HEADER TRANSCRIPTION 18-APR-14 4Q5Y
TITLE CRYSTAL STRUCTURE OF EXTENDED-TUDOR 10-11 OF DROSOPHILA MELANOGASTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATERNAL PROTEIN TUDOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTENDED-TUDOR 10-11, UNP RESIDUES 2164-2515;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: CG9450, TUD, TUDOR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-SMT3
KEYWDS TUDOR DOMAIN, RECOGNIZE SDMA OF AUBERGINE, SDMA OF AUBERGINE,
KEYWDS 2 NUCLEUS, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LIU,R.REN,W.WANG,M.WANG,N.YANG,Y.DONG,W.GONG,R.LEHMANN,R.M.XU
REVDAT 3 08-NOV-23 4Q5Y 1 SEQADV
REVDAT 2 17-SEP-14 4Q5Y 1 JRNL
REVDAT 1 21-MAY-14 4Q5Y 0
JRNL AUTH R.REN,H.LIU,W.WANG,M.WANG,N.YANG,Y.H.DONG,W.GONG,R.LEHMANN,
JRNL AUTH 2 R.M.XU
JRNL TITL STRUCTURE AND DOMAIN ORGANIZATION OF DROSOPHILA TUDOR
JRNL REF CELL RES. V. 24 1146 2014
JRNL REFN ISSN 1001-0602
JRNL PMID 24810300
JRNL DOI 10.1038/CR.2014.63
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 12930
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 676
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2673
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 56
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Q5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085645.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.99985
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13606
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3NTK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TACSIMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 35.62350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.87350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.72050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.87350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.62350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.72050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.62350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.72050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 75.87350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.72050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.62350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 75.87350
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 62.72050
REMARK 350 BIOMT3 2 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 LEU A 2199
REMARK 465 LYS A 2200
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 SER A2161 OG
REMARK 470 GLU A2162 CG CD OE1 OE2
REMARK 470 PHE A2163 CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A2173 CG OD1 ND2
REMARK 470 LYS A2176 CG CD CE NZ
REMARK 470 LYS A2183 CG CD CE NZ
REMARK 470 SER A2186 OG
REMARK 470 ASP A2190 CG OD1 OD2
REMARK 470 LYS A2194 CG CD CE NZ
REMARK 470 THR A2195 OG1 CG2
REMARK 470 SER A2198 OG
REMARK 470 LYS A2201 CG CD CE NZ
REMARK 470 GLU A2202 CG CD OE1 OE2
REMARK 470 LYS A2203 CG CD CE NZ
REMARK 470 LEU A2204 CG CD1 CD2
REMARK 470 LYS A2206 CG CD CE NZ
REMARK 470 ASP A2209 CG OD1 OD2
REMARK 470 GLN A2221 CG CD OE1 NE2
REMARK 470 CYS A2225 SG
