HEADER HYDROLASE 12-OCT-15 5E7I
TITLE CRYSTAL STRUCTURE OF THE ACTIVE CATALYTIC CORE OF THE HUMAN DEAD-BOX
TITLE 2 PROTEIN DDX3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;
COMPND 3 CHAIN: B, A, C;
COMPND 4 FRAGMENT: DEAD-BOX DOMAINS;
COMPND 5 SYNONYM: DEAD BOX PROTEIN 3,X-CHROMOSOMAL,DEAD BOX,X ISOFORM,
COMPND 6 HELICASE-LIKE PROTEIN 2,HLP2;
COMPND 7 EC: 3.6.4.13;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DDX3X, DBX, DDX3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHMGWA
KEYWDS DEAD-BOX PROTEIN, RNA HELICASE, RECA FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.N.FLOOR,K.J.CONDON,J.A.DOUDNA
REVDAT 3 10-FEB-16 5E7I 1 JRNL
REVDAT 2 09-DEC-15 5E7I 1 JRNL
REVDAT 1 02-DEC-15 5E7I 0
JRNL AUTH S.N.FLOOR,K.J.CONDON,D.SHARMA,E.JANKOWSKY,J.A.DOUDNA
JRNL TITL AUTOINHIBITORY INTERDOMAIN INTERACTIONS AND
JRNL TITL 2 SUBFAMILY-SPECIFIC EXTENSIONS REDEFINE THE CATALYTIC CORE OF
JRNL TITL 3 THE HUMAN DEAD-BOX PROTEIN DDX3.
JRNL REF J.BIOL.CHEM. V. 291 2412 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 26598523
JRNL DOI 10.1074/JBC.M115.700625
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 79683
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3985
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 86.1258 - 6.7504 1.00 2824 147 0.1593 0.1985
REMARK 3 2 6.7504 - 5.3582 1.00 2807 148 0.1974 0.2258
REMARK 3 3 5.3582 - 4.6809 1.00 2784 146 0.1615 0.2063
REMARK 3 4 4.6809 - 4.2530 1.00 2754 145 0.1528 0.1758
REMARK 3 5 4.2530 - 3.9481 1.00 2772 146 0.1823 0.2044
REMARK 3 6 3.9481 - 3.7154 1.00 2769 146 0.1885 0.2136
REMARK 3 7 3.7154 - 3.5293 1.00 2785 147 0.2031 0.2644
REMARK 3 8 3.5293 - 3.3756 1.00 2715 142 0.2209 0.2627
REMARK 3 9 3.3756 - 3.2457 1.00 2787 147 0.2331 0.2627
REMARK 3 10 3.2457 - 3.1337 1.00 2778 146 0.2435 0.2778
REMARK 3 11 3.1337 - 3.0357 1.00 2737 144 0.2530 0.2725
REMARK 3 12 3.0357 - 2.9489 1.00 2773 146 0.2584 0.3370
REMARK 3 13 2.9489 - 2.8713 1.00 2743 145 0.2560 0.2663
REMARK 3 14 2.8713 - 2.8012 1.00 2742 144 0.2638 0.3293
REMARK 3 15 2.8012 - 2.7375 1.00 2757 145 0.2689 0.2938
REMARK 3 16 2.7375 - 2.6793 1.00 2757 145 0.2699 0.2778
REMARK 3 17 2.6793 - 2.6257 1.00 2740 144 0.2772 0.3003
REMARK 3 18 2.6257 - 2.5761 1.00 2736 145 0.2777 0.3304
REMARK 3 19 2.5761 - 2.5301 1.00 2774 146 0.2850 0.3009
REMARK 3 20 2.5301 - 2.4872 1.00 2748 144 0.2841 0.3465
REMARK 3 21 2.4872 - 2.4471 1.00 2753 145 0.2854 0.3061
REMARK 3 22 2.4471 - 2.4095 1.00 2723 143 0.2892 0.3093
REMARK 3 23 2.4095 - 2.3740 1.00 2752 145 0.3079 0.3573
REMARK 3 24 2.3740 - 2.3406 1.00 2759 145 0.3031 0.3457
REMARK 3 25 2.3406 - 2.3089 0.97 2642 140 0.3094 0.3633
REMARK 3 26 2.3089 - 2.2790 0.93 2607 137 0.3218 0.3486
REMARK 3 27 2.2790 - 2.2505 0.88 2337 124 0.4353 0.4433
REMARK 3 28 2.2505 - 2.2233 0.66 1843 98 0.4275 0.4370
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.72
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 10247
REMARK 3 ANGLE : 0.816 13838
REMARK 3 CHIRALITY : 0.031 1542
REMARK 3 PLANARITY : 0.004 1809
REMARK 3 DIHEDRAL : 14.507 3911
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214491.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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) : 1.115869
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79724
