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HEADER HYDROLASE 28-OCT-21 7SNU
TITLE CRYSTAL STRUCTURE OF SHHTL7 FROM STRIGA HERMONTHICA IN COMPLEX WITH
TITLE 2 STRIGOLACTONE ANTAGONIST RG6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_COMMON: PURPLE WITCHWEED, BUCHNERA HERMONTHICA;
SOURCE 4 ORGANISM_TAXID: 68872;
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: PMCSG53
KEYWDS PARASITE, STRIGOLACTONE, RECEPTOR, ANTAGONIST, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ARELLANO-SAAB,P.J.STOGIOS,T.SKARINA,V.YIM,A.SAVCHENKO,P.MCCOURT
REVDAT 1 06-JUL-22 7SNU 0
JRNL AUTH A.ARELLANO-SAAB,C.S.P.MCERLEAN,S.LUMBA,A.SAVCHENKO,
JRNL AUTH 2 P.J.STOGIOS,P.MCCOURT
JRNL TITL A NOVEL STRIGOLACTONE RECEPTOR ANTAGONIST PROVIDES INSIGHTS
JRNL TITL 2 INTO THE STRUCTURAL INHIBITION, CONDITIONING, AND
JRNL TITL 3 GERMINATION OF THE CROP PARASITE STRIGA.
JRNL REF J.BIOL.CHEM. V. 298 01734 2022
JRNL REFN ESSN 1083-351X
JRNL PMID 35181340
JRNL DOI 10.1016/J.JBC.2022.101734
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1_4122
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) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 59235
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.129
REMARK 3 R VALUE (WORKING SET) : 0.128
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.260
REMARK 3 FREE R VALUE TEST SET COUNT : 1930
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 28.6800 - 3.5200 1.00 4474 156 0.1223 0.1574
REMARK 3 2 3.5200 - 2.7900 1.00 4398 149 0.1298 0.1451
REMARK 3 3 2.7900 - 2.4400 1.00 4373 147 0.1369 0.1868
REMARK 3 4 2.4400 - 2.2200 1.00 4385 144 0.1247 0.1523
REMARK 3 5 2.2200 - 2.0600 1.00 4359 143 0.1239 0.1579
REMARK 3 6 2.0600 - 1.9400 1.00 4381 145 0.1192 0.1665
REMARK 3 7 1.9400 - 1.8400 0.99 4334 150 0.1270 0.1580
REMARK 3 8 1.8400 - 1.7600 0.99 4323 147 0.1212 0.1376
REMARK 3 9 1.7600 - 1.6900 0.98 4273 140 0.1301 0.1681
REMARK 3 10 1.6900 - 1.6300 0.96 4235 142 0.1251 0.1627
REMARK 3 11 1.6300 - 1.5800 0.94 4038 135 0.1277 0.1706
REMARK 3 12 1.5800 - 1.5400 0.89 3918 134 0.1373 0.1983
REMARK 3 13 1.5400 - 1.5000 0.75 3246 110 0.1488 0.1768
REMARK 3 14 1.5000 - 1.4600 0.59 2568 88 0.1630 0.2318
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) : 0.116
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.09
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 2277
REMARK 3 ANGLE : 1.012 3100
REMARK 3 CHIRALITY : 0.094 348
REMARK 3 PLANARITY : 0.008 397
REMARK 3 DIHEDRAL : 5.921 327
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 7SNU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1000260749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97913
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 1.11
REMARK 200 DATA SCALING SOFTWARE : HKL-3000 1.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62389
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.19.1_4122
REMARK 200 STARTING MODEL: PDB ENTRY 5CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M SODIUM ACETATE, 0.1 M IMIDAZOLE PH
REMARK 280 7.0, 5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, 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 46.23867
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 23.11933
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 34.67900
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 11.55967
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 57.79833
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 ASP A 270
REMARK 465 HIS A 271
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 405 O HOH A 600 2.13
REMARK 500 OG SER A 69 O HOH A 401 2.18
REMARK 500 O1 GOL A 302 O HOH A 402 2.19
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 95 -93.75 27.24
