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HEADER HYDROLASE 02-JUN-20 7C8L
TITLE HYBRID DESIGNING OF POTENT INHIBITORS OF STRIGA STRIGOLACTONE RECEPTOR
TITLE 2 SHHTL7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SHHTL7;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_COMMON: PURPLE WITCHWEED;
SOURCE 4 ORGANISM_TAXID: 68872;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SHHTL7, KOK1007, COVALENT INHIBITOR, SPECIFICITY, STRIGA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.F.SHAHUL HAMEED,S.T.AROLD
REVDAT 1 02-JUN-21 7C8L 0
JRNL AUTH U.F.SHAHUL HAMEED,S.T.AROLD
JRNL TITL HYBRID DESIGNING OF POTENT INHIBITORS OF STRIGA
JRNL TITL 2 STRIGOLACTONE RECEPTOR SHHTL7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 66675
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.850
REMARK 3 FREE R VALUE TEST SET COUNT : 1903
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 46.2370 - 3.4914 1.00 4881 145 0.1459 0.1688
REMARK 3 2 3.4914 - 2.7713 1.00 4837 139 0.1313 0.1688
REMARK 3 3 2.7713 - 2.4210 1.00 4810 147 0.1298 0.1588
REMARK 3 4 2.4210 - 2.1997 1.00 4788 139 0.1237 0.1615
REMARK 3 5 2.1997 - 2.0420 1.00 4785 147 0.1074 0.1412
REMARK 3 6 2.0420 - 1.9216 1.00 4761 137 0.1091 0.1401
REMARK 3 7 1.9216 - 1.8254 0.99 4762 138 0.1110 0.1434
REMARK 3 8 1.8254 - 1.7459 0.99 4713 140 0.1379 0.1892
REMARK 3 9 1.7459 - 1.6787 0.98 4679 132 0.1459 0.1761
REMARK 3 10 1.6787 - 1.6208 0.96 4621 139 0.1640 0.2077
REMARK 3 11 1.6208 - 1.5701 0.94 4452 133 0.1925 0.2266
REMARK 3 12 1.5701 - 1.5252 0.92 4445 130 0.2075 0.2549
REMARK 3 13 1.5252 - 1.4850 0.88 4213 116 0.2369 0.2966
REMARK 3 14 1.4850 - 1.4500 0.84 4025 121 0.2542 0.2959
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.51
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 7C8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1300017190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68930
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.449
REMARK 200 RESOLUTION RANGE LOW (A) : 46.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 18.70
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.090
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: 5Z89
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 8000, 100 MM MES/ SODIUM
REMARK 280 HYDROXIDE PH 6.0, 200 MM CALCIUM ACETATE, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 53.50400
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 26.75200
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 40.12800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 13.37600
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 66.88000
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: 160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 271
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 95 -90.32 7.72
REMARK 500 ARG A 123 131.54 -172.31
REMARK 500 LEU A 247 63.83 -119.19
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 670 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 671 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A 674 DISTANCE = 7.21 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EGC A 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EGC A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FP6 A 305
DBREF1 7C8L A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 7C8L A A0A0M3PNA2 1 271
SEQADV 7C8L GLY A -4 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 7C8L PRO A -3 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 7C8L LEU A -2 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 7C8L GLY A -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 7C8L SER A 0 UNP A0A0M3PNA EXPRESSION TAG
SEQRES 1 A 276 GLY PRO LEU GLY SER MET SER SER ILE GLY LEU ALA HIS
