| content |
HEADER HYDROLASE 27-SEP-22 8B6O
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7 CIRCULAR
TITLE 2 PERMUTATED AT POSITIONS 141-156 (CPHALOTAGDELTA) FUSED TO M13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALOTAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 M13, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
REVDAT 1 11-OCT-23 8B6O 0
JRNL AUTH M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7
JRNL TITL 2 CIRCULAR PERMUTATED AT POSITIONS 141-156 (CPHALOTAGDELTA)
JRNL TITL 3 FUSED TO M13
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19255
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 963
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 40.6600 - 3.8300 1.00 2740 145 0.1810 0.1918
REMARK 3 2 3.8200 - 3.0400 1.00 2637 139 0.2158 0.2543
REMARK 3 3 3.0400 - 2.6500 1.00 2611 137 0.2523 0.3129
REMARK 3 4 2.6500 - 2.4100 1.00 2584 136 0.2647 0.2815
REMARK 3 5 2.4100 - 2.2400 1.00 2568 135 0.2885 0.3396
REMARK 3 6 2.2400 - 2.1100 1.00 2560 135 0.2866 0.3404
REMARK 3 7 2.1100 - 2.0000 1.00 2592 136 0.3067 0.3463
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) : 0.262
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.404
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.50
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 : 0.003 2388
REMARK 3 ANGLE : 0.616 3260
REMARK 3 CHIRALITY : 0.043 349
REMARK 3 PLANARITY : 0.005 425
REMARK 3 DIHEDRAL : 4.267 312
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 9 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1403 -8.6995 -32.9641
REMARK 3 T TENSOR
REMARK 3 T11: 0.4122 T22: 0.5299
REMARK 3 T33: 0.5771 T12: -0.0644
REMARK 3 T13: 0.0090 T23: 0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 5.1868 L22: 6.7635
REMARK 3 L33: 5.7495 L12: -2.8911
REMARK 3 L13: 2.6261 L23: 2.8538
REMARK 3 S TENSOR
REMARK 3 S11: -0.1197 S12: 0.3937 S13: 0.8252
REMARK 3 S21: 0.1794 S22: -0.1224 S23: 0.9573
REMARK 3 S31: -0.5271 S32: -0.4011 S33: 0.1865
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1677 -10.0208 -24.2628
REMARK 3 T TENSOR
REMARK 3 T11: 0.2752 T22: 0.2410
REMARK 3 T33: 0.3222 T12: -0.0558
REMARK 3 T13: 0.0287 T23: 0.1385
REMARK 3 L TENSOR
REMARK 3 L11: 2.5001 L22: 1.8771
REMARK 3 L33: 6.8012 L12: -0.3114
REMARK 3 L13: 2.0488 L23: 0.9287
REMARK 3 S TENSOR
REMARK 3 S11: -0.1597 S12: 0.2430 S13: 0.0278
REMARK 3 S21: 0.0547 S22: -0.1524 S23: 0.0559
REMARK 3 S31: 0.0355 S32: 0.3049 S33: 0.2287
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0082 6.1096 -20.5584
REMARK 3 T TENSOR
REMARK 3 T11: 0.8052 T22: 0.6450
REMARK 3 T33: 0.7236 T12: -0.3949
REMARK 3 T13: -0.1546 T23: 0.3067
REMARK 3 L TENSOR
REMARK 3 L11: 0.9903 L22: 1.8249
REMARK 3 L33: 3.6993 L12: -1.2236
REMARK 3 L13: -0.7168 L23: -0.1049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0812 S12: 0.1360 S13: 0.4390
REMARK 3 S21: 0.0028 S22: 0.2948 S23: -0.0770
REMARK 3 S31: -0.8480 S32: 0.5414 S33: 0.1005
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3343 -16.5997 -17.6733
REMARK 3 T TENSOR
REMARK 3 T11: 0.4166 T22: 0.5112
REMARK 3 T33: 0.3874 T12: 0.0946
REMARK 3 T13: -0.0023 T23: 0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 2.9488 L22: 2.3701
REMARK 3 L33: 5.9043 L12: -0.3797
REMARK 3 L13: 2.2548 L23: 0.2605
REMARK 3 S TENSOR
REMARK 3 S11: 0.0300 S12: 0.5619 S13: -0.1992
REMARK 3 S21: 0.3663 S22: 0.1260 S23: -0.3650
REMARK 3 S31: 0.7695 S32: 1.2607 S33: -0.0436
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 263 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0660 -7.8650 -12.0294
REMARK 3 T TENSOR
REMARK 3 T11: 0.3127 T22: 0.2756
REMARK 3 T33: 0.3245 T12: -0.0519
REMARK 3 T13: 0.0342 T23: 0.1125
REMARK 3 L TENSOR
REMARK 3 L11: 4.5969 L22: 2.2502
REMARK 3 L33: 6.6141 L12: 0.4747
REMARK 3 L13: 2.4246 L23: 2.4466
REMARK 3 S TENSOR
REMARK 3 S11: -0.1634 S12: -0.1060 S13: 0.1023
REMARK 3 S21: 0.3167 S22: -0.0574 S23: 0.0870
REMARK 3 S31: 0.0419 S32: 0.3167 S33: 0.1617
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 8B6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1292125778.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-18
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99995
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19257
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.810
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: D_1292125777
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 0.65 M
REMARK 280 SODIUM DIHYDROGEN PHOSPHATE, 1.00 M DIPOTASSIUM HYDROGEN
