HEADER HYDROLASE 12-OCT-15 5E7J
TITLE CRYSTAL STRUCTURE OF THE ACTIVE CATALYTIC CORE OF THE HUMAN DEAD-BOX
TITLE 2 PROTEIN DDX3 BOUND TO AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DEAD BOX PROTEIN 3,X-CHROMOSOMAL,DEAD BOX,X ISOFORM,
COMPND 5 HELICASE-LIKE PROTEIN 2,HLP2;
COMPND 6 EC: 3.6.4.13;
COMPND 7 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 4 06-MAR-24 5E7J 1 JRNL REMARK
REVDAT 3 10-FEB-16 5E7J 1 JRNL
REVDAT 2 09-DEC-15 5E7J 1 JRNL
REVDAT 1 02-DEC-15 5E7J 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. 2.23 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) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 24005
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1200
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 69.0402 - 4.6365 0.99 2780 147 0.1809 0.2090
REMARK 3 2 4.6365 - 3.6802 0.98 2632 138 0.1869 0.2277
REMARK 3 3 3.6802 - 3.2150 0.99 2620 138 0.2213 0.2535
REMARK 3 4 3.2150 - 2.9210 1.00 2636 139 0.2552 0.3491
REMARK 3 5 2.9210 - 2.7117 1.00 2589 136 0.2626 0.2605
REMARK 3 6 2.7117 - 2.5518 0.99 2605 137 0.2753 0.3041
REMARK 3 7 2.5518 - 2.4240 1.00 2601 137 0.2829 0.3053
REMARK 3 8 2.4240 - 2.3185 0.98 2528 133 0.2864 0.2992
REMARK 3 9 2.3185 - 2.2292 0.70 1814 95 0.4394 0.4476
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.40
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 : 0.003 3514
REMARK 3 ANGLE : 0.790 4749
REMARK 3 CHIRALITY : 0.027 525
REMARK 3 PLANARITY : 0.003 617
REMARK 3 DIHEDRAL : 13.549 1337
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 5E7J 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_1000214492.
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24117
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 69.007
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 49.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, 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 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 25.67500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.82500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.95500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.82500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.67500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.95500
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 TOTAL BURIED SURFACE AREA: 540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 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 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 ASP A 164
REMARK 465 ASP A 165
REMARK 465 GLU A 256
REMARK 465 ASN A 257
REMARK 465 GLY A 258
REMARK 465 ARG A 259
REMARK 465 TYR A 260
REMARK 465 GLY A 261
REMARK 465 ARG A 262
REMARK 465 ARG A 263
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 266 OG SER A 569 2375 2.19
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 A 143 104.44 -166.98
REMARK 500 SER A 152 59.44 -113.55
REMARK 500 ASP A 368 -139.85 -115.90
REMARK 500 ASN A 509 113.70 -34.73
REMARK 500 ARG A 534 -101.09 -127.00
REMARK 500 VAL A 535 -47.80 -142.92
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 SER A 508 ASN A 509 -146.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP A 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E7M RELATED DB: PDB
REMARK 900 RELATED ID: 5E7I RELATED DB: PDB
DBREF 5E7J A 133 584 UNP O00571 DDX3X_HUMAN 133 584
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
HET AMP A 801 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 2 AMP C10 H14 N5 O7 P
HELIX 1 AA1 SER A 143 SER A 152 1 10
HELIX 2 AA2 SER A 181 VAL A 185 5 5
HELIX 3 AA3 GLY A 188 THR A 198 1 11
HELIX 4 AA4 THR A 204 GLU A 216 1 13
HELIX 5 AA5 GLY A 229 GLY A 246 1 18
HELIX 6 AA6 GLY A 248 ALA A 253 1 6
HELIX 7 AA7 THR A 275 SER A 290 1 16
HELIX 8 AA8 ASP A 305 ARG A 315 1 11
HELIX 9 AA9 THR A 323 ARG A 333 1 11
HELIX 10 AB1 GLU A 348 MET A 355 1 8
HELIX 11 AB2 PHE A 357 GLN A 367 1 11
HELIX 12 AB3 PRO A 386 LEU A 397 1 12
HELIX 13 AB4 GLU A 423 SER A 425 5 3
HELIX 14 AB5 ASP A 426 ASN A 436 1 11
HELIX 15 AB6 THR A 450 GLU A 464 1 15
HELIX 16 AB7 SER A 476 SER A 489 1 14
HELIX 17 AB8 ALA A 499 ARG A 503 1 5
HELIX 18 AB9 ASP A 521 GLY A 530 1 10
HELIX 19 AC1 ASN A 546 ASN A 551 5 6
HELIX 20 AC2 ILE A 552 ALA A 563 1 12
HELIX 21 AC3 PRO A 568 TYR A 576 1 9
HELIX 22 AC4 GLU A 577 LYS A 581 5 5
SHEET 1 AA1 8 VAL A 168 THR A 171 0
SHEET 2 AA1 8 ILE A 401 VAL A 405 -1 O PHE A 402 N THR A 171
SHEET 3 AA1 8 LEU A 220 CYS A 223 1 N CYS A 223 O LEU A 403
SHEET 4 AA1 8 HIS A 377 PHE A 381 1 O MET A 380 N ALA A 222
SHEET 5 AA1 8 TYR A 343 ASP A 347 1 N LEU A 346 O PHE A 381
SHEET 6 AA1 8 SER A 269 LEU A 272 1 N LEU A 270 O TYR A 343
SHEET 7 AA1 8 LEU A 319 ALA A 322 1 O LEU A 320 N VAL A 271
SHEET 8 AA1 8 PRO A 297 VAL A 300 1 N CYS A 298 O VAL A 321
SHEET 1 AA2 6 ILE A 415 TRP A 421 0
SHEET 2 AA2 6 GLY A 539 PHE A 545 1 O ALA A 541 N THR A 416
SHEET 3 AA2 6 HIS A 512 ASN A 515 1 N ASN A 515 O THR A 542
SHEET 4 AA2 6 THR A 444 VAL A 448 1 N LEU A 445 O ILE A 514
SHEET 5 AA2 6 ILE A 494 THR A 498 1 O LEU A 495 N VAL A 446
SHEET 6 AA2 6 CYS A 468 ILE A 471 1 N THR A 469 O VAL A 496
SITE 1 AC1 10 TYR A 200 ARG A 202 THR A 204 GLN A 207
SITE 2 AC1 10 THR A 226 GLY A 227 SER A 228 GLY A 229
SITE 3 AC1 10 LYS A 230 THR A 231
CRYST1 51.350 89.910 107.650 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 0.019474 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009289 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
