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HEADER HYDROLASE 30-JAN-18 5Z7X
TITLE CRYSTAL STRUCTURE OF STRIGA HERMONTHICA HTL4 (SHHTL4)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE ACTIVITY, PUTATIVE RECEPTOR OF STRIGOLACTONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA
REVDAT 1 29-AUG-18 5Z7X 0
JRNL AUTH Y.XU,T.MIYAKAWA,S.NOSAKI,A.NAKAMURA,Y.LYU,H.NAKAMURA,U.OHTO,
JRNL AUTH 2 H.ISHIDA,T.SHIMIZU,T.ASAMI,M.TANOKURA
JRNL TITL COMPREHENSIVE STRUCTURAL STUDIES REVEAL EVOLUTION OF
JRNL TITL 2 STRIGOLACTONE/KARRIKIN SELECTIVITY OF HTL AND D14 PROTEINS
JRNL TITL 3 IN STRIGA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.280
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 29369
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1454
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 38.9870 - 4.4261 1.00 2829 138 0.1615 0.1669
REMARK 3 2 4.4261 - 3.5138 1.00 2844 134 0.1505 0.1925
REMARK 3 3 3.5138 - 3.0699 1.00 2820 147 0.1706 0.2082
REMARK 3 4 3.0699 - 2.7893 1.00 2764 172 0.2014 0.2564
REMARK 3 5 2.7893 - 2.5894 1.00 2847 166 0.2258 0.3046
REMARK 3 6 2.5894 - 2.4368 1.00 2814 148 0.2235 0.2827
REMARK 3 7 2.4368 - 2.3147 1.00 2816 124 0.2277 0.2805
REMARK 3 8 2.3147 - 2.2140 1.00 2829 144 0.2422 0.2694
REMARK 3 9 2.2140 - 2.1288 1.00 2785 158 0.2663 0.3255
REMARK 3 10 2.1288 - 2.0553 0.90 2567 123 0.2979 0.3566
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 2139
REMARK 3 ANGLE : 0.549 2903
REMARK 3 CHIRALITY : 0.044 335
REMARK 3 PLANARITY : 0.004 373
REMARK 3 DIHEDRAL : 11.168 1280
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 5Z7X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006458.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29377
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.055
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
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: 5CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 90MM TRIS-HCL (PH 9.0), 27% (W/V) PEG
REMARK 280 4000, 180MM MGCL2, 1MM GSH, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.50000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.50000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.90000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.98000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.90000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.98000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.50000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.90000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 38.98000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.50000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.90000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 38.98000
REMARK 290 SMTRY3 8 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: 110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 499 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 540 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 542 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 562 LIES ON A SPECIAL POSITION.
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 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 -115.98 53.36
REMARK 500 ARG A 123 126.82 -171.00
REMARK 500 GLU A 148 -71.39 -60.07
REMARK 500 PRO A 242 80.43 -69.48
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 586 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A 587 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 588 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH A 589 DISTANCE = 6.76 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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
DBREF1 5Z7X A 1 269 UNP A0A0M4AMQ0_STRHE
DBREF2 5Z7X A A0A0M4AMQ0 1 269
SEQADV 5Z7X GLY A -4 UNP A0A0M4AMQ EXPRESSION TAG
SEQADV 5Z7X PRO A -3 UNP A0A0M4AMQ EXPRESSION TAG
SEQADV 5Z7X LEU A -2 UNP A0A0M4AMQ EXPRESSION TAG
SEQADV 5Z7X GLY A -1 UNP A0A0M4AMQ EXPRESSION TAG
SEQADV 5Z7X SER A 0 UNP A0A0M4AMQ EXPRESSION TAG
SEQRES 1 A 274 GLY PRO LEU GLY SER MET SER THR VAL GLY SER ALA HIS
SEQRES 2 A 274 ASN VAL ARG VAL LEU GLY SER GLY GLU THR THR VAL VAL
SEQRES 3 A 274 LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS
SEQRES 4 A 274 GLN LEU VAL PRO TYR LEU THR ASP GLU TYR ARG VAL LEU
SEQRES 5 A 274 LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN PRO ASP
SEQRES 6 A 274 CYS TYR ASP PHE GLU ARG TYR SER SER LEU GLU GLY HIS
SEQRES 7 A 274 SER ASN ASP LEU ILE ALA ILE LEU ASP ASP PHE HIS VAL
SEQRES 8 A 274 THR LYS CYS ILE TYR VAL GLY HIS SER LEU SER SER MET
SEQRES 9 A 274 ALA ALA ALA VAL SER SER ILE PHE ARG PRO ASP LEU PHE
SEQRES 10 A 274 ARG LYS VAL VAL MET ILE SER ALA THR PRO ARG ILE THR
SEQRES 11 A 274 ASN THR GLU ASP TYR TYR GLY GLY PHE GLU GLN GLU GLU
SEQRES 12 A 274 ILE ASN GLN MET ASN THR ALA MET GLU GLU ASN PHE LYS
SEQRES 13 A 274 THR MET MET MET GLY PHE ALA PRO ILE VAL VAL GLY GLY
SEQRES 14 A 274 ASP LEU GLU SER ASP ALA ILE GLN GLU PHE SER ARG THR
SEQRES 15 A 274 LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER ILE CYS
SEQRES 16 A 274 ARG MET ILE SER GLY LEU ASP LEU ARG PRO TYR LEU GLY
SEQRES 17 A 274 LEU ILE VAL VAL PRO CYS HIS ILE ILE GLN SER SER LYS
SEQRES 18 A 274 ASP MET LEU VAL PRO VAL ALA VAL ALA GLU TYR LEU HIS
SEQRES 19 A 274 LYS ASN LEU GLY GLY LYS SER VAL VAL GLU LEU ILE PRO
SEQRES 20 A 274 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO GLU LEU
SEQRES 21 A 274 THR ILE PRO VAL LEU VAL ARG HIS ILE LYS HIS ASP ILE
SEQRES 22 A 274 ALA
HET EDO A 301 4
HET MG A 302 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO C2 H6 O2
FORMUL 3 MG MG 2+
FORMUL 4 HOH *189(H2 O)
HELIX 1 AA1 SER A 2 HIS A 8 1 7
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 TYR A 62 5 5
HELIX 5 AA5 GLU 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 ASN A 149 1 15
HELIX 9 AA9 ASN A 149 GLY A 163 1 15
HELIX 10 AB1 SER A 168 ASN A 180 1 13
HELIX 11 AB2 ARG A 182 LEU A 196 1 15
HELIX 12 AB3 LEU A 198 ILE A 205 5 8
HELIX 13 AB4 PRO A 221 LEU A 232 1 12
HELIX 14 AB5 LEU A 247 ALA A 252 1 6
HELIX 15 AB6 ALA A 252 HIS A 266 1 15
SHEET 1 AA1 7 ARG A 11 GLY A 14 0
SHEET 2 AA1 7 ARG A 45 LEU A 48 -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 ARG 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 LYS A 216 1 O ILE A 212 N MET A 117
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O VAL A 237 N ILE A 211
SITE 1 AC1 3 SER A 95 LEU A 219 HIS A 246
SITE 1 AC2 4 SER A 95 LEU A 96 MET A 99 THR A 121
CRYST1 63.800 77.960 99.000 90.00 90.00 90.00 C 2 2 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 0.015674 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010101 0.00000
TER 2092 ALA A 269
MASTER 286 0 2 15 7 0 2 6 2285 1 4 22
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