 S TENSOR
REMARK 3 S11: -0.0463 S12: 0.0439 S13: 0.0182
REMARK 3 S21: -0.0516 S22: 0.0088 S23: -0.2606
REMARK 3 S31: -0.0465 S32: 0.0761 S33: -0.0312
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 6S42 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1292103026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68322
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 41.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.180
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4K2A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MGCL2, TRIS-HCL 7.5, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 64.47250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.97500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.47250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.97500
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 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 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 CL CL A 411 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 1
REMARK 465 THR A 2
REMARK 465 ILE A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 ASP A 6
REMARK 465 ARG A 299
REMARK 465 HIS A 300
REMARK 465 ALA A 301
REMARK 465 ALA A 302
REMARK 465 LEU A 303
REMARK 465 GLU A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 298 CG CD OE1 NE2
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 847 O HOH A 877 1.96
REMARK 500 O HOH A 894 O HOH A 896 1.97
REMARK 500 O HOH A 789 O HOH A 823 1.97
REMARK 500 NE2 GLN A 140 O HOH A 501 2.03
REMARK 500 O HOH A 699 O HOH A 813 2.04
REMARK 500 O HOH A 809 O HOH A 920 2.08
REMARK 500 O HOH A 796 O HOH A 820 2.09
REMARK 500 O HOH A 502 O HOH A 810 2.11
REMARK 500 NH2 ARG A 145 O HOH A 502 2.15
REMARK 500 O HOH A 807 O HOH A 865 2.16
REMARK 500 O HOH A 516 O HOH A 675 2.19
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 560 O HOH A 760 2556 1.74
REMARK 500 O HOH A 741 O HOH A 801 4456 2.00
REMARK 500 O HOH A 760 O HOH A 832 2556 2.07
REMARK 500 O HOH A 624 O HOH A 831 2556 2.11
REMARK 500 O HOH A 850 O HOH A 861 4456 2.15
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 17 -153.28 -123.48
REMARK 500 PRO A 39 56.39 -107.57
REMARK 500 THR A 40 -154.52 -99.43
REMARK 500 SER A 41 -168.09 -162.93
REMARK 500 ASP A 103 -129.46 63.36
REMARK 500 HIS A 139 -175.14 71.63
REMARK 500 ALA A 244 -71.74 -132.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 962 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 963 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 964 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 965 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 966 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 967 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 968 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A 969 DISTANCE = 7.46 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K2A RELATED DB: PDB
REMARK 900 WILD TYPE
DBREF 6S42 A 1 302 UNP E2RV62 E2RV62_BRAEL 1 302
SEQADV 6S42 LEU A 44 UNP E2RV62 ILE 44 ENGINEERED MUTATION
SEQADV 6S42 HIS A 102 UNP E2RV62 GLN 102 ENGINEERED MUTATION
SEQADV 6S42 LEU A 303 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 GLU A 304 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 HIS A 305 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 HIS A 306 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 HIS A 307 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 HIS A 308 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 HIS A 309 UNP E2RV62 EXPRESSION TAG
SEQADV 6S42 HIS A 310 UNP E2RV62 EXPRESSION TAG
SEQRES 1 A 310 MET THR ILE SER ALA ASP ILE SER LEU HIS HIS ARG ALA
SEQRES 2 A 310 VAL LEU GLY SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 A 310 SER ASP ALA PRO HIS VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 310 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO LEU VAL
