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HEADER HYDROLASE 12-DEC-21 7WA8
TITLE STRIGOLACTONE RECEPTORS IN STRIGA SHHTL7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HTL7 PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_TAXID: 68872;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RECEPTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WANG,R.YAO
REVDAT 1 05-JAN-22 7WA8 0
JRNL AUTH D.XIE,M.S.SMITH,R.YAO,Y.WANG
JRNL TITL MOLECULAR BASIS FOR HIGH LIGAND SENSITIVITY AND SELECTIVITY
JRNL TITL 2 OF STRIGOLACTONE RECEPTORS IN STRIGA.
JRNL REF PLANT PHYSIOLOGY V. 185 1411 2021
JRNL REFN ISSN 4
JRNL PMID 33793945
JRNL DOI 10.1093/PLPHYS/KIAA048
REMARK 2
REMARK 2 RESOLUTION. 2.33 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) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 23300
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1188
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 46.4000 - 4.6594 1.00 2914 166 0.2087 0.2529
REMARK 3 2 4.6594 - 3.6988 1.00 2824 139 0.1778 0.2261
REMARK 3 3 3.6988 - 3.2314 1.00 2785 136 0.1820 0.2727
REMARK 3 4 3.2314 - 2.9360 1.00 2744 142 0.1921 0.2659
REMARK 3 5 2.9360 - 2.7256 1.00 2760 141 0.2157 0.3029
REMARK 3 6 2.7256 - 2.5649 1.00 2717 159 0.2181 0.2780
REMARK 3 7 2.5649 - 2.4365 1.00 2739 137 0.2165 0.3185
REMARK 3 8 2.4365 - 2.3304 0.98 2629 168 0.2099 0.3359
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.74
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 7WA8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1300026285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23355
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.61100
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: 5Z8P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 4MM CALCIUM CHLORIDE,
REMARK 280 20MM SODIUM ACETATE PH 4.6, 6% (V/V) (+/-)-2-METHYL-2,4-
REMARK 280 PENTANEDIOL, 160MM MAGNESIUM CHLORIDE, 80MM TRIS PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 37.28650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.46150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.16900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.46150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.28650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.16900
REMARK 290 SMTRY3 4 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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASP A 270
REMARK 465 HIS A 271
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 269
REMARK 465 ASP B 270
REMARK 465 HIS B 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 THR A 28 -165.87 -115.33
REMARK 500 SER A 95 -131.91 58.05
REMARK 500 THR A 127 -163.33 -123.62
REMARK 500 ASN B 58 126.96 -38.32
REMARK 500 SER B 95 -122.00 47.81
REMARK 500 LEU B 146 -88.98 -68.47
REMARK 500 ASP B 147 -9.65 -59.84
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7WA8 A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 7WA8 A A0A0M3PNA2 1 271
DBREF1 7WA8 B 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 7WA8 B A0A0M3PNA2 1 271
SEQRES 1 A 271 MET SER SER ILE GLY LEU ALA HIS ASN VAL THR ILE LEU
SEQRES 2 A 271 GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY TYR
SEQRES 3 A 271 GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL PRO TYR
SEQRES 4 A 271 LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP HIS MET
SEQRES 5 A 271 GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE ASP
SEQRES 6 A 271 ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP LEU ILE
SEQRES 7 A 271 ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS ILE TYR
SEQRES 8 A 271 VAL GLY HIS SER MET SER SER MET ALA ALA ALA VAL ALA
SEQRES 9 A 271 SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU VAL MET
SEQRES 10 A 271 ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU GLU TYR
SEQRES 11 A 271 TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU THR LEU
SEQRES 12 A 271 ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER LEU GLY
SEQRES 13 A 271 THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU SER ALA