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 86.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.36100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.920
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CITRATE, PH 5.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 52.69000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 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 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: 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: 3
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: C
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 GLU B 133
REMARK 465 GLY B 154
REMARK 465 ASN B 155
REMARK 465 THR B 156
REMARK 465 GLY B 157
REMARK 465 ILE B 158
REMARK 465 ASN B 159
REMARK 465 PHE B 160
REMARK 465 GLU B 161
REMARK 465 LYS B 162
REMARK 465 TYR B 163
REMARK 465 ASP B 164
REMARK 465 ASP B 165
REMARK 465 ASN B 257
REMARK 465 GLY B 258
REMARK 465 ARG B 259
REMARK 465 TYR B 260
REMARK 465 GLY B 261
REMARK 465 ARG B 262
REMARK 465 GLY B 473
REMARK 465 ASP B 474
REMARK 465 ARG B 475
REMARK 465 SER B 476
REMARK 465 GLN B 477
REMARK 465 ARG B 478
REMARK 465 ASP B 479
REMARK 465 ARG B 480
REMARK 465 HIS B 578
REMARK 465 HIS B 579
REMARK 465 TYR B 580
REMARK 465 LYS B 581
REMARK 465 GLY B 582
REMARK 465 SER B 583
REMARK 465 SER B 584
REMARK 465 GLU A 133
REMARK 465 GLY A 154
REMARK 465 ASN A 155
REMARK 465 THR A 156
REMARK 465 GLY A 157
REMARK 465 ILE A 158
REMARK 465 ASN A 159
REMARK 465 PHE A 160
REMARK 465 GLU A 161
REMARK 465 LYS A 162
REMARK 465 TYR A 163
REMARK 465 ASN A 257
REMARK 465 GLY A 258
REMARK 465 ARG A 259
REMARK 465 TYR A 260
REMARK 465 HIS A 578
REMARK 465 HIS A 579
REMARK 465 TYR A 580
REMARK 465 LYS A 581
REMARK 465 GLY A 582
REMARK 465 SER A 583
REMARK 465 SER A 584
REMARK 465 GLU C 133
REMARK 465 GLY C 154
REMARK 465 ASN C 155
REMARK 465 THR C 156
REMARK 465 GLY C 157
REMARK 465 ILE C 158
REMARK 465 ASN C 159
REMARK 465 PHE C 160
REMARK 465 GLU C 161
REMARK 465 LYS C 162
REMARK 465 TYR C 163
REMARK 465 ASP C 164
REMARK 465 GLU C 256
REMARK 465 ASN C 257
REMARK 465 GLY C 258
REMARK 465 ARG C 259
REMARK 465 TYR C 260
REMARK 465 GLY C 261
REMARK 465 ARG C 262
REMARK 465 TYR C 576
REMARK 465 GLU C 577
REMARK 465 HIS C 578
REMARK 465 HIS C 579
REMARK 465 TYR C 580
REMARK 465 LYS C 581
REMARK 465 GLY C 582
REMARK 465 SER C 583
REMARK 465 SER C 584
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 ND2 ASN A 436 OH TYR A 466 1.99
REMARK 500 O LEU B 484 N ARG B 488 2.01
REMARK 500
REMARK 500 REMARK: NULL
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 GLU B 482 CB GLU B 482 CG -0.125
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 THR B 201 -68.60 -102.04
REMARK 500 ASP B 368 -140.84 -125.36
REMARK 500 VAL B 375 -61.22 -102.10
REMARK 500 GLU B 399 58.15 39.72
REMARK 500 VAL B 405 47.66 -96.72
REMARK 500 GLU B 413 -26.62 75.82
REMARK 500 ASP B 441 -26.20 71.23
REMARK 500 GLU B 482 60.31 140.22
REMARK 500 ARG A 199 26.80 41.02
REMARK 500 THR A 201 -88.06 -120.00
REMARK 500 MET A 254 31.60 -155.23
REMARK 500 ARG A 262 74.90 -115.36
REMARK 500 ASP A 368 -139.64 -119.40
REMARK 500 PRO C 167 128.60 -38.48
REMARK 500 ASP C 368 -133.89 -114.17
REMARK 500 VAL C 375 -61.75 -102.84
REMARK 500 GLU C 413 -24.12 70.53
