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HEADER PLANT PROTEIN 02-JAN-19 6J2R
TITLE CRYSTAL STRUCTURE OF STRIGA HERMONTHICA HTL8 (SHHTL8)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 8;
COMPND 3 CHAIN: A;
COMPND 4 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 STRIGA HERMONTHICA, HTL8, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHANG,Z.XI
REVDAT 2 27-JAN-21 6J2R 1 JRNL
REVDAT 1 15-JAN-20 6J2R 0
JRNL AUTH Y.ZHANG,D.WANG,Y.SHEN,Z.XI
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL CHARACTERIZATION OF STRIGA
JRNL TITL 2 HERMONTHICA HYPO-SENSITIVE TO LIGHT 8 (SHHTL8) IN
JRNL TITL 3 STRIGOLACTONE SIGNALING PATHWAY.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 523 1040 2020
JRNL REFN ESSN 1090-2104
JRNL PMID 31973817
JRNL DOI 10.1016/J.BBRC.2020.01.056
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 56868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.210
REMARK 3 FREE R VALUE TEST SET COUNT : 2963
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 10.0000 - 3.8560 0.97 2938 143 0.1765 0.1801
REMARK 3 2 3.8560 - 3.0615 1.00 2862 129 0.1594 0.1677
REMARK 3 3 3.0615 - 2.6748 1.00 2806 164 0.1763 0.2104
REMARK 3 4 2.6748 - 2.4304 1.00 2782 155 0.1680 0.1878
REMARK 3 5 2.4304 - 2.2562 1.00 2798 151 0.1610 0.1884
REMARK 3 6 2.2562 - 2.1232 1.00 2789 151 0.1611 0.1679
REMARK 3 7 2.1232 - 2.0169 1.00 2749 159 0.1605 0.1907
REMARK 3 8 2.0169 - 1.9292 1.00 2764 162 0.1587 0.1679
REMARK 3 9 1.9292 - 1.8549 1.00 2721 165 0.1623 0.1644
REMARK 3 10 1.8549 - 1.7909 1.00 2766 160 0.1706 0.1895
REMARK 3 11 1.7909 - 1.7349 1.00 2749 151 0.1687 0.1687
REMARK 3 12 1.7349 - 1.6853 1.00 2695 169 0.1714 0.1988
REMARK 3 13 1.6853 - 1.6410 1.00 2781 135 0.1711 0.1939
REMARK 3 14 1.6410 - 1.6009 1.00 2721 155 0.1744 0.1783
REMARK 3 15 1.6009 - 1.5645 0.99 2731 157 0.1811 0.1938
REMARK 3 16 1.5645 - 1.5312 0.97 2668 153 0.1922 0.2074
REMARK 3 17 1.5312 - 1.5006 0.93 2517 130 0.1986 0.2152
REMARK 3 18 1.5006 - 1.4723 0.85 2345 129 0.2157 0.2215
REMARK 3 19 1.4723 - 1.4460 0.73 1982 112 0.2234 0.2259
REMARK 3 20 1.4460 - 1.4215 0.57 1584 77 0.2389 0.2672
REMARK 3 21 1.4215 - 1.4000 0.42 1157 56 0.2473 0.3511
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.23
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 : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2178 -3.4967 -0.8207
REMARK 3 T TENSOR
REMARK 3 T11: 0.1047 T22: 0.1305
REMARK 3 T33: 0.0662 T12: 0.0020
REMARK 3 T13: -0.0018 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.6702 L22: 0.4457
REMARK 3 L33: 1.9543 L12: -0.0507
REMARK 3 L13: -0.0856 L23: -0.0527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: -0.0315 S13: -0.0059
REMARK 3 S21: 0.0341 S22: 0.0310 S23: -0.0177
REMARK 3 S31: 0.0108 S32: 0.0145 S33: -0.0245
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SF FILE CONTAINS FRIEDEL PAIRS UNDER
REMARK 3 I/F_MINUS AND I/F_PLUS COLUMNS.