REMARK 500 ARG A 123 129.61 -174.88
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 873 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A 874 DISTANCE = 6.34 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 308 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 231 OD1
REMARK 620 2 HOH A 558 O 94.0
REMARK 620 3 HOH A 583 O 87.4 92.2
REMARK 620 4 HOH A 689 O 82.5 86.9 169.8
REMARK 620 5 HOH A 715 O 82.8 174.7 91.9 88.5
REMARK 620 6 HOH A 824 O 170.8 94.2 96.5 93.7 88.7
REMARK 620 N 1 2 3 4 5
DBREF1 7SNU A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 7SNU A A0A0M3PNA2 1 271
SEQADV 7SNU GLY A 0 UNP A0A0M3PNA EXPRESSION TAG
SEQRES 1 A 272 GLY MET SER SER ILE GLY LEU ALA HIS ASN VAL THR ILE
SEQRES 2 A 272 LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY
SEQRES 3 A 272 TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL PRO
SEQRES 4 A 272 TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP HIS
SEQRES 5 A 272 MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE
SEQRES 6 A 272 ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP LEU
SEQRES 7 A 272 ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS ILE
SEQRES 8 A 272 TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA VAL
SEQRES 9 A 272 ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU VAL
SEQRES 10 A 272 MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU GLU
SEQRES 11 A 272 TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU THR
SEQRES 12 A 272 LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER LEU
SEQRES 13 A 272 GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU SER
SEQRES 14 A 272 ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN MET
SEQRES 15 A 272 ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE CYS
SEQRES 16 A 272 GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR VAL
SEQRES 17 A 272 PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET VAL
SEQRES 18 A 272 PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU GLY
SEQRES 19 A 272 GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY HIS
SEQRES 20 A 272 LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO VAL
SEQRES 21 A 272 VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
HET GOL A 301 6
HET GOL A 302 6
HET ACT A 303 4
HET ACT A 304 4
HET ACT A 305 4
HET ACT A 306 4
HET ACT A 307 4
HET MG A 308 1
HET IMD A 309 5
HET HFJ A 310 30
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM MG MAGNESIUM ION
HETNAM IMD IMIDAZOLE
HETNAM HFJ 2-{(2S)-1-[(4-ETHOXYPHENYL)METHYL]-4-[(2E)-3-(4-
HETNAM 2 HFJ METHOXYPHENYL)PROP-2-EN-1-YL]PIPERAZIN-2-YL}ETHAN-1-OL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN HFJ RG6
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 ACT 5(C2 H3 O2 1-)
FORMUL 9 MG MG 2+
FORMUL 10 IMD C3 H5 N2 1+
FORMUL 11 HFJ C25 H34 N2 O3
FORMUL 12 HOH *474(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 68 5 4
HELIX 6 AA6 SER A 69 PHE A 84 1 16
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 GLY A 195 1 14
HELIX 12 AB3 LEU A 198 VAL A 205 5 8
HELIX 13 AB4 PRO A 221 LEU A 232 1 12
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 OD1 ASN A 231 MG MG A 308 1555 1555 2.35
LINK MG MG A 308 O HOH A 558 1555 1555 2.42
LINK MG MG A 308 O HOH A 583 1555 1555 2.52
LINK MG MG A 308 O HOH A 689 1555 1555 2.55
LINK MG MG A 308 O HOH A 715 1555 1555 2.77
LINK MG MG A 308 O HOH A 824 1555 1555 2.41
CRYST1 96.216 96.216 69.358 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 0.010393 0.006001 0.000000 0.00000
SCALE2 0.000000 0.012001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014418 0.00000
TER 2157 THR A 269
MASTER 277 0 10 15 7 0 0 6 2640 1 75 21
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