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HEADER HYDROLASE 15-JAN-20 6TY7
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE VARIANT DHAA115 DOMAIN-
TITLE 2 SWAPPED DIMER TYPE-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE VARIANT DHAA115 DOMAIN-SWAPPED
COMPND 3 DIMER TYPE-1;
COMPND 4 CHAIN: A, B;
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,R.CHALOUPKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 27-JAN-21 6TY7 0
JRNL AUTH K.MARKOVA,R.CHALOUPKOVA,J.DAMBORSKY,M.MAREK
JRNL TITL STRUCTURES OF HALOALKANE DEHALOGENASE VARIANT DHAA115
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 96088
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4710
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 71.9500 - 4.6605 1.00 3361 170 0.1626 0.1717
REMARK 3 2 4.6605 - 3.6992 1.00 3265 145 0.1388 0.1448
REMARK 3 3 3.6992 - 3.2316 1.00 3173 165 0.1586 0.1844
REMARK 3 4 3.2316 - 2.9361 1.00 3151 164 0.1764 0.1872
REMARK 3 5 2.9361 - 2.7257 1.00 3178 160 0.1735 0.2041
REMARK 3 6 2.7257 - 2.5649 1.00 3131 147 0.1716 0.2110
REMARK 3 7 2.5649 - 2.4365 1.00 3118 181 0.1649 0.1783
REMARK 3 8 2.4365 - 2.3304 1.00 3122 157 0.1683 0.1853
REMARK 3 9 2.3304 - 2.2407 1.00 3109 165 0.1575 0.1831
REMARK 3 10 2.2407 - 2.1634 1.00 3126 160 0.1637 0.2206
REMARK 3 11 2.1634 - 2.0957 1.00 3094 163 0.1679 0.2003
REMARK 3 12 2.0957 - 2.0358 1.00 3121 177 0.1684 0.1768
REMARK 3 13 2.0358 - 1.9822 1.00 3097 167 0.1671 0.1838
REMARK 3 14 1.9822 - 1.9338 1.00 3077 172 0.1650 0.1979
REMARK 3 15 1.9338 - 1.8899 1.00 3127 145 0.1661 0.1839
REMARK 3 16 1.8899 - 1.8497 1.00 3092 161 0.1659 0.1952
REMARK 3 17 1.8497 - 1.8127 1.00 3071 182 0.1674 0.2070
REMARK 3 18 1.8127 - 1.7784 1.00 3132 149 0.1650 0.1974
REMARK 3 19 1.7784 - 1.7467 1.00 3068 156 0.1650 0.2006
REMARK 3 20 1.7467 - 1.7171 1.00 3109 141 0.1625 0.1911
REMARK 3 21 1.7171 - 1.6894 1.00 3070 181 0.1717 0.2028
REMARK 3 22 1.6894 - 1.6634 1.00 3087 168 0.1836 0.2057
REMARK 3 23 1.6634 - 1.6389 0.99 3068 148 0.1948 0.2323
REMARK 3 24 1.6389 - 1.6158 0.99 3052 164 0.2087 0.2399
REMARK 3 25 1.6158 - 1.5940 0.99 3026 141 0.2255 0.2421
REMARK 3 26 1.5940 - 1.5733 0.96 2972 162 0.2318 0.2876
REMARK 3 27 1.5733 - 1.5536 0.92 2833 135 0.2477 0.3211
REMARK 3 28 1.5536 - 1.5349 0.86 2667 114 0.2608 0.2997
REMARK 3 29 1.5349 - 1.5171 0.82 2504 131 0.2733 0.2965
REMARK 3 30 1.5171 - 1.5000 0.77 2377 139 0.2710 0.3020
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.84
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 6TY7 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_1292106257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96088
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 75.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 45.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, PEG MME 550, SODIUM
REMARK 280 NITRATE, DISODIUM HYDROGENPHOSPHATE, AMMONIUM SULPHATE, MES,
REMARK 280 IMIDAZOLE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 292.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.96500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.95000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.82500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.95000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.96500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.82500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 214 OE1
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 50.54 -109.57
