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HEADER HYDROLASE 25-AUG-25 9WGM
TITLE CRYSTAL STRUCTURE OF THE OCUKAI2D2 PROTEIN FROM OROBANCHE CUMANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KAI2D2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OROBANCHE CERNUA VAR. CUMANA;
SOURCE 3 ORGANISM_TAXID: 78542;
SOURCE 4 GENE: KAI2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS OCKAI2D2, DEHYDROCOSTUS LACTONE, RECEPTOR, ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.F.S.HAMEED,S.T.AROLD
REVDAT 1 20-MAY-26 9WGM 0
JRNL AUTH U.F.SHAHUL HAMEED,M.JAMIL,R.ZARBAN,Y.SAITO,K.ALASHOOR,
JRNL AUTH 2 A.BALAKRISHNA,T.ASAMI,S.T.AROLD,S.AL-BABILI
JRNL TITL OROBANCHE CUMANA KAI2D2 MEDIATES PERCEPTION OF DEHYDROCOSTUS
JRNL TITL 2 LACTONE AND STRIGOLACTONES AND IS INHIBITED BY TRIAZOLE
JRNL TITL 3 UREAS.
JRNL REF PLANT COMMUN. 01889 2026
JRNL REFN ISSN 2590-3462
JRNL PMID 42104616
JRNL DOI 10.1016/J.XPLC.2026.101889
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430 (REFMACAT 0.4.105)
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 18113
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1812
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1395
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.4300
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : 0.4500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2073
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.22000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.252
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.137
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2114 ; 0.007 ; 0.017
REMARK 3 BOND LENGTHS OTHERS (A): 1995 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2866 ; 0.978 ; 1.796
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4583 ; 0.378 ; 1.559
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 275 ; 5.863 ; 5.218
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 345 ;13.132 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 328 ; 0.047 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2453 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 463 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 405 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 102 ; 0.124 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1034 ; 0.166 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 64 ; 0.183 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1070 ; 1.116 ; 4.067
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1070 ; 1.116 ; 4.067
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1327 ; 1.884 ; 7.294
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1328 ; 1.883 ; 7.294
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1044 ; 1.167 ; 4.164
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1044 ; 1.167 ; 4.163
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1539 ; 1.983 ; 7.618
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1540 ; 1.983 ; 7.617
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3390 42.3020 21.2570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1427 T22: 0.1839
REMARK 3 T33: 0.0429 T12: 0.0755
REMARK 3 T13: -0.0188 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 4.2301 L22: 3.1426
REMARK 3 L33: 1.7957 L12: -2.0606
REMARK 3 L13: 1.2025 L23: -0.6538
REMARK 3 S TENSOR
REMARK 3 S11: -0.3829 S12: -0.7736 S13: 0.2650
REMARK 3 S21: 0.3840 S22: 0.4194 S23: -0.1312
REMARK 3 S31: 0.1345 S32: -0.2913 S33: -0.0365
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9WGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-25.
REMARK 100 THE DEPOSITION ID IS D_1300062988.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-18
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19763
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 49.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 20.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.8
REMARK 200 DATA REDUNDANCY IN SHELL : 15.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.850
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M BIS-TRIS PH 6.5, 25% V/V PEG3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 18.95133
