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HEADER HYDROLASE 15-JAN-20 6XT8
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE VARIANT DHAA115 DOMAIN-
TITLE 2 SWAPPED DIMER TYPE-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE VARIANT DHAA115 DOMAIN-SWAPPED
COMPND 3 DIMER TYPE-2;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES
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 HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MARKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 27-JAN-21 6XT8 0
JRNL AUTH K.MARKOVA,J.DAMBORSKY,M.MAREK
JRNL TITL STRUCTURES OF HALOALKANE DEHALOGENASE VARIANT DHAA115
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 141366
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 7006
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 45.5280 - 5.2796 0.96 4436 251 0.1587 0.1574
REMARK 3 2 5.2796 - 4.1915 0.99 4576 229 0.1345 0.1498
REMARK 3 3 4.1915 - 3.6620 0.99 4572 232 0.1496 0.1865
REMARK 3 4 3.6620 - 3.3273 0.93 4294 218 0.1640 0.1746
REMARK 3 5 3.3273 - 3.0888 0.98 4518 238 0.1725 0.2067
REMARK 3 6 3.0888 - 2.9068 0.99 4496 275 0.1848 0.2145
REMARK 3 7 2.9068 - 2.7612 0.99 4521 246 0.1917 0.2262
REMARK 3 8 2.7612 - 2.6410 0.99 4517 229 0.1885 0.2226
REMARK 3 9 2.6410 - 2.5394 0.99 4634 229 0.1965 0.2510
REMARK 3 10 2.5394 - 2.4517 0.99 4550 224 0.1955 0.2418
REMARK 3 11 2.4517 - 2.3751 0.97 4403 220 0.2013 0.2344
REMARK 3 12 2.3751 - 2.3072 0.93 4328 221 0.1916 0.2266
REMARK 3 13 2.3072 - 2.2465 0.98 4426 257 0.1924 0.2448
REMARK 3 14 2.2465 - 2.1917 0.99 4539 264 0.2071 0.2435
REMARK 3 15 2.1917 - 2.1418 0.99 4478 230 0.2044 0.2245
REMARK 3 16 2.1418 - 2.0962 0.99 4599 210 0.2108 0.2387
REMARK 3 17 2.0962 - 2.0543 0.99 4450 228 0.2131 0.2501
REMARK 3 18 2.0543 - 2.0156 0.99 4533 242 0.2202 0.2725
REMARK 3 19 2.0156 - 1.9796 0.99 4486 253 0.2160 0.2573
REMARK 3 20 1.9796 - 1.9460 0.99 4514 221 0.2149 0.2406
REMARK 3 21 1.9460 - 1.9146 0.99 4564 245 0.2208 0.2649
REMARK 3 22 1.9146 - 1.8851 0.98 4494 224 0.2256 0.2759
REMARK 3 23 1.8851 - 1.8574 0.98 4500 197 0.2338 0.2819
REMARK 3 24 1.8574 - 1.8313 0.92 4231 229 0.2478 0.2991
REMARK 3 25 1.8313 - 1.8065 0.97 4378 244 0.2582 0.2920
REMARK 3 26 1.8065 - 1.7831 0.98 4442 234 0.2611 0.3228
REMARK 3 27 1.7831 - 1.7608 0.98 4528 219 0.2616 0.3133
REMARK 3 28 1.7608 - 1.7395 0.98 4451 242 0.2584 0.2948
REMARK 3 29 1.7395 - 1.7193 0.98 4446 232 0.2733 0.3066
REMARK 3 30 1.7193 - 1.7000 0.96 4456 223 0.2898 0.3170
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.26
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 : NULL
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 6XT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1292106262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 0.861
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 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141424
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.60100
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: 4HZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM NITRATE, BIS-TRIS,
REMARK 280 PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 82.30650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 HIS D 295
REMARK 465 HIS D 296
REMARK 465 HIS D 297
REMARK 465 HIS D 298
REMARK 465 HIS D 299
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 42 51.36 -102.53
REMARK 500 THR A 43 -156.70 -107.23
REMARK 500 GLU A 98 -92.81 -110.98
REMARK 500 ASP A 106 -132.55 55.67
REMARK 500 ASP A 156 -56.60 72.03
REMARK 500 TRP A 198 -118.69 58.84
REMARK 500 VAL A 245 -71.74 -129.51
REMARK 500 LEU A 271 -92.90 -116.32
REMARK 500 PRO B 42 52.34 -106.11
REMARK 500 THR B 43 -154.11 -106.93
REMARK 500 GLU B 98 -90.39 -103.90