REMARK 280 PHOSPHATE, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
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+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
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 76.51000
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 76.51000
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 22.30000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.66000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 22.30000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.66000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.51000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.30000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.66000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.51000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 22.30000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.66000
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 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 GLY A 1
REMARK 465 MET A 2
REMARK 465 VAL A 3
REMARK 465 ASP A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 169
REMARK 465 ILE A 170
REMARK 465 GLY A 171
REMARK 465 GLY A 172
REMARK 465 THR A 173
REMARK 465 GLY A 174
REMARK 465 GLY A 175
REMARK 465 SER A 176
REMARK 465 GLY A 177
REMARK 465 GLY A 178
REMARK 465 THR A 179
REMARK 465 GLY A 180
REMARK 465 GLY A 181
REMARK 465 SER A 182
REMARK 465 GLY A 183
REMARK 465 GLY A 184
REMARK 465 SER A 185
REMARK 465 ILE A 186
REMARK 465 GLY A 187
REMARK 465 THR A 188
REMARK 465 GLY A 189
REMARK 465 PHE A 190
REMARK 465 GLU A 322
REMARK 465 TRP A 323
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 VAL A 120 -65.84 -132.96
REMARK 500 LEU A 146 -98.07 -118.96
REMARK 500 PRO A 224 49.62 -106.87
REMARK 500 THR A 225 -162.00 -103.93
REMARK 500 GLU A 280 -80.40 -102.35
REMARK 500 ASP A 288 -132.74 59.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8B6N RELATED DB: PDB
REMARK 900 RELATED ID: 8B6P RELATED DB: PDB
REMARK 900 RELATED ID: 8B6Q RELATED DB: PDB
DBREF 8B6O A 31 168 UNP P0A3G3 DHAA_RHOSO 156 293
DBREF 8B6O A 186 323 UNP P0A3G3 DHAA_RHOSO 4 141
SEQADV 8B6O GLY A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O MET A 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O VAL A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ASP A 4 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O SER A 5 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O SER A 6 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ARG A 7 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ARG A 8 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O LYS A 9 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O TRP A 10 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ASN A 11 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O LYS A 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O THR A 13 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O GLY A 14 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O HIS A 15 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ALA A 16 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O VAL A 17 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ARG A 18 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ALA A 19 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ILE A 20 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O GLY A 21 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O ARG A 22 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O LEU A 23 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O SER A 24 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O SER A 25 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O LEU A 26 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O GLU A 27 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O GLY A 28 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O GLY A 29 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O SER A 30 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6O LYS A 35 UNP P0A3G3 GLU 160 CONFLICT
SEQADV 8B6O VAL A 42 UNP P0A3G3 ALA 167 CONFLICT
SEQADV 8B6O THR A 47 UNP P0A3G3 ALA 172 CONFLICT
SEQADV 8B6O MET A 50 UNP P0A3G3 LYS 175 CONFLICT
SEQADV 8B6O GLY A 51 UNP P0A3G3 CYS 176 CONFLICT
SEQADV 8B6O ASN A 70 UNP P0A3G3 LYS 195 CONFLICT
SEQADV 8B6O GLU A 99 UNP P0A3G3 ALA 224 CONFLICT
SEQADV 8B6O ASP A 102 UNP P0A3G3 ASN 227 CONFLICT
SEQADV 8B6O LYS A 132 UNP P0A3G3 GLU 257 CONFLICT
SEQADV 8B6O ALA A 139 UNP P0A3G3 THR 264 CONFLICT
SEQADV 8B6O ASN A 147 UNP P0A3G3 HIS 272 CONFLICT