SEQRES 14 A 271 ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 271 PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE CYS GLY
SEQRES 16 A 271 LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR VAL PRO
SEQRES 17 A 271 CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET VAL PRO
SEQRES 18 A 271 VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU GLY GLY
SEQRES 19 A 271 PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY HIS LEU
SEQRES 20 A 271 PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO VAL VAL
SEQRES 21 A 271 LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
SEQRES 1 B 271 MET SER SER ILE GLY LEU ALA HIS ASN VAL THR ILE LEU
SEQRES 2 B 271 GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY TYR
SEQRES 3 B 271 GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL PRO TYR
SEQRES 4 B 271 LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP HIS MET
SEQRES 5 B 271 GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE ASP
SEQRES 6 B 271 ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP LEU ILE
SEQRES 7 B 271 ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS ILE TYR
SEQRES 8 B 271 VAL GLY HIS SER MET SER SER MET ALA ALA ALA VAL ALA
SEQRES 9 B 271 SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU VAL MET
SEQRES 10 B 271 ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU GLU TYR
SEQRES 11 B 271 TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU THR LEU
SEQRES 12 B 271 ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER LEU GLY
SEQRES 13 B 271 THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU SER ALA
SEQRES 14 B 271 ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN MET ARG
SEQRES 15 B 271 PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE CYS GLY
SEQRES 16 B 271 LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR VAL PRO
SEQRES 17 B 271 CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET VAL PRO
SEQRES 18 B 271 VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU GLY GLY
SEQRES 19 B 271 PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY HIS LEU
SEQRES 20 B 271 PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO VAL VAL
SEQRES 21 B 271 LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
FORMUL 3 HOH *79(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 LEU A 70 GLN A 85 1 16
HELIX 6 AA6 SER A 95 ARG A 108 1 14
HELIX 7 AA7 GLU A 135 SER A 145 1 11
HELIX 8 AA8 ASN A 149 ALA A 163 1 15
HELIX 9 AA9 SER A 168 PHE A 179 1 12
HELIX 10 AB1 ARG A 182 GLY A 195 1 14
HELIX 11 AB2 LEU A 198 VAL A 205 5 8
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 MET A 252 1 6
HELIX 14 AB5 MET A 252 GLN A 266 1 15
HELIX 15 AB6 ILE B 4 HIS B 8 1 5
HELIX 16 AB7 ASP B 29 LYS B 34 5 6
HELIX 17 AB8 LEU B 36 LEU B 40 5 5
HELIX 18 AB9 ASP B 63 SER B 68 1 6
HELIX 19 AC1 LEU B 70 PHE B 84 1 15
HELIX 20 AC2 SER B 95 ARG B 108 1 14
HELIX 21 AC3 GLU B 135 ASN B 149 1 15
HELIX 22 AC4 ASN B 149 ALA B 163 1 15
HELIX 23 AC5 SER B 168 ASN B 180 1 13
HELIX 24 AC6 ARG B 182 GLY B 195 1 14
HELIX 25 AC7 LEU B 198 VAL B 205 5 8
HELIX 26 AC8 PRO B 221 LEU B 232 1 12
HELIX 27 AC9 LEU B 247 MET B 252 1 6
HELIX 28 AD1 MET B 252 GLN B 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 LEU A 47
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 HIS A 113 N CYS A 89
SHEET 6 AA1 7 CYS A 209 ASN A 216 1 O HIS A 210 N LEU A 115
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O MET A 241 N GLN A 213
SHEET 1 AA2 7 THR B 11 GLY B 14 0
SHEET 2 AA2 7 LYS B 45 LEU B 48 -1 O VAL B 46 N LEU B 13
SHEET 3 AA2 7 THR B 19 GLY B 23 1 N VAL B 20 O LYS B 45
SHEET 4 AA2 7 CYS B 89 HIS B 94 1 O VAL B 92 N VAL B 21
SHEET 5 AA2 7 PHE B 112 ILE B 118 1 O VAL B 116 N TYR B 91
SHEET 6 AA2 7 CYS B 209 ASN B 216 1 O ILE B 212 N MET B 117
SHEET 7 AA2 7 SER B 236 GLU B 244 1 O MET B 241 N GLN B 213
CRYST1 74.573 78.338 90.923 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 0.013410 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012765 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010998 0.00000
TER 2081 THR A 269
TER 4161 ILE B 268
MASTER 243 0 0 28 14 0 0 6 4232 2 0 42
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