SEQRES 2 A 276 ASN VAL THR ILE LEU GLY SER GLY GLU THR THR VAL VAL
SEQRES 3 A 276 LEU GLY HIS GLY TYR GLY THR ASP GLN SER VAL TRP LYS
SEQRES 4 A 276 LEU LEU VAL PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU
SEQRES 5 A 276 LEU TYR ASP HIS MET GLY ALA GLY THR THR ASN PRO ASP
SEQRES 6 A 276 TYR PHE ASP PHE ASP ARG TYR SER SER LEU GLU GLY TYR
SEQRES 7 A 276 SER TYR ASP LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL
SEQRES 8 A 276 SER LYS CYS ILE TYR VAL GLY HIS SER MET SER SER MET
SEQRES 9 A 276 ALA ALA ALA VAL ALA SER ILE PHE ARG PRO ASP LEU PHE
SEQRES 10 A 276 HIS LYS LEU VAL MET ILE SER PRO THR PRO ARG LEU ILE
SEQRES 11 A 276 ASN THR GLU GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL
SEQRES 12 A 276 MET ASP GLU THR LEU ARG SER LEU ASP GLU ASN PHE LYS
SEQRES 13 A 276 SER LEU SER LEU GLY THR ALA PRO LEU LEU LEU ALA CYS
SEQRES 14 A 276 ASP LEU GLU SER ALA ALA MET GLN GLU TYR CYS ARG THR
SEQRES 15 A 276 LEU PHE ASN MET ARG PRO ASP ILE ALA CYS CYS ILE THR
SEQRES 16 A 276 ARG MET ILE CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY
SEQRES 17 A 276 HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER SER ASN
SEQRES 18 A 276 ASP ILE MET VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG
SEQRES 19 A 276 LYS ASN LEU GLY GLY PRO SER VAL VAL GLU VAL MET PRO
SEQRES 20 A 276 THR GLU GLY HIS LEU PRO HIS LEU SER MET PRO GLU VAL
SEQRES 21 A 276 THR ILE PRO VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE
SEQRES 22 A 276 THR ASP HIS
HET EGC A 301 31
HET SO4 A 302 5
HET SO4 A 303 5
HET GOL A 304 6
HET FP6 A 305 7
HETNAM EGC 2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-TETRAMETHYL-
HETNAM 2 EGC BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 3 EGC ETHOXY)-ETHOXY]-ETHOX Y}-ETHOXY)-ETHANOL
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM FP6 PYRROLIDINE-1-CARBALDEHYDE
HETSYN EGC TRITON X-100
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EGC C32 H58 O10
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 FP6 C5 H9 N O
FORMUL 7 HOH *274(H2 O)
HELIX 1 AA1 SER A 3 HIS A 8 1 6
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 ASN A 58 PHE A 62 5 5
HELIX 5 AA5 ASP A 65 SER A 69 5 5
HELIX 6 AA6 LEU A 70 PHE A 84 1 15
HELIX 7 AA7 SER A 95 ARG A 108 1 14
HELIX 8 AA8 GLU A 135 SER A 145 1 11
HELIX 9 AA9 SER A 145 ALA A 163 1 19
HELIX 10 AB1 SER A 168 PHE A 179 1 12
HELIX 11 AB2 ARG A 182 LEU A 196 1 15
HELIX 12 AB3 LEU A 198 VAL A 205 5 8
HELIX 13 AB4 VAL A 222 LEU A 232 1 11
HELIX 14 AB5 LEU A 247 MET A 252 1 6
HELIX 15 AB6 MET A 252 GLN A 266 1 15
SHEET 1 AA1 7 THR A 11 GLY A 14 0
SHEET 2 AA1 7 LYS A 45 TYR A 49 -1 O VAL A 46 N LEU A 13
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N VAL A 20 O LYS A 45
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O VAL A 92 N VAL A 21
SHEET 5 AA1 7 PHE A 112 ILE A 118 1 O VAL A 116 N TYR A 91
SHEET 6 AA1 7 CYS A 209 ASN A 216 1 O HIS A 210 N MET A 117
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O VAL A 237 N ILE A 211
LINK OG SER A 95 CAB FP6 A 305 1555 1555 1.37
SITE 1 AC1 10 ILE A 106 PHE A 107 PRO A 109 PHE A 134
SITE 2 AC1 10 VAL A 138 THR A 142 LEU A 153 THR A 157
SITE 3 AC1 10 MET A 219 HOH A 485
SITE 1 AC2 5 SER A 15 GLY A 16 LYS A 45 ARG A 229
SITE 2 AC2 5 HOH A 587
SITE 1 AC3 2 THR A 127 ARG A 199
SITE 1 AC4 7 TYR A 130 TYR A 131 ALA A 223 TYR A 227
SITE 2 AC4 7 HOH A 473 HOH A 481 HOH A 555
SITE 1 AC5 6 SER A 95 MET A 96 THR A 121 LEU A 196
SITE 2 AC5 6 HIS A 246 HOH A 409
CRYST1 92.474 92.474 80.256 90.00 90.00 120.00 P 65 6
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 0.010814 0.006243 0.000000 0.00000
SCALE2 0.000000 0.012487 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012460 0.00000
TER 2095 ASP A 270
MASTER 294 0 5 15 7 0 10 6 2416 1 55 22
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