HEADER PROTEIN BINDING 15-MAR-12 3VPY
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS DDL FHA DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FHA DOMAIN-CONTAINING PROTEIN DDL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DDL FHA DOMAIN, UNP RESIDUES 181-310;
COMPND 5 SYNONYM: PROTEIN DAWDLE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: DDL, AT3G20550, K10D20.9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FHA DOMAIN, DCL1 PT RECOGNITION, ARABIDOPSIS DCL1, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.A.YUAN,S.MACHIDA
REVDAT 1 06-FEB-13 3VPY 0
JRNL AUTH S.MACHIDA,A.Y.YUAN
JRNL TITL CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DAWDLE
JRNL TITL 2 FORKHEAD-ASSOCIATED DOMAIN REVEALS A CONSERVED
JRNL TITL 3 PHOSPHO-THREONINE RECOGNITION CLEFT FOR DICER-LIKE1 BINDING.
JRNL REF MOL PLANT 2013
JRNL REFN ESSN 1752-9867
JRNL PMID 23313986
JRNL DOI 10.1093/MP/SST007
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 13269
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1487
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 937
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1162
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : 0.21000
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): 0.133
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.100
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1191 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1609 ; 1.285 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 144 ; 6.472 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 59 ;35.727 ;23.559
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 206 ;13.579 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;14.691 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 165 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 927 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 465 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 806 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 101 ; 0.109 ; 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): 49 ; 0.180 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.155 ; 0.200
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): 747 ; 0.850 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1169 ; 1.369 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 499 ; 2.562 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 440 ; 4.016 ; 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 : 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 141
REMARK 3 ORIGIN FOR THE GROUP (A): 46.5174 30.7025 0.6246
REMARK 3 T TENSOR
REMARK 3 T11: -0.1133 T22: -0.0987
REMARK 3 T33: -0.0991 T12: 0.0003
REMARK 3 T13: 0.0075 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.8928 L22: 1.5935
REMARK 3 L33: 1.2847 L12: 0.0838
REMARK 3 L13: 0.1633 L23: -0.6027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: 0.1233 S13: 0.0002
REMARK 3 S21: -0.1012 S22: 0.0073 S23: 0.0266
REMARK 3 S31: 0.0306 S32: 0.0598 S33: -0.0376
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3VPY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB095354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 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 : 13269
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 36.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.52100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, HEPES, AS, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING 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 24.28200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.34400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.35450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 27.34400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.28200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.35450
REMARK 290 SMTRY3 4 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 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 1 OG1 CG2
REMARK 470 ASN A 132 CG OD1 ND2
REMARK 470 SER A 133 OG
REMARK 470 GLU A 135 CG CD OE1 OE2
REMARK 470 LEU A 136 CG CD1 CD2
REMARK 470 GLU A 137 CG CD OE1 OE2
REMARK 470 HIS A 138 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 139 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 140 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 141 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 142 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 143 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 144 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 145 CG ND1 CD2 CE1 NE2
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 HIS A 35 14.21 -141.86
REMARK 500 LEU A 90 33.75 -98.42
REMARK 500 LYS A 95 166.52 80.67
REMARK 500 LYS A 114 -2.11 82.97
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3VPY A 1 131 UNP Q8W4D8 DDL_ARATH 180 310
SEQADV 3VPY ASN A 132 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY SER A 133 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY ALA A 134 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY GLU A 135 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY LEU A 136 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY GLU A 137 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 138 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 139 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 140 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 141 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 142 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 143 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 144 UNP Q8W4D8 EXPRESSION TAG
SEQADV 3VPY HIS A 145 UNP Q8W4D8 EXPRESSION TAG
SEQRES 1 A 145 THR LEU LEU PHE ASN GLU PRO PRO GLU ALA ARG LYS PRO
SEQRES 2 A 145 SER GLU ARG TRP ARG LEU TYR VAL PHE LYS ASP GLY GLU
SEQRES 3 A 145 PRO LEU ASN GLU PRO LEU CYS LEU HIS ARG GLN SER CYS
SEQRES 4 A 145 TYR LEU PHE GLY ARG GLU ARG ARG ILE ALA ASP ILE PRO
SEQRES 5 A 145 THR ASP HIS PRO SER CYS SER LYS GLN HIS ALA VAL ILE
SEQRES 6 A 145 GLN TYR ARG GLU MSE GLU LYS GLU LYS PRO ASP GLY MSE
SEQRES 7 A 145 MSE GLY LYS GLN VAL LYS PRO TYR ILE MSE ASP LEU GLY
SEQRES 8 A 145 SER THR ASN LYS THR TYR ILE ASN GLU SER PRO ILE GLU
SEQRES 9 A 145 PRO GLN ARG TYR TYR GLU LEU PHE GLU LYS ASP THR ILE
SEQRES 10 A 145 LYS PHE GLY ASN SER SER ARG GLU TYR VAL LEU LEU HIS
SEQRES 11 A 145 GLU ASN SER ALA GLU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 12 A 145 HIS HIS
MODRES 3VPY MSE A 70 MET SELENOMETHIONINE
MODRES 3VPY MSE A 78 MET SELENOMETHIONINE
MODRES 3VPY MSE A 79 MET SELENOMETHIONINE
MODRES 3VPY MSE A 88 MET SELENOMETHIONINE
HET MSE A 70 8
HET MSE A 78 8
HET MSE A 79 8
HET MSE A 88 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 HOH *140(H2 O)
HELIX 1 1 SER A 133 HIS A 145 1 13
SHEET 1 A 3 GLU A 26 PRO A 27 0
SHEET 2 A 3 ARG A 18 LYS A 23 -1 N LYS A 23 O GLU A 26
SHEET 3 A 3 LEU A 32 CYS A 33 -1 O LEU A 32 N LEU A 19
SHEET 1 B 6 GLU A 26 PRO A 27 0
SHEET 2 B 6 ARG A 18 LYS A 23 -1 N LYS A 23 O GLU A 26
SHEET 3 B 6 ARG A 124 LEU A 129 -1 O LEU A 129 N ARG A 18
SHEET 4 B 6 THR A 116 PHE A 119 -1 N ILE A 117 O TYR A 126
SHEET 5 B 6 THR A 96 ILE A 98 -1 N TYR A 97 O LYS A 118
SHEET 6 B 6 SER A 101 PRO A 102 -1 O SER A 101 N ILE A 98
SHEET 1 C 5 ILE A 51 PRO A 52 0
SHEET 2 C 5 CYS A 39 GLY A 43 1 N LEU A 41 O ILE A 51
SHEET 3 C 5 ALA A 63 GLU A 73 -1 O ALA A 63 N PHE A 42
SHEET 4 C 5 MSE A 79 ASP A 89 -1 O TYR A 86 N GLN A 66
SHEET 5 C 5 TYR A 109 GLU A 110 -1 O TYR A 109 N ILE A 87
LINK C GLU A 69 N MSE A 70 1555 1555 1.34
LINK C MSE A 70 N GLU A 71 1555 1555 1.33
LINK C GLY A 77 N MSE A 78 1555 1555 1.33
LINK C MSE A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N GLY A 80 1555 1555 1.33
LINK C ILE A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N ASP A 89 1555 1555 1.33
CRYST1 48.564 48.709 54.688 90.00 90.00 90.00 P 21 21 21 4
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 0.020591 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020530 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018286 0.00000
(ATOM LINES ARE NOT SHOWN.)
END