REMARK 500 LYS C 440 -11.34 72.69
REMARK 500 ASN C 509 87.08 -36.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU B 481 GLU B 482 -131.71
REMARK 500 SER C 508 ASN C 509 -127.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E7M RELATED DB: PDB
REMARK 900 RELATED ID: 5E7J RELATED DB: PDB
DBREF 5E7I B 133 584 UNP O00571 DDX3X_HUMAN 133 584
DBREF 5E7I A 133 584 UNP O00571 DDX3X_HUMAN 133 584
DBREF 5E7I C 133 584 UNP O00571 DDX3X_HUMAN 133 584
SEQRES 1 B 452 GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU ARG
SEQRES 2 B 452 LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY ILE
SEQRES 3 B 452 ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA THR
SEQRES 4 B 452 GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER ASP
SEQRES 5 B 452 VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU LEU
SEQRES 6 B 452 THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS ALA
SEQRES 7 B 452 ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA CYS
SEQRES 8 B 452 ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU LEU
SEQRES 9 B 452 PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY GLU
SEQRES 10 B 452 ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY ARG
SEQRES 11 B 452 ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO THR
SEQRES 12 B 452 ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG LYS
SEQRES 13 B 452 PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL TYR
SEQRES 14 B 452 GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU GLU
SEQRES 15 B 452 ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG LEU
SEQRES 16 B 452 VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP PHE
SEQRES 17 B 452 CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET LEU
SEQRES 18 B 452 ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL GLU
SEQRES 19 B 452 GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR MET
SEQRES 20 B 452 MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET LEU
SEQRES 21 B 452 ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA VAL
SEQRES 22 B 452 GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN LYS
SEQRES 23 B 452 VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE LEU
SEQRES 24 B 452 LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU THR
SEQRES 25 B 452 LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER LEU
SEQRES 26 B 452 GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR SER
SEQRES 27 B 452 ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU ALA
SEQRES 28 B 452 LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU VAL
SEQRES 29 B 452 ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER ASN
SEQRES 30 B 452 VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP ILE
SEQRES 31 B 452 GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG VAL
SEQRES 32 B 452 GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU ARG
SEQRES 33 B 452 ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU VAL
SEQRES 34 B 452 GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN MET
SEQRES 35 B 452 ALA TYR GLU HIS HIS TYR LYS GLY SER SER
SEQRES 1 A 452 GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU ARG
SEQRES 2 A 452 LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY ILE
SEQRES 3 A 452 ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA THR