REMARK 470 TYR A2226 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A2232 CG CD CE NZ
REMARK 470 VAL A2234 CG1 CG2
REMARK 470 LEU A2252 CG CD1 CD2
REMARK 470 GLN A2259 CG CD OE1 NE2
REMARK 470 LEU A2260 CG CD1 CD2
REMARK 470 GLN A2262 CG CD OE1 NE2
REMARK 470 GLU A2265 CG CD OE1 OE2
REMARK 470 GLU A2286 CG CD OE1 OE2
REMARK 470 LYS A2287 CG CD CE NZ
REMARK 470 GLU A2312 CG CD OE1 OE2
REMARK 470 GLU A2314 CG CD OE1 OE2
REMARK 470 THR A2315 OG1 CG2
REMARK 470 LYS A2316 CG CD CE NZ
REMARK 470 GLU A2345 CG CD OE1 OE2
REMARK 470 LYS A2394 CG CD CE NZ
REMARK 470 LYS A2465 CG CD CE NZ
REMARK 470 ASP A2467 CG OD1 OD2
REMARK 470 LYS A2505 CG CD CE NZ
REMARK 470 GLU A2513 CG CD OE1 OE2
REMARK 470 CYS A2514 SG
REMARK 470 GLN A2515 CG CD OE1 NE2
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 PHE A 2300 N GLU A 2302 2.14
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 SER A2177 114.92 -165.50
REMARK 500 THR A2195 27.90 -64.57
REMARK 500 LEU A2204 -155.45 169.85
REMARK 500 LYS A2205 -167.96 166.74
REMARK 500 ILE A2208 72.96 -65.43
REMARK 500 PRO A2210 121.31 -19.55
REMARK 500 ASN A2213 -7.41 71.75
REMARK 500 SER A2230 118.68 -174.80
REMARK 500 TYR A2248 -42.99 -141.19
REMARK 500 VAL A2257 -166.16 -107.30
REMARK 500 TRP A2258 -152.56 -156.12
REMARK 500 GLN A2262 56.03 -58.03
REMARK 500 GLU A2263 -56.52 -140.13
REMARK 500 GLU A2265 -29.47 -39.14
REMARK 500 PRO A2280 100.68 -54.82
REMARK 500 GLN A2298 -3.64 -57.15
REMARK 500 HIS A2299 -84.89 -129.81
REMARK 500 PHE A2300 -149.59 68.93
REMARK 500 PRO A2310 170.66 -53.80
REMARK 500 VAL A2340 122.10 -25.12
REMARK 500 GLN A2341 -160.78 -67.75
REMARK 500 GLN A2355 108.77 -166.68
REMARK 500 ASP A2357 29.01 -143.76
REMARK 500 SER A2361 106.51 -169.23
REMARK 500 ASP A2378 -72.15 -72.10
REMARK 500 ASP A2392 71.53 -60.93
REMARK 500 LEU A2393 62.64 -69.93
REMARK 500 CYS A2399 177.22 168.47
REMARK 500 PRO A2404 -78.02 -47.78
REMARK 500 ASP A2420 -40.20 116.87
REMARK 500 LYS A2465 2.83 -61.44
REMARK 500 ALA A2469 -72.87 -60.45
REMARK 500 ARG A2478 50.24 -116.38
REMARK 500 SER A2504 -4.73 65.75
REMARK 500 GLU A2513 34.64 145.82
REMARK 500 CYS A2514 70.73 76.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q5W RELATED DB: PDB
DBREF 4Q5Y A 2164 2515 UNP P25823 TUD_DROME 2164 2515
SEQADV 4Q5Y SER A 2161 UNP P25823 EXPRESSION TAG
SEQADV 4Q5Y GLU A 2162 UNP P25823 EXPRESSION TAG
SEQADV 4Q5Y PHE A 2163 UNP P25823 EXPRESSION TAG
SEQRES 1 A 355 SER GLU PHE ASN SER GLU CYS ILE ILE SER TYR GLY ASN
SEQRES 2 A 355 SER PRO LYS SER PHE TYR VAL GLN MET LYS HIS ASN SER
SEQRES 3 A 355 ALA ASP LEU ASP LEU ILE VAL LYS THR LEU GLN SER LEU
SEQRES 4 A 355 LYS LYS GLU LYS LEU LYS LYS LEU ILE ASP PRO THR THR
SEQRES 5 A 355 ASN SER ASN GLY VAL CYS TYR SER GLN GLU ASP ALA CYS
SEQRES 6 A 355 TYR TYR ARG CYS SER ILE LYS SER VAL LEU ASP PRO SER
SEQRES 7 A 355 GLN GLY PHE GLU VAL PHE LEU LEU ASP TYR GLY ASN THR
SEQRES 8 A 355 LEU VAL VAL PRO GLU VAL TRP GLN LEU PRO GLN GLU ILE
SEQRES 9 A 355 GLU PRO ILE PRO SER LEU ALA LEU HIS CYS GLN LEU SER
SEQRES 10 A 355 LYS ILE PRO MET ASP VAL SER ASP GLU LYS LEU GLU GLU
