HEADER DNA BINDING PROTEIN 07-APR-11 3AXJ
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF C3PO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GM27569P;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSLIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRANSLIN ASSOCIATED FACTOR X, ISOFORM B;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: TRAX;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: 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: TRSN, TRANSLIN, CG11761, DMEL_CG11761;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET DUET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 11 ORGANISM_COMMON: FRUIT FLY;
SOURCE 12 ORGANISM_TAXID: 7227;
SOURCE 13 GENE: TRAX, DMEL_CG5063;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSLIN/TRAX HETERODIMER, PASSENGER RNA CLEAVAGE, RNASE, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.A.YUAN,X.YANG
REVDAT 1 20-APR-11 3AXJ 0
JRNL AUTH Y.A.YUAN,X.YANG
JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURE OF C3PO
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 40056
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2128
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2886
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 159
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3783
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.67000
REMARK 3 B22 (A**2) : 3.60000
REMARK 3 B33 (A**2) : -2.93000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.190
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3844 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5175 ; 1.375 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 462 ; 5.182 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 197 ;30.953 ;24.213
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 726 ;15.153 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;20.402 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 576 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2877 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1680 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2712 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 167 ; 0.155 ; 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): 94 ; 0.246 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.184 ; 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): 2390 ; 1.405 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3724 ; 1.965 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1650 ; 3.169 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1451 ; 4.907 ; 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -3 A 221
REMARK 3 RESIDUE RANGE : B 23 B 282
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0344 32.2088 -1.8280
REMARK 3 T TENSOR
REMARK 3 T11: -0.1060 T22: -0.1184
REMARK 3 T33: -0.0470 T12: -0.0284
REMARK 3 T13: -0.0052 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.3880 L22: 0.1453
REMARK 3 L33: 1.4558 L12: 0.0518
REMARK 3 L13: -0.3906 L23: 0.1477
REMARK 3 S TENSOR
REMARK 3 S11: 0.0124 S12: -0.0052 S13: 0.0447
REMARK 3 S21: -0.0183 S22: -0.0067 S23: 0.0139
REMARK 3 S31: -0.0755 S32: -0.0221 S33: -0.0057
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: CHAIN B HAS BEEN TRANSLATED WITH
REMARK 3 SYMMETRY OPERATION AFTER REFINEMENT. CURRENT TLS ORIGIN IS
REMARK 3 INCONSISTENT WITH THE COORDINATES.
REMARK 4
REMARK 4 3AXJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB029819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-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) : 0.9792
REMARK 200 MONOCHROMATOR : 360 DEGREE WITH 1 DEGREE
REMARK 200 OSCILLATION
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40056
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 56.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, CACODYLATE, MG2+, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.95450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.95450
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 1.000000 0.000000 0.000000 50.83800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.36000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.83800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.36000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.95450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.83800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.36000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.95450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.83800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.36000