REMARK 500 THR A 43 -158.06 -104.20
REMARK 500 LYS A 74 68.24 -117.23
REMARK 500 GLU A 98 -89.73 -108.22
REMARK 500 ASP A 106 -130.15 56.60
REMARK 500 ASP A 156 -76.39 -98.97
REMARK 500 VAL A 245 -68.51 -134.79
REMARK 500 LEU A 271 -95.89 -111.84
REMARK 500 PHE B 8 77.95 -119.77
REMARK 500 PRO B 42 51.27 -104.45
REMARK 500 THR B 43 -158.15 -104.80
REMARK 500 GLU B 98 -90.96 -106.49
REMARK 500 ASP B 106 -126.87 51.65
REMARK 500 ASP B 156 -51.42 72.20
REMARK 500 VAL B 245 -66.10 -136.84
REMARK 500 LEU B 271 -99.24 -114.78
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 B 677 DISTANCE = 6.14 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 307
DBREF 6TY7 A 1 299 PDB 6TY7 6TY7 1 299
DBREF 6TY7 B 1 299 PDB 6TY7 6TY7 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
HET EDO A 500 4
HET EDO A 501 4
HET MES B 301 12
HET GOL B 302 6
HET PG4 B 303 13
HET NO3 B 304 4
HET EDO B 305 4
HET EDO B 306 4
HET EDO B 307 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM NO3 NITRATE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 EDO 5(C2 H6 O2)
FORMUL 5 MES C6 H13 N O4 S
FORMUL 6 GOL C3 H8 O3
FORMUL 7 PG4 C8 H18 O5
FORMUL 8 NO3 N O3 1-
FORMUL 12 HOH *543(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 PHE A 144 THR A 154 1 11
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 LYS A 195 TRP A 198 5 4
HELIX 13 AB4 ARG A 199 GLU A 208 1 10
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 TYR A 273 ASP A 277 5 5
HELIX 17 AB8 ASN A 278 LEU A 290 1 13
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 GLU B 143 ARG B 153 1 11
HELIX 23 AC5 ASP B 156 ILE B 163 1 8
HELIX 24 AC6 ASN B 166 GLY B 171 1 6
HELIX 25 AC7 GLY B 171 PHE B 176 1 6
HELIX 26 AC8 THR B 182 GLU B 191 1 10
HELIX 27 AC9 PRO B 192 LEU B 194 5 3
HELIX 28 AD1 LYS B 195 TRP B 198 5 4
HELIX 29 AD2 ARG B 199 LEU B 209 1 11
HELIX 30 AD3 PRO B 215 SER B 232 1 18
HELIX 31 AD4 PRO B 248 LEU B 259 1 12
HELIX 32 AD5 TYR B 273 ASP B 277 5 5
HELIX 33 AD6 ASN B 278 LEU B 290 1 13
HELIX 34 AD7 PRO B 291 HIS B 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 PHE A 37 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 ILE B 267 N TRP B 240
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 LYS A 263
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
CISPEP 1 ASN A 41 PRO A 42 0 -0.74
CISPEP 2 GLU A 214 PRO A 215 0 -5.46
CISPEP 3 THR A 242 PRO A 243 0 8.73
CISPEP 4 ASN B 41 PRO B 42 0 -2.18
CISPEP 5 TRP B 141 PRO B 142 0 0.86
CISPEP 6 GLU B 214 PRO B 215 0 -7.76
CISPEP 7 THR B 242 PRO B 243 0 8.00
SITE 1 AC1 6 TRP A 240 PRO A 249 ALA A 253 HOH A 725
SITE 2 AC1 6 HOH A 776 HOH A 826
SITE 1 AC2 1 HOH A 725
SITE 1 AC3 13 ASN A 41 ASP A 106 TRP A 107 PHE B 149
SITE 2 AC3 13 PHE B 168 ILE B 172 PHE B 176 PHE B 205
SITE 3 AC3 13 PRO B 206 LEU B 209 LEU B 246 HIS B 272
SITE 4 AC3 13 TYR B 273
SITE 1 AC4 5 PRO A 235 TRP A 289 PRO A 291 VAL B 101
SITE 2 AC4 5 LYS B 124
SITE 1 AC5 2 LYS B 175 HOH B 401
SITE 1 AC6 4 PRO A 206 ASN B 41 ASP B 106 TRP B 107
SITE 1 AC7 3 TRP B 240 PRO B 249 ALA B 253
SITE 1 AC8 1 PHE B 266
SITE 1 AC9 3 PRO B 9 PHE B 10 ASP B 11
CRYST1 55.930 75.650 143.900 90.00 90.00 90.00 P 21 21 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 0.017879 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013219 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006949 0.00000
TER 2370 LEU A 293
TER 4834 HIS B 299
MASTER 332 0 9 34 16 0 14 6 5387 2 55 46
END |