HEADER HYDROLASE 27-FEB-09 3GFP
TITLE STRUCTURE OF THE C-TERMINAL DOMAIN OF THE DEAD-BOX PROTEIN DBP5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEAD BOX PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HELICASE C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: ATP-DEPENDENT RNA HELICASE DBP5, HELICASE CA5/6, RIBONUCLEIC
COMPND 6 ACID-TRAFFICKING PROTEIN 8;
COMPND 7 EC: 3.6.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: DBP5, RAT8, YOR046C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS MRNA EXPORT, ATPASE, RECA-FOLD, ATP-BINDING, HELICASE, HYDROLASE,
KEYWDS 2 MEMBRANE, MRNA TRANSPORT, NUCLEAR PORE COMPLEX, NUCLEOTIDE-BINDING,
KEYWDS 3 NUCLEUS, PHOSPHOPROTEIN, PROTEIN TRANSPORT, RNA-BINDING,
KEYWDS 4 TRANSLOCATION, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.ERZBERGER,Z.Y.DOSSANI,C.S.WEIRICH,K.WEIS,J.M.BERGER
REVDAT 3 13-JUL-11 3GFP 1 VERSN
REVDAT 2 13-OCT-09 3GFP 1 JRNL
REVDAT 1 01-SEP-09 3GFP 0
JRNL AUTH Z.Y.DOSSANI,C.S.WEIRICH,J.P.ERZBERGER,J.M.BERGER,K.WEIS
JRNL TITL STRUCTURE OF THE C-TERMINUS OF THE MRNA EXPORT FACTOR DBP5
JRNL TITL 2 REVEALS THE INTERACTION SURFACE FOR THE ATPASE ACTIVATOR
JRNL TITL 3 GLE1
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 16251 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19805289
JRNL DOI 10.1073/PNAS.0902251106
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19340
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1016
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1404
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1422
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 25.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : -0.82000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : -0.41000
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): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.320
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1451 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1959 ; 0.956 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 180 ; 5.219 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 66 ;30.504 ;24.242
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 268 ;14.028 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;18.491 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 228 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1069 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 738 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1022 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 119 ; 0.146 ; 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): 57 ; 0.156 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.149 ; 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): 919 ; 0.851 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1454 ; 1.251 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 588 ; 2.011 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 505 ; 2.965 ; 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 : 2
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 300 A 479
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9794 -19.9272 -8.4130
REMARK 3 T TENSOR
REMARK 3 T11: -0.0285 T22: -0.0326
REMARK 3 T33: -0.0399 T12: -0.0184
REMARK 3 T13: -0.0466 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 1.0484 L22: 1.3285
REMARK 3 L33: 0.7842 L12: -0.2151
REMARK 3 L13: 0.1901 L23: -0.0990
REMARK 3 S TENSOR
REMARK 3 S11: -0.1296 S12: 0.0642 S13: 0.1011
REMARK 3 S21: 0.0240 S22: 0.0543 S23: -0.0772
REMARK 3 S31: -0.0900 S32: 0.0649 S33: 0.0753
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7709 -20.7604 -9.6589
REMARK 3 T TENSOR
REMARK 3 T11: -0.0344 T22: -0.0096
REMARK 3 T33: -0.0479 T12: -0.0090
REMARK 3 T13: -0.0237 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 0.4479 L22: 1.0719
REMARK 3 L33: 0.4110 L12: -0.2593
REMARK 3 L13: 0.1624 L23: -0.1058
REMARK 3 S TENSOR
REMARK 3 S11: -0.1049 S12: 0.0778 S13: 0.0472
REMARK 3 S21: 0.0156 S22: 0.0276 S23: -0.0478
REMARK 3 S31: -0.0411 S32: 0.0162 S33: 0.0773
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3GFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB051801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795,1.0332,1.11588
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24212
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 56.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04000
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) : 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA/K HPO4, 100MM NA CACODYLATE PH
REMARK 280 6.5, 8% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 37.71867
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 18.85933
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 37.71867
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 18.85933
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 2 LIES ON A SPECIAL POSITION.