SEQRES 4 A 452 GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER ASP
SEQRES 5 A 452 VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU LEU
SEQRES 6 A 452 THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS ALA
SEQRES 7 A 452 ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA CYS
SEQRES 8 A 452 ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU LEU
SEQRES 9 A 452 PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY GLU
SEQRES 10 A 452 ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY ARG
SEQRES 11 A 452 ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO THR
SEQRES 12 A 452 ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG LYS
SEQRES 13 A 452 PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL TYR
SEQRES 14 A 452 GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU GLU
SEQRES 15 A 452 ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG LEU
SEQRES 16 A 452 VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP PHE
SEQRES 17 A 452 CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET LEU
SEQRES 18 A 452 ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL GLU
SEQRES 19 A 452 GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR MET
SEQRES 20 A 452 MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET LEU
SEQRES 21 A 452 ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA VAL
SEQRES 22 A 452 GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN LYS
SEQRES 23 A 452 VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE LEU
SEQRES 24 A 452 LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU THR
SEQRES 25 A 452 LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER LEU
SEQRES 26 A 452 GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR SER
SEQRES 27 A 452 ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU ALA
SEQRES 28 A 452 LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU VAL
SEQRES 29 A 452 ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER ASN
SEQRES 30 A 452 VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP ILE
SEQRES 31 A 452 GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG VAL
SEQRES 32 A 452 GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU ARG
SEQRES 33 A 452 ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU VAL
SEQRES 34 A 452 GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN MET
SEQRES 35 A 452 ALA TYR GLU HIS HIS TYR LYS GLY SER SER
SEQRES 1 C 452 GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU ARG
SEQRES 2 C 452 LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY ILE
SEQRES 3 C 452 ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA THR
SEQRES 4 C 452 GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER ASP
SEQRES 5 C 452 VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU LEU
SEQRES 6 C 452 THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS ALA
SEQRES 7 C 452 ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA CYS
SEQRES 8 C 452 ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU LEU
SEQRES 9 C 452 PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY GLU
SEQRES 10 C 452 ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY ARG
SEQRES 11 C 452 ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO THR
SEQRES 12 C 452 ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG LYS
