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HEADER HYDROLASE 18-SEP-12 3VXK
TITLE CRYSTAL STRUCTURE OF OSD14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DWARF 88 ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 54-318;
COMPND 5 SYNONYM: ALPHA/BETA HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN,
COMPND 6 EXPRESSED, OS03G0203200 PROTEIN, CDNA CLONE J023064N24, FULL INSERT
COMPND 7 SEQUENCE;
COMPND 8 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: D88, OS03G0203200, LOC_OS03G10620;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA/BETA-HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-L.XUE,T.MIYAKAWA,F.HOU,H.-M.QIN,M.TANOKURA
REVDAT 3 30-APR-14 3VXK 1 JRNL
REVDAT 2 23-OCT-13 3VXK 1 JRNL
REVDAT 1 25-SEP-13 3VXK 0
JRNL AUTH H.NAKAMURA,Y.-L.XUE,T.MIYAKAWA,F.HOU,H.-M.QIN,K.FUKUI,X.SHI,
JRNL AUTH 2 E.ITO,S.ITO,S.-H.PARK,Y.MIYAUCHI,A.ASANO,N.TOTSUKA,T.UEDA,
JRNL AUTH 3 M.TANOKURA,T.ASAMI
JRNL TITL MOLECULAR MECHANISM OF STRIGOLACTONE PERCEPTION BY DWARF14
JRNL REF NAT COMMUN V. 4 2613 2013
JRNL REFN ESSN 2041-1723
JRNL PMID 24131983
JRNL DOI 10.1038/NCOMMS3613
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 49279
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2643
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3559
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 195
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : 0.13000
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): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.172
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4164 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5674 ; 1.933 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 524 ; 6.179 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;26.181 ;22.043
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 644 ;14.573 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;20.503 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 658 ; 0.153 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3190 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2618 ; 1.298 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4216 ; 2.165 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1546 ; 3.540 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1458 ; 5.485 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 3VXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB095625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51922
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 FOR THE DATA SET : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33700
REMARK 200 FOR SHELL : 6.500
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: 1WOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 20000, 2% 1,4-DIOXANE, 0.1M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 24.07000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.30500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.30500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.07000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.36000
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 GLY A 45
REMARK 465 PRO A 46
REMARK 465 GLY A 47
REMARK 465 TYR A 48
REMARK 465 GLN A 49
REMARK 465 ASP A 50
REMARK 465 PRO A 51
REMARK 465 ASN A 52
REMARK 465 SER A 53
REMARK 465 ALA A 54
REMARK 465 LYS A 55
REMARK 465 GLY B 45
REMARK 465 PRO B 46
REMARK 465 GLY B 47
REMARK 465 TYR B 48
REMARK 465 GLN B 49
REMARK 465 ASP B 50
REMARK 465 PRO B 51
REMARK 465 ASN B 52
REMARK 465 SER B 53
REMARK 465 ALA B 54
REMARK 465 LYS B 55
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 147 -127.36 69.62
REMARK 500 ARG A 175 120.19 -174.95
REMARK 500 ASP A 181 42.88 34.05
REMARK 500 ASN A 201 82.15 -158.29
REMARK 500 ALA A 303 59.08 -144.71
REMARK 500 ASP B 81 -163.11 -116.92
REMARK 500 SER B 147 -126.74 65.52
REMARK 500 ARG B 175 126.59 -170.69
REMARK 500 ASP B 181 -23.47 78.71
REMARK 500 ASN B 201 85.57 -155.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3VXK A 54 318 UNP Q10QA5 Q10QA5_ORYSJ 54 318
DBREF 3VXK B 54 318 UNP Q10QA5 Q10QA5_ORYSJ 54 318
SEQADV 3VXK GLY A 45 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK PRO A 46 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK GLY A 47 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK TYR A 48 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK GLN A 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK ASP A 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK PRO A 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK ASN A 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK SER A 53 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK GLY B 45 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK PRO B 46 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK GLY B 47 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK TYR B 48 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK GLN B 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK ASP B 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK PRO B 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK ASN B 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 3VXK SER B 53 UNP Q10QA5 EXPRESSION TAG