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 37.90267
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 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 18.95133
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 37.90267
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 18.95133
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 37.90267
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 18.95133
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.90267
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 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 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 ILE A 29 -138.27 39.72
REMARK 500 ASP A 30 -161.02 -174.92
REMARK 500 SER A 96 -128.01 54.09
REMARK 500 THR A 128 -157.48 -121.47
REMARK 500 ASN A 150 67.40 -152.94
REMARK 500 LEU A 248 60.59 -119.93
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9WGM A 1 269 UNP A0A2U8XPZ9_OROCE
DBREF2 9WGM A A0A2U8XPZ9 1 264
SEQADV 9WGM MET A 14 UNP A0A2U8XPZ INSERTION
SEQADV 9WGM GLY A 15 UNP A0A2U8XPZ INSERTION
SEQADV 9WGM SER A 16 UNP A0A2U8XPZ INSERTION
SEQADV 9WGM GLY A 17 UNP A0A2U8XPZ INSERTION
SEQADV 9WGM GLN A 18 UNP A0A2U8XPZ INSERTION
SEQADV 9WGM GLY A 88 UNP A0A2U8XPZ GLU 83 CONFLICT
SEQADV 9WGM TYR A 151 UNP A0A2U8XPZ HIS 146 CONFLICT
SEQADV 9WGM ALA A 155 UNP A0A2U8XPZ LEU 150 CONFLICT
SEQADV 9WGM MET A 158 UNP A0A2U8XPZ LEU 153 CONFLICT
SEQADV 9WGM VAL A 163 UNP A0A2U8XPZ ILE 158 CONFLICT
SEQADV 9WGM VAL A 206 UNP A0A2U8XPZ LEU 201 CONFLICT
SEQRES 1 A 269 MET GLY SER ILE VAL GLY ALA ALA HIS ASN VAL ARG VAL
SEQRES 2 A 269 MET GLY SER GLY GLN THR THR VAL VAL LEU GLY HIS GLY
SEQRES 3 A 269 LEU GLY ILE ASP GLN SER VAL TRP ARG HIS LEU VAL PRO
SEQRES 4 A 269 ARG LEU VAL ASP HIS TYR LYS VAL VAL LEU TYR ASP ASN
SEQRES 5 A 269 MET GLY ALA GLY THR THR ASN PRO ASP LYS TYR ASP PHE
SEQRES 6 A 269 ASN ARG TYR ALA THR LEU ASN GLY TYR ALA ASP ASP LEU
SEQRES 7 A 269 LEU ALA ILE LEU GLU GLU PHE SER VAL GLY LYS CYS ILE
SEQRES 8 A 269 TYR VAL GLY HIS SER PHE SER ALA MET VAL GLY ALA MET
SEQRES 9 A 269 ALA SER ILE LEU ARG PRO ASP LEU PHE ARG LYS LEU ILE
SEQRES 10 A 269 MET ILE ALA ALA THR PRO ARG MET SER ASN THR GLU ASP
SEQRES 11 A 269 TYR TYR GLY GLY LEU ASN GLN GLU ASP VAL ASP GLN LEU
SEQRES 12 A 269 LEU TYR GLY LEU GLU THR ASN TYR ASN SER MET ALA HIS
SEQRES 13 A 269 GLY MET ALA PRO LEU VAL VAL GLY GLY ASP MET ASP SER
SEQRES 14 A 269 GLU VAL VAL GLN GLU TYR SER ARG THR LEU PHE ASN MET
SEQRES 15 A 269 ARG PRO ASP ILE ALA LEU SER VAL ALA ARG MET ILE ASN
SEQRES 16 A 269 SER TYR ASP MET ARG PRO PHE LEU GLY SER VAL VAL VAL
SEQRES 17 A 269 PRO CYS HIS ILE ILE HIS SER CYS LYS ASP HIS ALA VAL
SEQRES 18 A 269 PRO VAL THR VAL ALA GLU TYR ILE HIS GLU ASN LEU GLY
SEQRES 19 A 269 GLY LYS SER VAL LEU GLU VAL MET SER THR GLU GLY HIS
SEQRES 20 A 269 LEU PRO HIS LEU SER ALA PRO GLU ILE THR ILE PRO VAL
SEQRES 21 A 269 LEU LEU ARG HIS ILE ASN ASN ASP ILE
FORMUL 2 HOH *28(H2 O)
HELIX 1 AA1 SER A 3 HIS A 9 1 7
HELIX 2 AA2 ASP A 30 ARG A 35 5 6
HELIX 3 AA3 LEU A 37 LEU A 41 5 5
HELIX 4 AA4 ASN A 59 TYR A 63 5 5
HELIX 5 AA5 ASN A 66 ALA A 69 5 4
HELIX 6 AA6 THR A 70 SER A 86 1 17
HELIX 7 AA7 SER A 96 ARG A 109 1 14
HELIX 8 AA8 ASN A 136 ASN A 150 1 15
HELIX 9 AA9 ASN A 150 GLY A 164 1 15
HELIX 10 AB1 SER A 169 ASN A 181 1 13
HELIX 11 AB2 ARG A 183 TYR A 197 1 15
HELIX 12 AB3 MET 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 ASN A 267 1 15
SHEET 1 AA1 7 ARG A 12 GLY A 15 0
SHEET 2 AA1 7 LYS A 46 LEU A 49 -1 O VAL A 47 N MET A 14
SHEET 3 AA1 7 THR A 20 GLY A 24 1 N VAL A 21 O LYS A 46
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 TYR A 92
SHEET 6 AA1 7 CYS A 210 LYS A 217 1 O ILE A 213 N MET A 118
SHEET 7 AA1 7 SER A 237 GLU A 245 1 O MET A 242 N HIS A 214
CRYST1 149.799 149.799 56.854 90.00 90.00 120.00 P 64 2 2 12
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 0.006676 0.003854 0.000000 0.00000
SCALE2 0.000000 0.007708 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017589 0.00000
TER 2074 ILE A 269
MASTER 309 0 0 15 7 0 0 6 2101 1 0 21
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