SEQADV 8B6O LEU A 148 UNP P0A3G3 TYR 273 CONFLICT
SEQADV 8B6O SER A 166 UNP P0A3G3 PRO 291 CONFLICT
SEQADV 8B6O THR A 167 UNP P0A3G3 ALA 292 CONFLICT
SEQADV 8B6O GLU A 169 UNP P0A3G3 LINKER
SEQADV 8B6O ILE A 170 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 171 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 172 UNP P0A3G3 LINKER
SEQADV 8B6O THR A 173 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 174 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 175 UNP P0A3G3 LINKER
SEQADV 8B6O SER A 176 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 177 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 178 UNP P0A3G3 LINKER
SEQADV 8B6O THR A 179 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 180 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 181 UNP P0A3G3 LINKER
SEQADV 8B6O SER A 182 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 183 UNP P0A3G3 LINKER
SEQADV 8B6O GLY A 184 UNP P0A3G3 LINKER
SEQADV 8B6O SER A 185 UNP P0A3G3 LINKER
SEQADV 8B6O VAL A 229 UNP P0A3G3 LEU 47 CONFLICT
SEQADV 8B6O THR A 240 UNP P0A3G3 SER 58 CONFLICT
SEQADV 8B6O GLY A 260 UNP P0A3G3 ASP 78 CONFLICT
SEQADV 8B6O PHE A 269 UNP P0A3G3 TYR 87 CONFLICT
SEQADV 8B6O MET A 270 UNP P0A3G3 LEU 88 CONFLICT
SEQADV 8B6O PHE A 310 UNP P0A3G3 CYS 128 CONFLICT
SEQRES 1 A 323 GLY MET VAL ASP SER SER ARG ARG LYS TRP ASN LYS THR
SEQRES 2 A 323 GLY HIS ALA VAL ARG ALA ILE GLY ARG LEU SER SER LEU
SEQRES 3 A 323 GLU GLY GLY SER ASP VAL GLY ARG LYS LEU ILE ILE ASP
SEQRES 4 A 323 GLN ASN VAL PHE ILE GLU GLY THR LEU PRO MET GLY VAL
SEQRES 5 A 323 VAL ARG PRO LEU THR GLU VAL GLU MET ASP HIS TYR ARG
SEQRES 6 A 323 GLU PRO PHE LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP
SEQRES 7 A 323 ARG PHE PRO ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA
SEQRES 8 A 323 ASN ILE VAL ALA LEU VAL GLU GLU TYR MET ASP TRP LEU
SEQRES 9 A 323 HIS GLN SER PRO VAL PRO LYS LEU LEU PHE TRP GLY THR
SEQRES 10 A 323 PRO GLY VAL LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU
SEQRES 11 A 323 ALA LYS SER LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY
SEQRES 12 A 323 PRO GLY LEU ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU
SEQRES 13 A 323 ILE GLY SER GLU ILE ALA ARG TRP LEU SER THR LEU GLU
SEQRES 14 A 323 ILE GLY GLY THR GLY GLY SER GLY GLY THR GLY GLY SER
SEQRES 15 A 323 GLY GLY SER ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 16 A 323 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 17 A 323 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 18 A 323 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 19 A 323 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 20 A 323 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 21 A 323 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 22 A 323 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 23 A 323 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 24 A 323 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 25 A 323 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP
HET CL A 401 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *47(H2 O)
HELIX 1 AA1 LYS A 9 ALA A 19 1 11
HELIX 2 AA2 ALA A 19 GLU A 27 1 9
HELIX 3 AA3 ASP A 31 ASP A 39 1 9
HELIX 4 AA4 ASN A 41 GLY A 46 1 6
HELIX 5 AA5 LEU A 48 VAL A 52 5 5
HELIX 6 AA6 THR A 57 GLU A 66 1 10
HELIX 7 AA7 PRO A 67 LEU A 69 5 3
HELIX 8 AA8 ASN A 70 ASP A 73 5 4
HELIX 9 AA9 ARG A 74 GLU A 83 1 10
HELIX 10 AB1 PRO A 90 SER A 107 1 18
HELIX 11 AB2 PRO A 123 LEU A 134 1 12
HELIX 12 AB3 LEU A 148 ASN A 153 1 6
HELIX 13 AB4 ASN A 153 THR A 167 1 15
HELIX 14 AB5 SER A 226 ARG A 231 5 6
HELIX 15 AB6 ILE A 233 ALA A 238 1 6
HELIX 16 AB7 PHE A 262 LEU A 277 1 16
HELIX 17 AB8 ASP A 288 ASN A 301 1 14
SHEET 1 AA1 8 CYS A 137 GLY A 145 0
SHEET 2 AA1 8 LYS A 111 PRO A 118 1 N LEU A 113 O VAL A 140
SHEET 3 AA1 8 VAL A 305 MET A 311 1 O PHE A 310 N PHE A 114
SHEET 4 AA1 8 VAL A 282 HIS A 287 1 N LEU A 284 O ALA A 309
SHEET 5 AA1 8 VAL A 217 LEU A 220 1 N LEU A 218 O VAL A 283
SHEET 6 AA1 8 CYS A 243 PRO A 246 1 O ILE A 244 N PHE A 219
SHEET 7 AA1 8 GLU A 202 VAL A 209 -1 N VAL A 209 O CYS A 243
SHEET 8 AA1 8 HIS A 195 VAL A 199 -1 N VAL A 199 O GLU A 202
CISPEP 1 GLU A 89 PRO A 90 0 -1.18
CISPEP 2 THR A 117 PRO A 118 0 0.16
CISPEP 3 ASN A 223 PRO A 224 0 -1.09
CRYST1 44.600 81.320 153.020 90.00 90.00 90.00 C 2 2 21 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 0.022422 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006535 0.00000
TER 2315 ASP A 321
MASTER 352 0 1 17 8 0 0 6 2362 1 0 25
END |