SEQRES 5 A 310 ALA PRO VAL GLY HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 310 TYR GLY GLN SER GLY LYS PRO ASP ILE SER TYR ARG PHE
SEQRES 7 A 310 PHE ASP GLN ALA ASP TYR LEU ASP ALA LEU ILE ASP GLU
SEQRES 8 A 310 LEU GLY ILE ALA SER ALA TYR LEU VAL ALA HIS ASP TRP
SEQRES 9 A 310 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 A 310 GLN LEU VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 310 PRO MET ARG ASP TRP SER ASP PHE HIS GLN HIS ASP ALA
SEQRES 12 A 310 ALA ARG GLU THR PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 A 310 GLY GLU ALA MET ILE LEU ASP ASN ASN ALA PHE VAL GLU
SEQRES 14 A 310 ARG VAL LEU PRO GLY SER ILE LEU ARG THR LEU SER GLU
SEQRES 15 A 310 GLU GLU MET ALA ALA TYR ARG ALA PRO PHE ALA THR ARG
SEQRES 16 A 310 GLU SER ARG MET PRO THR LEU MET LEU PRO ARG GLU LEU
SEQRES 17 A 310 PRO ILE ALA GLY GLU PRO ALA ASP VAL THR GLN ALA LEU
SEQRES 18 A 310 THR ALA ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 A 310 LYS LEU LEU PHE VAL GLY SER PRO GLY ALA LEU VAL SER
SEQRES 20 A 310 PRO ALA PHE ALA ALA GLU PHE ALA LYS THR LEU LYS HIS
SEQRES 21 A 310 CYS ALA VAL ILE GLN LEU GLY ALA GLY GLY HIS TYR LEU
SEQRES 22 A 310 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG SER VAL ALA
SEQRES 23 A 310 GLY TRP ILE ALA GLY ILE GLU ALA ALA SER ALA GLN ARG
SEQRES 24 A 310 HIS ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET HEZ A 401 8
HET IOD A 402 1
HET IOD A 403 1
HET IOD A 404 1
HET IOD A 405 1
HET IOD A 406 1
HET IOD A 407 1
HET IOD A 408 1
HET IOD A 409 1
HET CL A 410 1
HET CL A 411 1
HET CL A 412 1
HETNAM HEZ HEXANE-1,6-DIOL
HETNAM IOD IODIDE ION
HETNAM CL CHLORIDE ION
FORMUL 2 HEZ C6 H14 O2
FORMUL 3 IOD 8(I 1-)
FORMUL 11 CL 3(CL 1-)
FORMUL 14 HOH *469(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 1 6
HELIX 3 AA3 ARG A 77 LEU A 92 1 16
HELIX 4 AA4 ASP A 103 ARG A 116 1 14
HELIX 5 AA5 ASP A 134 PHE A 138 5 5
HELIX 6 AA6 HIS A 141 ARG A 152 1 12
HELIX 7 AA7 GLY A 155 LEU A 162 1 8
HELIX 8 AA8 ASN A 165 ARG A 170 1 6
HELIX 9 AA9 ARG A 170 SER A 175 1 6
HELIX 10 AB1 SER A 181 ALA A 190 1 10
HELIX 11 AB2 PRO A 191 ALA A 193 5 3
HELIX 12 AB3 ARG A 195 SER A 197 5 3
HELIX 13 AB4 ARG A 198 LEU A 208 1 11
HELIX 14 AB5 PRO A 214 SER A 231 1 18
HELIX 15 AB6 SER A 247 THR A 257 1 11
HELIX 16 AB7 TYR A 272 HIS A 277 1 6
HELIX 17 AB8 HIS A 277 ALA A 297 1 21
SHEET 1 AA1 8 HIS A 10 VAL A 14 0
SHEET 2 AA1 8 SER A 17 THR A 24 -1 O SER A 17 N VAL A 14
SHEET 3 AA1 8 HIS A 57 PRO A 61 -1 O CYS A 58 N THR A 24
SHEET 4 AA1 8 HIS A 31 LEU A 35 1 N VAL A 32 O ILE A 59
SHEET 5 AA1 8 ALA A 97 HIS A 102 1 O VAL A 100 N LEU A 33
SHEET 6 AA1 8 VAL A 120 MET A 126 1 O ALA A 124 N LEU A 99
SHEET 7 AA1 8 LYS A 235 PRO A 242 1 O LEU A 236 N PHE A 125
SHEET 8 AA1 8 CYS A 261 GLY A 269 1 O LEU A 266 N VAL A 239
CISPEP 1 ASN A 38 PRO A 39 0 -12.31
CISPEP 2 GLU A 213 PRO A 214 0 -4.46
CISPEP 3 SER A 241 PRO A 242 0 4.45
SITE 1 AC1 7 ASP A 103 HIS A 139 PHE A 148 VAL A 171
SITE 2 AC1 7 SER A 175 HIS A 271 IOD A 402
SITE 1 AC2 5 ASN A 38 TRP A 104 PHE A 167 PRO A 205
SITE 2 AC2 5 HEZ A 401
SITE 1 AC3 1 ASN A 164
SITE 1 AC4 1 HOH A 853
SITE 1 AC5 1 ARG A 22
SITE 1 AC6 1 LYS A 150
SITE 1 AC7 1 ARG A 149
SITE 1 AC8 2 GLN A 265 GLY A 267
SITE 1 AC9 5 HIS A 31 ALA A 95 SER A 96 HOH A 701
SITE 2 AC9 5 HOH A 899
SITE 1 AD1 3 GLU A 279 ALA A 280 HOH A 797
SITE 1 AD2 2 ARG A 133 HOH A 716
CRYST1 128.945 63.950 46.053 90.00 106.27 90.00 C 1 2 1 4
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 0.007755 0.000000 0.002263 0.00000
SCALE2 0.000000 0.015637 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022620 0.00000
TER 2334 GLN A 298
MASTER 451 0 12 17 8 0 14 6 2730 1 8 24
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