SEQRES 13 C 452 PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL TYR
SEQRES 14 C 452 GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU GLU
SEQRES 15 C 452 ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG LEU
SEQRES 16 C 452 VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP PHE
SEQRES 17 C 452 CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET LEU
SEQRES 18 C 452 ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL GLU
SEQRES 19 C 452 GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR MET
SEQRES 20 C 452 MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET LEU
SEQRES 21 C 452 ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA VAL
SEQRES 22 C 452 GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN LYS
SEQRES 23 C 452 VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE LEU
SEQRES 24 C 452 LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU THR
SEQRES 25 C 452 LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER LEU
SEQRES 26 C 452 GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR SER
SEQRES 27 C 452 ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU ALA
SEQRES 28 C 452 LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU VAL
SEQRES 29 C 452 ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER ASN
SEQRES 30 C 452 VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP ILE
SEQRES 31 C 452 GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG VAL
SEQRES 32 C 452 GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU ARG
SEQRES 33 C 452 ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU VAL
SEQRES 34 C 452 GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN MET
SEQRES 35 C 452 ALA TYR GLU HIS HIS TYR LYS GLY SER SER
HELIX 1 AA1 SER B 143 SER B 152 1 10
HELIX 2 AA2 SER B 181 VAL B 185 5 5
HELIX 3 AA3 MET B 187 THR B 198 1 12
HELIX 4 AA4 THR B 204 GLU B 216 1 13
HELIX 5 AA5 GLY B 229 ASP B 245 1 17
HELIX 6 AA6 GLY B 248 MET B 254 1 7
HELIX 7 AA7 THR B 275 SER B 290 1 16
HELIX 8 AA8 ASP B 305 GLU B 314 1 10
HELIX 9 AA9 THR B 323 ARG B 333 1 11
HELIX 10 AB1 GLU B 348 MET B 355 1 8
HELIX 11 AB2 PHE B 357 GLU B 366 1 10
HELIX 12 AB3 PRO B 386 LEU B 397 1 12
HELIX 13 AB4 GLU B 423 SER B 425 5 3
HELIX 14 AB5 ASP B 426 ALA B 437 1 12
HELIX 15 AB6 THR B 450 GLU B 464 1 15
HELIX 16 AB7 LEU B 484 GLY B 490 1 7
HELIX 17 AB8 ASP B 521 GLY B 530 1 10
HELIX 18 AB9 ASN B 546 ASN B 551 5 6
HELIX 19 AC1 ILE B 552 ALA B 563 1 12
HELIX 20 AC2 TRP B 570 TYR B 576 1 7
HELIX 21 AC3 ARG A 145 SER A 152 1 8
HELIX 22 AC4 MET A 187 THR A 198 1 12
HELIX 23 AC5 THR A 204 GLU A 216 1 13
HELIX 24 AC6 GLY A 229 GLY A 246 1 18
HELIX 25 AC7 GLY A 248 ALA A 253 1 6
HELIX 26 AC8 THR A 275 SER A 290 1 16
HELIX 27 AC9 ASP A 305 GLU A 314 1 10
HELIX 28 AD1 THR A 323 ARG A 333 1 11
HELIX 29 AD2 GLU A 348 MET A 355 1 8
HELIX 30 AD3 PHE A 357 GLN A 367 1 11
HELIX 31 AD4 PRO A 386 LEU A 397 1 12
HELIX 32 AD5 GLU A 423 SER A 425 5 3
HELIX 33 AD6 ASP A 426 THR A 438 1 13
HELIX 34 AD7 THR A 450 GLU A 464 1 15
HELIX 35 AD8 SER A 476 SER A 489 1 14
HELIX 36 AD9 THR A 498 ARG A 503 1 6
HELIX 37 AE1 ASP A 521 GLY A 530 1 10
HELIX 38 AE2 ASN A 546 ASN A 551 5 6
HELIX 39 AE3 ILE A 552 ALA A 563 1 12
HELIX 40 AE4 PRO A 568 GLU A 577 1 10
HELIX 41 AE5 SER C 143 PHE C 151 1 9