SEQRES 1 A 274 GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES 2 A 274 GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES 3 A 274 VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES 4 A 274 ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES 5 A 274 ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES 6 A 274 ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES 7 A 274 ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES 8 A 274 LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES 9 A 274 SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES 10 A 274 ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES 11 A 274 ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES 12 A 274 LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES 13 A 274 ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES 14 A 274 VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES 15 A 274 ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES 16 A 274 VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES 17 A 274 LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES 18 A 274 THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES 19 A 274 LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES 20 A 274 LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES 21 A 274 SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES 22 A 274 TYR
SEQRES 1 B 274 GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES 2 B 274 GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES 3 B 274 VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES 4 B 274 ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES 5 B 274 ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES 6 B 274 ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES 7 B 274 ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES 8 B 274 LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES 9 B 274 SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES 10 B 274 ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES 11 B 274 ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES 12 B 274 LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES 13 B 274 ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES 14 B 274 VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES 15 B 274 ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES 16 B 274 VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES 17 B 274 LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES 18 B 274 THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES 19 B 274 LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES 20 B 274 LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES 21 B 274 SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES 22 B 274 TYR
FORMUL 3 HOH *340(H2 O)
HELIX 1 1 ASP A 81 SER A 86 5 6
HELIX 2 2 VAL A 88 LEU A 92 5 5
HELIX 3 3 ASN A 110 PHE A 114 5 5
HELIX 4 4 ARG A 117 ASP A 120 5 4
HELIX 5 5 ASN A 121 LEU A 136 1 16
HELIX 6 6 SER A 147 ARG A 160 1 14
HELIX 7 7 GLU A 187 ASN A 201 1 15
HELIX 8 8 ASN A 201 GLY A 215 1 15
HELIX 9 9 VAL A 218 ASN A 231 1 14
HELIX 10 10 ARG A 233 LYS A 246 1 14
HELIX 11 11 LEU A 249 VAL A 256 5 8
HELIX 12 12 SER A 274 LEU A 283 1 10
HELIX 13 13 LEU A 298 ALA A 303 1 6
HELIX 14 14 ALA A 303 LEU A 315 1 13
HELIX 15 15 ASP B 81 SER B 86 5 6
HELIX 16 16 VAL B 88 LEU B 92 5 5
HELIX 17 17 ASN B 110 PHE B 114 5 5
HELIX 18 18 ARG B 117 ASP B 120 5 4
HELIX 19 19 ASN B 121 LEU B 136 1 16
HELIX 20 20 SER B 147 ARG B 160 1 14
HELIX 21 21 GLU B 187 ASN B 201 1 15
HELIX 22 22 ASN B 201 GLY B 215 1 15
HELIX 23 23 VAL B 218 MET B 232 1 15
HELIX 24 24 ARG B 233 LYS B 246 1 14
HELIX 25 25 LEU B 249 VAL B 256 5 8
HELIX 26 26 SER B 274 LEU B 283 1 10
HELIX 27 27 LEU B 298 ALA B 303 1 6
HELIX 28 28 ALA B 303 LEU B 315 1 13
SHEET 1 A 7 ARG A 63 GLY A 66 0
SHEET 2 A 7 ARG A 97 LEU A 100 -1 O VAL A 98 N VAL A 65
SHEET 3 A 7 VAL A 71 SER A 75 1 N VAL A 72 O VAL A 99
SHEET 4 A 7 CYS A 141 HIS A 146 1 O VAL A 144 N VAL A 73
SHEET 5 A 7 PHE A 164 ILE A 170 1 O ALA A 165 N CYS A 141
SHEET 6 A 7 CYS A 260 GLN A 264 1 O VAL A 263 N LEU A 169
SHEET 7 A 7 THR A 287 PHE A 291 1 O GLU A 290 N GLN A 264
SHEET 1 B 7 ARG B 63 GLY B 66 0
SHEET 2 B 7 ARG B 97 LEU B 100 -1 O VAL B 98 N VAL B 65
SHEET 3 B 7 VAL B 71 SER B 75 1 N VAL B 72 O ARG B 97
SHEET 4 B 7 CYS B 141 HIS B 146 1 O VAL B 144 N VAL B 73
SHEET 5 B 7 PHE B 164 ILE B 170 1 O VAL B 168 N GLY B 145
SHEET 6 B 7 CYS B 260 GLN B 264 1 O VAL B 261 N LEU B 169
SHEET 7 B 7 THR B 287 PHE B 291 1 O GLU B 290 N GLN B 264
CRYST1 48.140 88.720 118.610 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 0.020773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008431 0.00000
TER 2038 TYR A 318
TER 4076 TYR B 318
MASTER 300 0 0 28 14 0 0 6 4414 2 0 44
END |