REMARK 500 ASP B 106 -131.91 53.17
REMARK 500 ASP B 156 -55.75 72.60
REMARK 500 TRP B 198 -113.67 55.58
REMARK 500 VAL B 245 -72.24 -129.96
REMARK 500 LEU B 271 -93.90 -116.88
REMARK 500 PRO C 42 49.05 -101.85
REMARK 500 THR C 43 -153.56 -103.94
REMARK 500 GLU C 98 -86.18 -108.42
REMARK 500 ASP C 106 -131.61 56.01
REMARK 500 ASP C 156 -50.56 75.08
REMARK 500 TRP C 198 -86.15 -118.20
REMARK 500 ASN C 217 -75.90 -29.87
REMARK 500 VAL C 245 -73.18 -127.18
REMARK 500 LEU C 271 -95.92 -116.12
REMARK 500 PRO D 9 56.13 -91.87
REMARK 500 PRO D 42 53.26 -111.99
REMARK 500 THR D 43 -154.81 -109.04
REMARK 500 SER D 44 -169.54 -162.62
REMARK 500 ASP D 106 -133.74 61.05
REMARK 500 ASP D 156 -44.40 70.97
REMARK 500 TRP D 198 -85.62 -122.72
REMARK 500 VAL D 245 -70.16 -130.79
REMARK 500 LEU D 271 -91.03 -120.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 306
DBREF 6XT8 A 1 299 PDB 6XT8 6XT8 1 299
DBREF 6XT8 B 1 299 PDB 6XT8 6XT8 1 299
DBREF 6XT8 C 1 299 PDB 6XT8 6XT8 1 299
DBREF 6XT8 D 1 299 PDB 6XT8 6XT8 1 299
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 B 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 B 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 B 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 B 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 B 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 B 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 B 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 B 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 B 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 B 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 B 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 B 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 B 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 B 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 B 299 PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 B 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU
SEQRES 18 B 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 B 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 B 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 B 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 B 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 B 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 C 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 C 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 C 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 C 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 C 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 C 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 C 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 C 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 C 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 C 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 C 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 C 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 C 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 C 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 C 299 PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 C 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU
SEQRES 18 C 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 C 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 C 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 C 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 C 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 C 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 D 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 D 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 D 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 D 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 D 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 D 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 D 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 D 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 D 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 D 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 D 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 D 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 D 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 D 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 D 299 PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 D 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU
SEQRES 18 D 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 D 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 D 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 D 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 D 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 D 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET GOL A 302 6
HET GOL A 303 6
HET PG4 A 304 13
HET EDO A 305 4
HET CL B 301 1
HET GOL B 302 6
HET GOL B 303 6
HET CL C 301 1
HET GOL C 302 6
HET GOL C 303 6
HET GOL C 304 6
HET EDO C 305 4
HET CL C 306 1
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 CL 4(CL 1-)
FORMUL 6 GOL 7(C3 H8 O3)
FORMUL 8 PG4 C8 H18 O5
FORMUL 9 EDO 2(C2 H6 O2)
FORMUL 19 HOH *683(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 ARG A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 GLY A 171 PHE A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ARG A 199 LEU A 209 1 11
HELIX 13 AB4 PRO A 215 SER A 232 1 18
HELIX 14 AB5 PRO A 248 LEU A 259 1 12
HELIX 15 AB6 TYR A 273 ASN A 278 1 6
HELIX 16 AB7 ASN A 278 LEU A 290 1 13
HELIX 17 AB8 PRO A 291 LEU A 293 5 3
HELIX 18 AB9 SER B 44 ARG B 49 5 6
HELIX 19 AC1 ILE B 51 ALA B 56 1 6
HELIX 20 AC2 ARG B 80 LEU B 95 1 16
HELIX 21 AC3 ASP B 106 ASN B 119 1 14
HELIX 22 AC4 THR B 137 TRP B 141 5 5
HELIX 23 AC5 PRO B 142 ARG B 153 1 12
HELIX 24 AC6 ASP B 156 ILE B 163 1 8
HELIX 25 AC7 ASN B 166 GLY B 171 1 6
HELIX 26 AC8 GLY B 171 PHE B 176 1 6
HELIX 27 AC9 THR B 182 GLU B 191 1 10
HELIX 28 AD1 PRO B 192 LEU B 194 5 3
HELIX 29 AD2 ARG B 199 PHE B 205 1 7
HELIX 30 AD3 PRO B 206 LEU B 209 5 4
HELIX 31 AD4 PRO B 215 SER B 232 1 18
HELIX 32 AD5 PRO B 248 LEU B 259 1 12
HELIX 33 AD6 TYR B 273 ASN B 278 1 6
HELIX 34 AD7 ASN B 278 LEU B 290 1 13
HELIX 35 AD8 PRO B 291 HIS B 294 5 4
HELIX 36 AD9 SER C 44 ARG C 49 5 6
HELIX 37 AE1 ILE C 51 ALA C 56 1 6
HELIX 38 AE2 ARG C 80 LEU C 95 1 16
HELIX 39 AE3 ASP C 106 ASN C 119 1 14
HELIX 40 AE4 THR C 137 TRP C 141 5 5
HELIX 41 AE5 PRO C 142 ARG C 153 1 12
HELIX 42 AE6 ASP C 156 ILE C 163 1 8
HELIX 43 AE7 ASN C 166 GLY C 171 1 6
HELIX 44 AE8 GLY C 171 PHE C 176 1 6
HELIX 45 AE9 THR C 182 GLU C 191 1 10
HELIX 46 AF1 PRO C 192 LEU C 194 5 3
HELIX 47 AF2 ARG C 199 PHE C 205 1 7
HELIX 48 AF3 PRO C 206 LEU C 209 5 4
HELIX 49 AF4 PRO C 215 SER C 232 1 18
HELIX 50 AF5 PRO C 248 LEU C 259 1 12
HELIX 51 AF6 TYR C 273 ASP C 277 5 5
HELIX 52 AF7 ASN C 278 LEU C 290 1 13
HELIX 53 AF8 PRO C 291 LEU C 293 5 3
HELIX 54 AF9 SER D 44 ARG D 49 5 6
HELIX 55 AG1 ILE D 51 ALA D 56 1 6
HELIX 56 AG2 ARG D 80 LEU D 95 1 16
HELIX 57 AG3 ASP D 106 ASN D 119 1 14
HELIX 58 AG4 ALA D 145 ARG D 153 1 9
HELIX 59 AG5 ASP D 156 ILE D 163 1 8
HELIX 60 AG6 ASN D 166 GLY D 171 1 6
HELIX 61 AG7 GLY D 171 PHE D 176 1 6
HELIX 62 AG8 THR D 182 GLU D 191 1 10
HELIX 63 AG9 PRO D 192 LEU D 194 5 3
HELIX 64 AH1 ARG D 199 LEU D 209 1 11
HELIX 65 AH2 PRO D 215 SER D 232 1 18
HELIX 66 AH3 PRO D 248 LEU D 259 1 12