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MSE A -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 GLU A 222
REMARK 465 LYS A 223
REMARK 465 ASP A 224
REMARK 465 GLN A 225
REMARK 465 GLN A 226
REMARK 465 GLU A 227
REMARK 465 GLU A 228
REMARK 465 PRO A 229
REMARK 465 ALA A 230
REMARK 465 VAL A 231
REMARK 465 PRO A 232
REMARK 465 ALA A 233
REMARK 465 THR A 234
REMARK 465 GLU A 235
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 LYS B 3
REMARK 465 ASN B 4
REMARK 465 GLY B 5
REMARK 465 GLY B 6
REMARK 465 ALA B 7
REMARK 465 GLY B 8
REMARK 465 HIS B 9
REMARK 465 ARG B 10
REMARK 465 ASN B 11
REMARK 465 THR B 12
REMARK 465 ALA B 13
REMARK 465 PRO B 14
REMARK 465 ARG B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 GLN B 18
REMARK 465 ILE B 19
REMARK 465 PRO B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 SER B 165
REMARK 465 GLN B 166
REMARK 465 PRO B 167
REMARK 465 LYS B 168
REMARK 465 GLU B 169
REMARK 465 GLU B 170
REMARK 465 PRO B 171
REMARK 465 THR B 172
REMARK 465 GLU B 173
REMARK 465 GLY B 174
REMARK 465 GLU B 175
REMARK 465 ASP B 176
REMARK 465 VAL B 177
REMARK 465 GLN B 178
REMARK 465 ALA B 179
REMARK 465 ILE B 180
REMARK 465 ALA B 181
REMARK 465 GLN B 182
REMARK 465 VAL B 183
REMARK 465 GLU B 184
REMARK 465 ALA B 283
REMARK 465 THR B 284
REMARK 465 PHE B 285
REMARK 465 ASP B 286
REMARK 465 GLN B 287
REMARK 465 LYS B 288
REMARK 465 PRO B 289
REMARK 465 ALA B 290
REMARK 465 ASP B 291
REMARK 465 GLU B 292
REMARK 465 VAL B 293
REMARK 465 ASP B 294
REMARK 465 GLU B 295
REMARK 465 GLY B 296
REMARK 465 PHE B 297
REMARK 465 TYR B 298
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 TRP B 281 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 281 CZ3 CH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER B 164 CB SER B 164 OG 0.093
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 167 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
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 ASN A 189 103.02 -38.87
REMARK 500 ARG B 75 112.49 -28.99
REMARK 500 GLN B 77 4.91 -59.83
REMARK 500 LYS B 79 -71.17 -50.58
REMARK 500 VAL B 96 -63.95 -105.97
REMARK 500 MSE B 158 54.34 -105.72
REMARK 500 ARG B 246 12.94 53.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3AXJ A 1 235 UNP Q7JVK6 Q7JVK6_DROME 1 235
DBREF 3AXJ B 1 298 UNP Q8INE1 Q8INE1_DROME 1 298
SEQADV 3AXJ MSE A -13 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ GLY A -12 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ SER A -11 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ SER A -10 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ HIS A -9 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ HIS A -8 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ HIS A -7 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ HIS A -6 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ HIS A -5 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ HIS A -4 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ SER A -3 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ GLN A -2 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ ASP A -1 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ PRO A 0 UNP Q7JVK6 EXPRESSION TAG
SEQADV 3AXJ GLN B 126 UNP Q8INE1 GLU 126 ENGINEERED MUTATION
SEQRES 1 A 249 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 249 PRO MSE SER ASN PHE VAL ASN LEU ASP ILE PHE SER ASN
SEQRES 3 A 249 TYR GLN LYS TYR ILE ASP ASN GLU GLN GLU VAL ARG GLU
SEQRES 4 A 249 ASN ILE ARG ILE VAL VAL ARG GLU ILE GLU HIS LEU SER
SEQRES 5 A 249 LYS GLU ALA GLN ILE LYS LEU GLN ILE ILE HIS SER ASP
SEQRES 6 A 249 LEU SER GLN ILE SER ALA ALA CYS GLY LEU ALA ARG LYS
SEQRES 7 A 249 GLN VAL GLU LEU CYS ALA GLN LYS TYR GLN LYS LEU ALA
SEQRES 8 A 249 GLU LEU VAL PRO ALA GLY GLN TYR TYR ARG TYR SER ASP
SEQRES 9 A 249 HIS TRP THR PHE ILE THR GLN ARG LEU ILE PHE ILE ILE
SEQRES 10 A 249 ALA LEU VAL ILE TYR LEU GLU ALA GLY PHE LEU VAL THR
SEQRES 11 A 249 ARG GLU THR VAL ALA GLU MSE LEU GLY LEU LYS ILE SER
SEQRES 12 A 249 GLN SER GLU GLY PHE HIS LEU ASP VAL GLU ASP TYR LEU