HELIX 42 AE6 SER C 181 VAL C 185 5 5
HELIX 43 AE7 GLY C 188 THR C 198 1 11
HELIX 44 AE8 THR C 204 GLU C 216 1 13
HELIX 45 AE9 GLY C 229 GLY C 246 1 18
HELIX 46 AF1 GLY C 248 ALA C 253 1 6
HELIX 47 AF2 THR C 275 SER C 290 1 16
HELIX 48 AF3 ASP C 305 ARG C 315 1 11
HELIX 49 AF4 THR C 323 ARG C 333 1 11
HELIX 50 AF5 GLU C 348 MET C 355 1 8
HELIX 51 AF6 PHE C 357 GLN C 367 1 11
HELIX 52 AF7 PRO C 386 LEU C 397 1 12
HELIX 53 AF8 GLU C 423 SER C 425 5 3
HELIX 54 AF9 ASP C 426 THR C 438 1 13
HELIX 55 AG1 THR C 450 GLU C 464 1 15
HELIX 56 AG2 SER C 476 SER C 489 1 14
HELIX 57 AG3 ASP C 521 GLY C 530 1 10
HELIX 58 AG4 ASN C 546 ASN C 551 5 6
HELIX 59 AG5 ILE C 552 ALA C 563 1 12
SHEET 1 AA1 8 GLU B 169 THR B 171 0
SHEET 2 AA1 8 ILE B 401 ALA B 404 -1 O PHE B 402 N THR B 171
SHEET 3 AA1 8 LEU B 220 CYS B 223 1 N CYS B 223 O LEU B 403
SHEET 4 AA1 8 HIS B 377 PHE B 381 1 O MET B 380 N LEU B 220
SHEET 5 AA1 8 TYR B 343 LEU B 346 1 N LEU B 346 O PHE B 381
SHEET 6 AA1 8 SER B 269 LEU B 272 1 N LEU B 270 O TYR B 343
SHEET 7 AA1 8 LEU B 319 ALA B 322 1 O LEU B 320 N VAL B 271
SHEET 8 AA1 8 PRO B 297 VAL B 300 1 N CYS B 298 O VAL B 321
SHEET 1 AA2 6 ILE B 415 TRP B 421 0
SHEET 2 AA2 6 GLY B 539 PHE B 545 1 O ALA B 541 N LYS B 418
SHEET 3 AA2 6 HIS B 512 ASN B 515 1 N VAL B 513 O LEU B 540
SHEET 4 AA2 6 THR B 444 PHE B 447 1 N LEU B 445 O ILE B 514
SHEET 5 AA2 6 ILE B 494 ALA B 497 1 O LEU B 495 N VAL B 446
SHEET 6 AA2 6 CYS B 468 ILE B 471 1 N THR B 469 O VAL B 496
SHEET 1 AA3 8 GLU A 169 THR A 171 0
SHEET 2 AA3 8 ILE A 401 ALA A 404 -1 O ALA A 404 N GLU A 169
SHEET 3 AA3 8 LEU A 220 CYS A 223 1 N CYS A 223 O LEU A 403
SHEET 4 AA3 8 HIS A 377 PHE A 381 1 O MET A 380 N LEU A 220
SHEET 5 AA3 8 TYR A 343 LEU A 346 1 N LEU A 344 O HIS A 377
SHEET 6 AA3 8 SER A 269 LEU A 272 1 N LEU A 272 O VAL A 345
SHEET 7 AA3 8 LEU A 319 ALA A 322 1 O LEU A 320 N VAL A 271
SHEET 8 AA3 8 PRO A 297 VAL A 300 1 N CYS A 298 O VAL A 321
SHEET 1 AA4 6 ILE A 415 TRP A 421 0
SHEET 2 AA4 6 GLY A 539 PHE A 545 1 O ALA A 541 N THR A 416
SHEET 3 AA4 6 HIS A 512 ASN A 515 1 N VAL A 513 O LEU A 540
SHEET 4 AA4 6 THR A 444 PHE A 447 1 N LEU A 445 O ILE A 514
SHEET 5 AA4 6 ILE A 494 ALA A 497 1 O LEU A 495 N VAL A 446
SHEET 6 AA4 6 CYS A 468 ILE A 471 1 N THR A 469 O VAL A 496
SHEET 1 AA5 8 GLU C 169 THR C 171 0
SHEET 2 AA5 8 ILE C 401 ALA C 404 -1 O PHE C 402 N THR C 171
SHEET 3 AA5 8 LEU C 220 CYS C 223 1 N CYS C 223 O LEU C 403
SHEET 4 AA5 8 HIS C 377 SER C 382 1 O MET C 380 N LEU C 220
SHEET 5 AA5 8 TYR C 343 LEU C 346 1 N LEU C 344 O HIS C 377
SHEET 6 AA5 8 SER C 269 LEU C 272 1 N LEU C 272 O VAL C 345
SHEET 7 AA5 8 LEU C 319 ALA C 322 1 O LEU C 320 N VAL C 271
SHEET 8 AA5 8 PRO C 297 VAL C 300 1 N CYS C 298 O VAL C 321
SHEET 1 AA6 6 THR C 416 TRP C 421 0
SHEET 2 AA6 6 LEU C 540 PHE C 545 1 O ALA C 541 N LYS C 418
SHEET 3 AA6 6 HIS C 512 ASN C 515 1 N ASN C 515 O THR C 542
SHEET 4 AA6 6 THR C 444 VAL C 448 1 N LEU C 445 O ILE C 514
SHEET 5 AA6 6 ILE C 494 THR C 498 1 O LEU C 495 N VAL C 446
SHEET 6 AA6 6 CYS C 468 ILE C 471 1 N THR C 469 O VAL C 496
CRYST1 92.710 105.380 94.610 90.00 114.54 90.00 P 1 21 1 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 0.010786 0.000000 0.004926 0.00000
SCALE2 0.000000 0.009489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