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 294
REMARK 465 ALA A 295
REMARK 465 THR A 296
REMARK 465 ASN A 297
REMARK 465 GLU A 298
REMARK 465 VAL A 299
REMARK 465 LEU A 480
REMARK 465 LYS A 481
REMARK 465 ASP A 482
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 LYS A 478 -71.08 -59.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 114 DISTANCE = 5.78 ANGSTROMS
DBREF 3GFP A 296 482 UNP P20449 DBP5_YEAST 296 482
SEQADV 3GFP GLY A 294 UNP P20449 EXPRESSION TAG
SEQADV 3GFP ALA A 295 UNP P20449 EXPRESSION TAG
SEQRES 1 A 189 GLY ALA THR ASN GLU VAL ASN VAL ASP ALA ILE LYS GLN
SEQRES 2 A 189 LEU TYR MSE ASP CYS LYS ASN GLU ALA ASP LYS PHE ASP
SEQRES 3 A 189 VAL LEU THR GLU LEU TYR GLY LEU MSE THR ILE GLY SER
SEQRES 4 A 189 SER ILE ILE PHE VAL ALA THR LYS LYS THR ALA ASN VAL
SEQRES 5 A 189 LEU TYR GLY LYS LEU LYS SER GLU GLY HIS GLU VAL SER
SEQRES 6 A 189 ILE LEU HIS GLY ASP LEU GLN THR GLN GLU ARG ASP ARG
SEQRES 7 A 189 LEU ILE ASP ASP PHE ARG GLU GLY ARG SER LYS VAL LEU
SEQRES 8 A 189 ILE THR THR ASN VAL LEU ALA ARG GLY ILE ASP ILE PRO
SEQRES 9 A 189 THR VAL SER MSE VAL VAL ASN TYR ASP LEU PRO THR LEU
SEQRES 10 A 189 ALA ASN GLY GLN ALA ASP PRO ALA THR TYR ILE HIS ARG
SEQRES 11 A 189 ILE GLY ARG THR GLY ARG PHE GLY ARG LYS GLY VAL ALA
SEQRES 12 A 189 ILE SER PHE VAL HIS ASP LYS ASN SER PHE ASN ILE LEU
SEQRES 13 A 189 SER ALA ILE GLN LYS TYR PHE GLY ASP ILE GLU MSE THR
SEQRES 14 A 189 ARG VAL PRO THR ASP ASP TRP ASP GLU VAL GLU LYS ILE
SEQRES 15 A 189 VAL LYS LYS VAL LEU LYS ASP
MODRES 3GFP MSE A 309 MET SELENOMETHIONINE
MODRES 3GFP MSE A 328 MET SELENOMETHIONINE
MODRES 3GFP MSE A 401 MET SELENOMETHIONINE
MODRES 3GFP MSE A 461 MET SELENOMETHIONINE
HET MSE A 309 8
HET MSE A 328 8
HET MSE A 401 8
HET MSE A 461 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 HOH *153(H2 O)
HELIX 1 1 ALA A 315 MSE A 328 1 14
HELIX 2 2 THR A 339 GLU A 353 1 15
HELIX 3 3 GLN A 365 GLY A 379 1 15
HELIX 4 4 ASP A 416 GLY A 425 1 10
HELIX 5 5 ASP A 442 PHE A 456 1 15
HELIX 6 6 ASP A 468 VAL A 479 1 12
SHEET 1 A 7 VAL A 357 LEU A 360 0
SHEET 2 A 7 VAL A 383 THR A 387 1 O ILE A 385 N LEU A 360
SHEET 3 A 7 SER A 333 VAL A 337 1 N ILE A 335 O LEU A 384
SHEET 4 A 7 MSE A 401 ASN A 404 1 O VAL A 403 N ILE A 334
SHEET 5 A 7 VAL A 435 VAL A 440 1 O ILE A 437 N VAL A 402
SHEET 6 A 7 LYS A 305 ASP A 310 1 N MSE A 309 O SER A 438
SHEET 7 A 7 THR A 462 PRO A 465 1 O VAL A 464 N TYR A 308
LINK C TYR A 308 N MSE A 309 1555 1555 1.33
LINK C MSE A 309 N ASP A 310 1555 1555 1.33
LINK C LEU A 327 N MSE A 328 1555 1555 1.33
LINK C MSE A 328 N THR A 329 1555 1555 1.33
LINK C SER A 400 N MSE A 401 1555 1555 1.33
LINK C MSE A 401 N VAL A 402 1555 1555 1.33
LINK C GLU A 460 N MSE A 461 1555 1555 1.33
LINK C MSE A 461 N THR A 462 1555 1555 1.33
CRYST1 82.423 82.423 56.578 90.00 90.00 120.00 P 62 6
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 0.012133 0.007005 0.000000 0.00000
SCALE2 0.000000 0.014009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017675 0.00000
(ATOM LINES ARE NOT SHOWN.)
END