SEQRES 13 A 249 LEU GLY ILE LEU GLN LEU ALA SER GLU LEU SER ARG PHE
SEQRES 14 A 249 ALA THR ASN SER VAL THR MSE GLY ASP TYR GLU ARG PRO
SEQRES 15 A 249 LEU ASN ILE SER HIS PHE ILE GLY ASP LEU ASN THR GLY
SEQRES 16 A 249 PHE ARG LEU LEU ASN LEU LYS ASN ASP GLY LEU ARG LYS
SEQRES 17 A 249 ARG PHE ASP ALA LEU LYS TYR ASP VAL LYS LYS ILE GLU
SEQRES 18 A 249 GLU VAL VAL TYR ASP VAL SER ILE ARG GLY LEU SER SER
SEQRES 19 A 249 LYS GLU LYS ASP GLN GLN GLU GLU PRO ALA VAL PRO ALA
SEQRES 20 A 249 THR GLU
SEQRES 1 B 298 MSE PRO LYS ASN GLY GLY ALA GLY HIS ARG ASN THR ALA
SEQRES 2 B 298 PRO ARG LYS ARG GLN ILE PRO ALA ALA GLN LEU ASP GLU
SEQRES 3 B 298 ASP SER PRO ILE VAL GLN GLN PHE ARG ILE TYR SER ASN
SEQRES 4 B 298 GLU LEU ILE MSE LYS HIS ASP ARG HIS GLU ARG ILE VAL
SEQRES 5 B 298 LYS LEU SER ARG ASP ILE THR ILE GLU SER LYS ARG ILE
SEQRES 6 B 298 ILE PHE LEU LEU HIS SER ILE ASP SER ARG LYS GLN ASN
SEQRES 7 B 298 LYS GLU LYS VAL LEU GLU GLU ALA ARG GLN ARG LEU ASN
SEQRES 8 B 298 LYS LEU ILE ALA VAL ASN PHE ARG ALA VAL ALA LEU GLU
SEQRES 9 B 298 LEU ARG ASP GLN ASP VAL TYR GLN PHE ARG SER SER TYR
SEQRES 10 B 298 SER PRO GLY LEU GLN GLU PHE ILE GLN ALA TYR THR TYR
SEQRES 11 B 298 MSE GLU TYR LEU CYS HIS GLU ASP ALA GLU GLY GLU ASN
SEQRES 12 B 298 GLU THR LYS SER VAL SER ASP TRP GLN ALA ILE GLN ALA
SEQRES 13 B 298 VAL MSE GLN TYR VAL GLU GLU SER SER GLN PRO LYS GLU
SEQRES 14 B 298 GLU PRO THR GLU GLY GLU ASP VAL GLN ALA ILE ALA GLN
SEQRES 15 B 298 VAL GLU SER PRO LYS LYS PHE GLN PHE PHE VAL ASP PRO
SEQRES 16 B 298 THR GLU TYR ILE LEU GLY LEU SER ASP LEU THR GLY GLU
SEQRES 17 B 298 LEU MSE ARG ARG CYS ILE ASN SER LEU GLY SER GLY ASP
SEQRES 18 B 298 THR ASP THR CYS LEU ASP THR CYS LYS ALA LEU GLN HIS
SEQRES 19 B 298 PHE TYR SER GLY TYR ILE SER LEU ASN CYS GLN ARG ALA
SEQRES 20 B 298 ARG GLU LEU TRP ARG LYS ILE THR THR MSE LYS GLN SER
SEQRES 21 B 298 VAL LEU LYS ALA GLU ASN VAL CYS TYR ASN VAL LYS VAL
SEQRES 22 B 298 ARG GLY GLY GLU ALA ALA LYS TRP GLY ALA THR PHE ASP
SEQRES 23 B 298 GLN LYS PRO ALA ASP GLU VAL ASP GLU GLY PHE TYR
MODRES 3AXJ MSE A 1 MET SELENOMETHIONINE
MODRES 3AXJ MSE A 123 MET SELENOMETHIONINE
MODRES 3AXJ MSE A 162 MET SELENOMETHIONINE
MODRES 3AXJ MSE B 43 MET SELENOMETHIONINE
MODRES 3AXJ MSE B 131 MET SELENOMETHIONINE
MODRES 3AXJ MSE B 158 MET SELENOMETHIONINE
MODRES 3AXJ MSE B 210 MET SELENOMETHIONINE
MODRES 3AXJ MSE B 257 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 123 8
HET MSE A 162 8
HET MSE B 43 8
HET MSE B 131 8
HET MSE B 158 8
HET MSE B 210 8
HET MSE B 257 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 HOH *208(H2 O)
HELIX 1 1 PRO A 0 VAL A 5 1 6
HELIX 2 2 ASN A 6 GLN A 46 1 41
HELIX 3 3 ILE A 47 SER A 50 5 4
HELIX 4 4 ASP A 51 SER A 53 5 3
HELIX 5 5 GLN A 54 VAL A 80 1 27
HELIX 6 6 GLN A 84 SER A 89 1 6
HELIX 7 7 TRP A 92 GLY A 112 1 21
HELIX 8 8 THR A 116 GLY A 125 1 10
HELIX 9 9 ASP A 137 MSE A 162 1 26
HELIX 10 10 GLU A 166 LEU A 185 1 20
HELIX 11 11 ASP A 190 ARG A 216 1 27
HELIX 12 12 SER B 28 HIS B 70 1 43
HELIX 13 13 ARG B 75 GLN B 77 5 3
HELIX 14 14 ASN B 78 VAL B 96 1 19
HELIX 15 15 VAL B 96 LEU B 105 1 10
HELIX 16 16 PHE B 113 ASP B 138 1 26
HELIX 17 17 GLY B 141 LYS B 146 5 6
HELIX 18 18 ASP B 150 MSE B 158 1 9
HELIX 19 19 ASP B 194 SER B 219 1 26
HELIX 20 20 ASP B 221 SER B 241 1 21
HELIX 21 21 ALA B 247 GLY B 275 1 29
HELIX 22 22 GLY B 275 TRP B 281 1 7
SHEET 1 A 2 GLN B 159 VAL B 161 0
SHEET 2 A 2 LYS B 188 GLN B 190 -1 O PHE B 189 N TYR B 160
LINK C PRO A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N SER A 2 1555 1555 1.33
LINK C GLU A 122 N MSE A 123 1555 1555 1.33
LINK C MSE A 123 N LEU A 124 1555 1555 1.33
LINK C THR A 161 N MSE A 162 1555 1555 1.33
LINK C MSE A 162 N GLY A 163 1555 1555 1.34
LINK C ILE B 42 N MSE B 43 1555 1555 1.33
LINK C MSE B 43 N LYS B 44 1555 1555 1.33
LINK C TYR B 130 N MSE B 131 1555 1555 1.33
LINK C MSE B 131 N GLU B 132 1555 1555 1.32
LINK C VAL B 157 N MSE B 158 1555 1555 1.32
LINK C MSE B 158 N GLN B 159 1555 1555 1.33
LINK C LEU B 209 N MSE B 210 1555 1555 1.33
LINK C MSE B 210 N ARG B 211 1555 1555 1.33
LINK C THR B 256 N MSE B 257 1555 1555 1.34
LINK C MSE B 257 N LYS B 258 1555 1555 1.33
CRYST1 101.676 114.720 123.909 90.00 90.00 90.00 C 2 2 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 0.009835 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