HELIX 67 AH4 TYR D 273 ASP D 277 5 5
HELIX 68 AH5 ASN D 278 LEU D 290 1 13
HELIX 69 AH6 PRO D 291 HIS D 294 5 4
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 SER A 20 VAL A 27 -1 O SER A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N VAL A 35 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE A 128
SHEET 8 AA1 8 LEU B 262 GLY B 270 1 O VAL B 265 N LEU B 238
SHEET 1 AA2 8 LEU A 262 GLY A 270 0
SHEET 2 AA2 8 LYS A 236 PRO A 243 1 N LEU A 238 O VAL A 265
SHEET 3 AA2 8 VAL B 123 MET B 129 1 O PHE B 128 N LEU A 237
SHEET 4 AA2 8 VAL B 100 HIS B 105 1 N LEU B 102 O ALA B 127
SHEET 5 AA2 8 VAL B 35 LEU B 38 1 N LEU B 36 O VAL B 101
SHEET 6 AA2 8 CYS B 61 PRO B 64 1 O ILE B 62 N PHE B 37
SHEET 7 AA2 8 SER B 20 VAL B 27 -1 N VAL B 27 O CYS B 61
SHEET 8 AA2 8 HIS B 13 VAL B 17 -1 N VAL B 17 O SER B 20
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 SER C 20 VAL C 27 -1 O SER C 20 N VAL C 17
SHEET 3 AA3 8 CYS C 61 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 VAL C 35 LEU C 38 1 N VAL C 35 O ILE C 62
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 101 N LEU C 36
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O ALA C 127 N LEU C 102
SHEET 7 AA3 8 LYS D 236 PRO D 243 1 O LEU D 237 N PHE C 128
SHEET 8 AA3 8 LEU D 262 GLY D 270 1 O LYS D 263 N LEU D 238
SHEET 1 AA4 8 LEU C 262 GLY C 270 0
SHEET 2 AA4 8 LYS C 236 PRO C 243 1 N LEU C 238 O VAL C 265
SHEET 3 AA4 8 VAL D 123 MET D 129 1 O PHE D 128 N LEU C 237
SHEET 4 AA4 8 VAL D 100 HIS D 105 1 N LEU D 102 O ALA D 127
SHEET 5 AA4 8 VAL D 35 LEU D 38 1 N LEU D 36 O VAL D 101
SHEET 6 AA4 8 CYS D 61 PRO D 64 1 O ILE D 62 N PHE D 37
SHEET 7 AA4 8 SER D 20 VAL D 27 -1 N VAL D 27 O CYS D 61
SHEET 8 AA4 8 HIS D 13 VAL D 17 -1 N VAL D 17 O SER D 20
CISPEP 1 ASN A 41 PRO A 42 0 -6.50
CISPEP 2 GLU A 214 PRO A 215 0 -5.65
CISPEP 3 THR A 242 PRO A 243 0 2.29
CISPEP 4 ASN B 41 PRO B 42 0 -5.04
CISPEP 5 GLU B 214 PRO B 215 0 -2.42
CISPEP 6 THR B 242 PRO B 243 0 6.48
CISPEP 7 ASN C 41 PRO C 42 0 -7.36
CISPEP 8 GLU C 214 PRO C 215 0 -3.59
CISPEP 9 THR C 242 PRO C 243 0 5.24
CISPEP 10 ASN D 41 PRO D 42 0 -1.78
CISPEP 11 GLU D 214 PRO D 215 0 0.77
CISPEP 12 THR D 242 PRO D 243 0 5.22
SITE 1 AC1 5 ASN A 41 TRP A 107 HOH A 407 PHE B 205
SITE 2 AC1 5 PRO B 206
SITE 1 AC2 8 ASP A 89 GLU A 93 ARG A 118 ASN A 119
SITE 2 AC2 8 ARG A 122 HOH A 405 HOH A 453 HOH A 473
SITE 1 AC3 8 TRP A 138 ARG A 153 HOH A 401 HOH A 518
SITE 2 AC3 8 HOH A 532 HOH A 590 ILE B 211 GLU B 214
SITE 1 AC4 4 THR A 242 PHE A 266 GLY A 268 PRO A 269
SITE 1 AC5 7 GLY A 213 TRP A 219 HOH A 411 HOH A 440
SITE 2 AC5 7 GLY B 5 THR B 6 GLY B 7
SITE 1 AC6 4 PHE A 205 PRO A 206 ASN B 41 TRP B 107
SITE 1 AC7 5 ASP B 89 ARG B 118 ASN B 119 HOH B 428
SITE 2 AC7 5 HOH B 543
SITE 1 AC8 9 PHE B 8 SER B 44 GLY B 70 LYS B 71
SITE 2 AC8 9 HIS B 188 GLU B 191 HOH B 404 HOH B 406
SITE 3 AC8 9 HOH B 419
SITE 1 AC9 6 ASN C 41 TRP C 107 PHE C 168 HOH C 409
SITE 2 AC9 6 PHE D 205 PRO D 206
SITE 1 AD1 6 GLY C 5 THR C 6 GLY C 7 HOH C 422
SITE 2 AD1 6 ASN D 227 GLN D 231
SITE 1 AD2 7 PHE C 8 GLY C 70 LYS C 71 HIS C 188
SITE 2 AD2 7 GLU C 191 HOH C 404 HOH C 407
SITE 1 AD3 7 ASP C 89 GLU C 93 TRP C 115 ARG C 118
SITE 2 AD3 7 ASN C 119 ARG C 122 HOH C 457
SITE 1 AD4 2 PHE C 144 HOH C 410
SITE 1 AD5 5 PHE C 205 PRO C 206 ASN D 41 TRP D 107
SITE 2 AD5 5 HOH D 387
CRYST1 44.900 164.613 92.736 90.00 100.92 90.00 P 1 21 1 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 0.022272 0.000000 0.004298 0.00000
SCALE2 0.000000 0.006075 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010982 0.00000
TER 2369 LEU A 293
TER 4749 HIS B 294
TER 7126 LEU C 293
TER 9533 HIS D 294
MASTER 372 0 14 69 32 0 26 610228 4 63 92
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