SEQRES 11 A 355 ALA PHE ALA ALA LEU LEU GLU GLN HIS PHE GLY GLU LEU
SEQRES 12 A 355 TYR GLU ILE THR THR GLN PRO ASN GLU ASP GLU THR LYS
SEQRES 13 A 355 PRO LEU ILE ALA GLU LEU ARG ILE ASN TYR LYS ASP PHE
SEQRES 14 A 355 VAL GLN GLU LEU VAL SER THR VAL THR GLY VAL GLN LYS
SEQRES 15 A 355 PRO LEU GLU ALA GLU LEU HIS ASN CYS VAL VAL VAL GLN
SEQRES 16 A 355 PHE ASP GLY PRO MET SER PHE TYR VAL GLN MET GLU SER
SEQRES 17 A 355 ASP VAL PRO ALA LEU GLU GLN MET THR ASP LYS LEU LEU
SEQRES 18 A 355 ASP ALA GLU GLN ASP LEU PRO ALA PHE SER ASP LEU LYS
SEQRES 19 A 355 GLU GLY ALA LEU CYS VAL ALA GLN PHE PRO GLU ASP GLU
SEQRES 20 A 355 VAL PHE TYR ARG ALA GLN ILE ARG LYS VAL LEU ASP ASP
SEQRES 21 A 355 GLY LYS CYS GLU VAL HIS PHE ILE ASP PHE GLY ASN ASN
SEQRES 22 A 355 ALA VAL THR GLN GLN PHE ARG GLN LEU PRO GLU GLU LEU
SEQRES 23 A 355 ALA LYS PRO ALA ARG TYR SER ARG HIS CYS GLU LEU ASP
SEQRES 24 A 355 ALA SER THR ILE SER LYS CYS ASP ALA ALA LEU LEU GLN
SEQRES 25 A 355 SER PHE ILE ASP THR ARG PHE SER GLU THR PHE GLN VAL
SEQRES 26 A 355 GLU ILE LEU ALA THR LYS GLY THR GLY THR HIS VAL VAL
SEQRES 27 A 355 ARG LEU PHE TYR GLN SER LYS ASN ILE SER GLU LYS LEU
SEQRES 28 A 355 GLN GLU CYS GLN
FORMUL 2 HOH *56(H2 O)
HELIX 1 1 ASN A 2185 THR A 2195 1 11
HELIX 2 2 SER A 2284 GLN A 2298 1 15
HELIX 3 3 PHE A 2329 THR A 2338 1 10
HELIX 4 4 PRO A 2343 ALA A 2346 5 4
HELIX 5 5 ASP A 2369 GLN A 2385 1 17
HELIX 6 6 PRO A 2443 ALA A 2447 5 5
HELIX 7 7 ASP A 2459 CYS A 2466 1 8
HELIX 8 8 ASP A 2467 ARG A 2478 1 12
HELIX 9 9 ILE A 2507 GLN A 2512 1 6
SHEET 1 A 7 LYS A2327 ASP A2328 0
SHEET 2 A 7 LEU A2318 ILE A2324 -1 N ILE A2324 O LYS A2327
SHEET 3 A 7 TYR A2304 GLN A2309 -1 N GLU A2305 O ARG A2323
SHEET 4 A 7 SER A2165 SER A2174 -1 N CYS A2167 O TYR A2304
SHEET 5 A 7 SER A2177 MET A2182 -1 O TYR A2179 N TYR A2171
SHEET 6 A 7 LEU A2272 LEU A2276 -1 O CYS A2274 N PHE A2178
SHEET 7 A 7 LEU A2318 ILE A2324 1 O ALA A2320 N GLN A2275
SHEET 1 B 2 VAL A2217 SER A2220 0
SHEET 2 B 2 CYS A2225 ARG A2228 -1 O CYS A2225 N SER A2220
SHEET 1 C 3 ILE A2231 VAL A2234 0
SHEET 2 C 3 PHE A2241 PHE A2244 -1 O GLU A2242 N LYS A2232
SHEET 3 C 3 THR A2251 VAL A2254 -1 O LEU A2252 N VAL A2243
SHEET 1 D 7 LYS A2505 ASN A2506 0
SHEET 2 D 7 HIS A2496 TYR A2502 -1 N TYR A2502 O LYS A2505
SHEET 3 D 7 THR A2482 THR A2490 -1 N ALA A2489 O VAL A2497
SHEET 4 D 7 LEU A2348 PHE A2356 -1 N CYS A2351 O PHE A2483
SHEET 5 D 7 PHE A2362 MET A2366 -1 O TYR A2363 N GLN A2355
SHEET 6 D 7 ARG A2454 LEU A2458 -1 O ARG A2454 N VAL A2364
SHEET 7 D 7 HIS A2496 TYR A2502 1 O HIS A2496 N HIS A2455
SHEET 1 E 4 LEU A2398 PHE A2403 0
SHEET 2 E 4 VAL A2408 VAL A2417 -1 O ALA A2412 N CYS A2399
SHEET 3 E 4 CYS A2423 PHE A2427 -1 O GLU A2424 N ARG A2415
SHEET 4 E 4 ASN A2433 THR A2436 -1 O ALA A2434 N VAL A2425
SSBOND 1 CYS A 2218 CYS A 2229 1555 1555 2.05
CRYST1 71.247 125.441 151.747 90.00 90.00 90.00 I 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 0.014036 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007972 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006590 0.00000
(ATOM LINES ARE NOT SHOWN.)
END