REMARK 4
REMARK 4 6J2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NFPSS
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97890
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58744
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.399
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 (%) : 95.4
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
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: 6A9D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FORMATE, 20% (W/V) PEG
REMARK 280 3500 AND 0.1 M ADA PH 6.6, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 303K
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 21.81400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.03850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.74150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.03850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.81400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.74150
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 MET A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 270
REMARK 465 ASP A 271
REMARK 465 GLN A 272
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 OE1 GLU A 136 O HOH A 501 2.07
REMARK 500 O HOH A 726 O HOH A 745 2.10
REMARK 500 NZ LYS A 138 O HOH A 502 2.13
REMARK 500 O HOH A 647 O HOH A 689 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 46 O HOH A 628 2554 1.99
REMARK 500 OE2 GLU A 66 O HOH A 689 1655 2.08
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 16 144.42 -173.38
REMARK 500 SER A 96 -117.49 48.87
REMARK 500 ARG A 124 113.97 -168.04
REMARK 500 ASN A 217 99.14 -164.58
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 GOL A 401
DBREF1 6J2R A 1 272 UNP A0A0M4APJ4_STRHE
DBREF2 6J2R A A0A0M4APJ4 1 272
SEQRES 1 A 272 MET ASN ASN SER VAL GLY SER THR HIS ASN VAL THR ILE
SEQRES 2 A 272 LEU GLY SER GLY GLU THR THR VAL VAL LEU SER HIS GLY
SEQRES 3 A 272 TYR GLY THR ASP GLN SER VAL TRP LYS LEU PHE VAL PRO
SEQRES 4 A 272 HIS LEU VAL ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN
SEQRES 5 A 272 MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE
SEQRES 6 A 272 GLU ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP LEU
SEQRES 7 A 272 ILE ALA ILE LEU ASP GLU PHE HIS VAL SER LYS CYS ILE
SEQRES 8 A 272 PHE VAL GLY HIS SER MET SER ALA MET ALA ALA ALA VAL
SEQRES 9 A 272 ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU ILE
SEQRES 10 A 272 MET ILE SER PRO SER PRO ARG LEU ALA ASN ALA GLU ASP
SEQRES 11 A 272 TYR TYR GLY GLY LEU GLU GLN LYS GLU ILE ASP GLU VAL
SEQRES 12 A 272 VAL GLY SER MET GLU GLU ASN TYR ARG SER MET ALA LEU
SEQRES 13 A 272 GLY SER ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU SER
SEQRES 14 A 272 ALA ALA VAL GLN GLU TYR CYS ARG THR LEU PHE ASN MET
SEQRES 15 A 272 ARG PRO ASP ILE SER CYS CYS MET ALA ARG MET ILE PHE
SEQRES 16 A 272 GLY LEU ASP LEU ARG PRO TYR LEU CYS HIS VAL THR VAL
SEQRES 17 A 272 PRO CYS HIS ILE LEU GLN SER SER ASN ASP VAL MET VAL
SEQRES 18 A 272 PRO VAL ALA VAL VAL GLU TYR LEU SER 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 ALA PRO GLU VAL THR ILE PRO VAL
SEQRES 21 A 272 VAL LEU ARG HIS ILE ARG HIS ASP ILE ALA ASP GLN
HET GOL A 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *267(H2 O)
HELIX 1 AA1 SER A 4 HIS A 9 1 6
HELIX 2 AA2 ASP A 30 LYS A 35 5 6
HELIX 3 AA3 PHE A 37 LEU A 41 5 5
HELIX 4 AA4 ASN A 59 PHE A 63 5 5
HELIX 5 AA5 GLU A 66 SER A 69 5 4
HELIX 6 AA6 SER A 70 PHE A 85 1 16
HELIX 7 AA7 SER A 96 ARG A 109 1 14
HELIX 8 AA8 GLU A 136 ASN A 150 1 15
HELIX 9 AA9 ASN A 150 ALA A 164 1 15
HELIX 10 AB1 SER A 169 ASN A 181 1 13
HELIX 11 AB2 ARG A 183 LEU A 197 1 15
HELIX 12 AB3 LEU A 199 VAL A 206 5 8
HELIX 13 AB4 PRO A 222 LEU A 233 1 12
HELIX 14 AB5 LEU A 248 ALA A 253 1 6
HELIX 15 AB6 ALA A 253 HIS A 267 1 15
SHEET 1 AA1 7 THR A 12 GLY A 15 0
SHEET 2 AA1 7 ARG A 46 TYR A 50 -1 O VAL A 47 N LEU A 14
SHEET 3 AA1 7 THR A 20 SER A 24 1 N VAL A 21 O LEU A 48
SHEET 4 AA1 7 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 22
SHEET 5 AA1 7 PHE A 113 ILE A 119 1 O ILE A 117 N PHE A 92
SHEET 6 AA1 7 CYS A 210 SER A 215 1 O HIS A 211 N LEU A 116
SHEET 7 AA1 7 SER A 237 MET A 242 1 O VAL A 238 N ILE A 212
SITE 1 AC1 6 PHE A 85 TYR A 131 TYR A 132 ALA A 224
SITE 2 AC1 6 TYR A 228 HOH A 630
CRYST1 43.628 83.483 84.077 90.00 90.00 90.00 P 21 21 21 4
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 0.022921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011978 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011894 0.00000
TER 2156 ILE A 269
MASTER 300 0 1 15 7 0 2 6 2342 1 6 21
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