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HEADER HYDROLASE 18-DEC-12 4IH9
TITLE CRYSTAL STRUCTURE OF RICE DWARF14 (D14)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DWARF 88 ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 51-318;
COMPND 5 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN, EXPRESSED,
COMPND 6 OS03G0203200 PROTEIN, CDNA CLONE J023064N24, FULL INSERT SEQUENCE;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 3 ORGANISM_COMMON: JAPANESE RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: D14, D88, LOC_OS03G10620, OS03G0203200;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETDUET1
KEYWDS STRIGOLACTONE RECEPTOR, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,L.-H.ZHAO,Z.-S.WU,W.YI,S.LI,Y.LI,Y.XU,T.-H.XU,Y.LIU,R.-
AUTHOR 2 Z.CHEN,A.KOVACH,Y.KANG,L.HOU,Y.HE,C.ZHANG,K.MELCHER,H.E.XU
REVDAT 1 30-JAN-13 4IH9 0
JRNL AUTH L.-H.ZHAO,X.E.ZHOU,Z.-S.WU,L.WANG,W.YI,S.LI,Y.LI,Y.XU,
JRNL AUTH 2 T.-H.XU,Y.LIU,R.-Z.CHEN,X.YANG,A.KOVACH,Y.KANG,L.HOU,Y.HE,
JRNL AUTH 3 C.XIE,D.ZHONG,L.JIANG,X.LIU,Y.XU,X.SHEN,C.ZHANG,Y.WANG,J.LI,
JRNL AUTH 4 K.MELCHER,H.E.XU
JRNL TITL CRYSTAL STRUCTURES OF TWO PHYTOHORMONE SIGNAL-TRANSDUCING
JRNL TITL 2 ALPHA/BETA HYDROLASES: KARRIKIN-SIGNALING KAI2 AND
JRNL TITL 3 STRIGOLACTONE-SIGNALING DWARF 14
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 75984
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 5487
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5092
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 412
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4100
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 372
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.00000
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): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.338
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4200 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2803 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5719 ; 1.235 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6771 ; 0.847 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 530 ; 4.829 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;28.645 ;22.043
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 653 ;12.009 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;15.360 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 663 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4724 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 922 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2645 ; 0.853 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1075 ; 0.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4255 ; 1.647 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1555 ; 2.498 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1464 ; 4.041 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4IH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-12.
REMARK 100 THE RCSB ID CODE IS RCSB076749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1.00
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76002
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: 4IH1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, MPD, PH 7.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
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 24.09800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.61400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.61400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.09800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.23000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 PRO A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 PRO B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
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 404 O HOH B 404 2.16
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 TYR A 69 43.56 -88.77
REMARK 500 SER A 97 -128.66 67.10
REMARK 500 ARG A 125 123.51 -171.56
REMARK 500 ASN A 151 81.49 -161.17
REMARK 500 ALA A 253 54.34 -140.89
REMARK 500 SER B 97 -126.77 63.26
REMARK 500 ARG B 125 126.49 -172.80
REMARK 500 ASP B 131 48.84 -147.07
REMARK 500 ALA B 253 54.39 -142.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IH1 RELATED DB: PDB
REMARK 900 RELATED ID: 4IH4 RELATED DB: PDB
REMARK 900 RELATED ID: 4IHA RELATED DB: PDB
DBREF 4IH9 A 1 268 UNP Q10QA5 Q10QA5_ORYSJ 51 318
DBREF 4IH9 B 1 268 UNP Q10QA5 Q10QA5_ORYSJ 51 318
SEQRES 1 A 268 PRO SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG
SEQRES 2 A 268 VAL VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS
SEQRES 3 A 268 GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU
SEQRES 4 A 268 PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP
SEQRES 5 A 268 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP
SEQRES 6 A 268 PHE ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP
SEQRES 7 A 268 LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS
SEQRES 8 A 268 ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 A 268 LEU ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU
SEQRES 10 A 268 VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER
SEQRES 11 A 268 ASP TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN
SEQRES 12 A 268 VAL PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA
SEQRES 13 A 268 THR GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 A 268 ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 A 268 ARG PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE
SEQRES 16 A 268 LYS THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA
SEQRES 17 A 268 PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL
SEQRES 18 A 268 PRO ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY
SEQRES 19 A 268 GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS
SEQRES 20 A 268 LEU PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL
SEQRES 21 A 268 LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 B 268 PRO SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG
SEQRES 2 B 268 VAL VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS
SEQRES 3 B 268 GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU
SEQRES 4 B 268 PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP
SEQRES 5 B 268 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP
SEQRES 6 B 268 PHE ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP
SEQRES 7 B 268 LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS
SEQRES 8 B 268 ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 B 268 LEU ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU
SEQRES 10 B 268 VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER
SEQRES 11 B 268 ASP TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN
SEQRES 12 B 268 VAL PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA
SEQRES 13 B 268 THR GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 B 268 ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 B 268 ARG PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE
SEQRES 16 B 268 LYS THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA
SEQRES 17 B 268 PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL
SEQRES 18 B 268 PRO ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY
SEQRES 19 B 268 GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS
SEQRES 20 B 268 LEU PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL
SEQRES 21 B 268 LEU ARG ARG ALA LEU ALA ARG TYR
FORMUL 3 HOH *372(H2 O)
HELIX 1 1 ALA A 4 LEU A 10 1 7
HELIX 2 2 ASP A 31 SER A 36 5 6
HELIX 3 3 VAL A 38 LEU A 42 5 5
HELIX 4 4 ASN A 60 PHE A 64 5 5
HELIX 5 5 LEU A 72 LEU A 86 1 15
HELIX 6 6 SER A 97 ARG A 110 1 14
HELIX 7 7 GLU A 137 ASN A 151 1 15
HELIX 8 8 ASN A 151 GLY A 165 1 15
HELIX 9 9 VAL A 168 PHE A 180 1 13
HELIX 10 10 ARG A 183 LYS A 196 1 14
HELIX 11 11 LEU A 199 VAL A 206 5 8
HELIX 12 12 PRO A 222 LEU A 233 1 12
HELIX 13 13 LEU A 248 ALA A 253 1 6
HELIX 14 14 ALA A 253 LEU A 265 1 13
HELIX 15 15 LYS B 5 LEU B 10 1 6
HELIX 16 16 ASP B 31 SER B 36 5 6
HELIX 17 17 VAL B 38 LEU B 42 5 5
HELIX 18 18 ASN B 60 PHE B 64 5 5
HELIX 19 19 ARG B 67 ASP B 70 5 4
HELIX 20 20 ASN B 71 LEU B 86 1 16
HELIX 21 21 SER B 97 ARG B 110 1 14
HELIX 22 22 GLU B 137 ASN B 151 1 15
HELIX 23 23 ASN B 151 GLY B 165 1 15
HELIX 24 24 VAL B 168 MET B 182 1 15
HELIX 25 25 ARG B 183 LYS B 196 1 14
HELIX 26 26 LEU B 199 VAL B 206 5 8
HELIX 27 27 ALA B 223 LEU B 233 1 11
HELIX 28 28 LEU B 248 ALA B 253 1 6
HELIX 29 29 ALA B 253 LEU B 265 1 13
SHEET 1 A 7 ARG A 13 GLY A 16 0
SHEET 2 A 7 ARG A 47 LEU A 50 -1 O VAL A 48 N VAL A 15
SHEET 3 A 7 VAL A 21 SER A 25 1 N VAL A 22 O VAL A 49
SHEET 4 A 7 CYS A 91 HIS A 96 1 O VAL A 94 N VAL A 23
SHEET 5 A 7 PHE A 114 ILE A 120 1 O ALA A 115 N CYS A 91
SHEET 6 A 7 CYS A 210 GLN A 214 1 O VAL A 211 N LEU A 119
SHEET 7 A 7 THR A 237 PHE A 241 1 O THR A 238 N VAL A 212
SHEET 1 B 7 ARG B 13 GLY B 16 0
SHEET 2 B 7 ARG B 47 TYR B 51 -1 O VAL B 48 N VAL B 15
SHEET 3 B 7 VAL B 21 SER B 25 1 N VAL B 22 O ARG B 47
SHEET 4 B 7 CYS B 91 HIS B 96 1 O VAL B 94 N VAL B 23
SHEET 5 B 7 PHE B 114 ILE B 120 1 O VAL B 118 N PHE B 93
SHEET 6 B 7 CYS B 210 GLN B 214 1 O VAL B 213 N LEU B 119
SHEET 7 B 7 THR B 237 PHE B 241 1 O GLU B 240 N GLN B 214
CRYST1 48.196 88.460 121.228 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 0.020749 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011305 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008249 0.00000
TER 2051 TYR A 268
TER 4102 TYR B 268
MASTER 293 0 0 29 14 0 0 6 4472 2 0 42
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