Header list of 1r4k.pdb file
Complete list - 2 20 Bytes
HEADER RNA BINDING PROTEIN 07-OCT-03 1R4K
TITLE SOLUTION STRUCTURE OF THE DROSOPHILA ARGONAUTE 1 PAZ DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARGONAUTE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAZ DOMAIN;
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: AGO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS BETA BARREL, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR K.S.YAN,S.YAN,A.FAROOQ,A.HAN,L.ZENG,M.-M.ZHOU
REVDAT 3 02-MAR-22 1R4K 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1R4K 1 VERSN
REVDAT 1 09-DEC-03 1R4K 0
JRNL AUTH K.S.YAN,S.YAN,A.FAROOQ,A.HAN,L.ZENG,M.-M.ZHOU
JRNL TITL STRUCTURE AND CONSERVED RNA BINDING OF THE PAZ DOMAIN
JRNL REF NATURE V. 426 468 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 14615802
JRNL DOI 10.1038/NATURE02129
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020428.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM SODIUM PHOSPHATE, 150MM
REMARK 210 NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM AGO1 PAZ DOMAIN, 100MM
REMARK 210 SODIUM PHOSPHATE, 150MM NACL,
REMARK 210 5MM DTT-D10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, NMRPIPE 3.1,
REMARK 210 NMRVIEW 5.0, X-PLOR 3.1, ARIA 1.2
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 296
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 ALA A 302 -84.20 -171.81
REMARK 500 GLN A 303 87.57 48.37
REMARK 500 ASP A 314 93.72 50.79
REMARK 500 ILE A 337 -133.06 -69.11
REMARK 500 LYS A 338 94.02 62.99
REMARK 500 HIS A 346 -40.17 -150.44
REMARK 500 GLN A 349 -43.91 -146.93
REMARK 500 MET A 350 -61.32 -102.29
REMARK 500 ARG A 351 148.80 60.41
REMARK 500 CYS A 357 -38.72 -144.61
REMARK 500 ASN A 358 -172.75 -174.62
REMARK 500 LYS A 385 -44.16 -156.98
REMARK 500 LEU A 395 -65.97 62.41
REMARK 500 TYR A 397 45.74 -144.77
REMARK 500 HIS A 409 35.61 -148.98
REMARK 500 HIS A 411 57.70 -151.75
REMARK 500 GLU A 417 -165.38 -59.43
REMARK 500 VAL A 418 -69.41 66.04
REMARK 500 ALA A 423 35.79 -177.61
REMARK 500 GLN A 425 72.87 -102.21
REMARK 500 ILE A 428 -166.74 -113.99
REMARK 500 THR A 432 -160.35 -167.95
REMARK 500 LYS A 441 -172.00 52.14
REMARK 500 SER A 446 -177.09 52.73
REMARK 500 ARG A 452 99.45 -59.61
REMARK 500 GLU A 453 70.96 -68.09
REMARK 500 ASN A 456 176.61 53.22
REMARK 500 LEU A 457 177.42 52.98
REMARK 500 VAL A 458 34.07 -161.21
REMARK 500 LYS A 459 171.68 55.20
REMARK 500 ASP A 462 174.72 53.95
REMARK 500 PHE A 463 -60.29 -104.99
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R4K A 297 464 UNP Q9V6V6 Q9V6V6_DROME 331 498
SEQADV 1R4K GLY A 296 UNP Q9V6V6 CLONING ARTIFACT
SEQRES 1 A 169 GLY THR ALA PHE TYR LYS ALA GLN PRO VAL ILE ASP PHE
SEQRES 2 A 169 MET CYS GLU VAL LEU ASP ILE ARG ASP ILE ASN GLU GLN
SEQRES 3 A 169 ARG LYS PRO LEU THR ASP SER GLN ARG VAL LYS PHE THR
SEQRES 4 A 169 LYS GLU ILE LYS GLY LEU LYS ILE GLU ILE THR HIS CYS
SEQRES 5 A 169 GLY GLN MET ARG ARG LYS TYR ARG VAL CYS ASN VAL THR
SEQRES 6 A 169 ARG ARG PRO ALA GLN MET GLN SER PHE PRO LEU GLN LEU
SEQRES 7 A 169 GLU ASN GLY GLN THR VAL GLU CYS THR VAL ALA LYS TYR
SEQRES 8 A 169 PHE LEU ASP LYS TYR ARG MET LYS LEU ARG TYR PRO HIS
SEQRES 9 A 169 LEU PRO CYS LEU GLN VAL GLY GLN GLU HIS LYS HIS THR
SEQRES 10 A 169 TYR LEU PRO LEU GLU VAL CYS ASN ILE VAL ALA GLY GLN
SEQRES 11 A 169 ARG CYS ILE LYS LYS LEU THR ASP MET GLN THR SER THR
SEQRES 12 A 169 MET ILE LYS ALA THR ALA ARG SER ALA PRO ASP ARG GLU
SEQRES 13 A 169 ARG GLU ILE ASN ASN LEU VAL LYS ARG ALA ASP PHE ASN
HELIX 1 1 PRO A 304 LEU A 313 1 10
HELIX 2 2 THR A 326 ILE A 337 1 12
HELIX 3 3 PRO A 363 MET A 366 5 4
HELIX 4 4 LYS A 385 LYS A 390 1 6
SHEET 1 A 3 ARG A 352 ARG A 355 0
SHEET 2 A 3 LYS A 341 THR A 345 -1 N ILE A 342 O TYR A 354
SHEET 3 A 3 VAL A 418 VAL A 422 -1 O ASN A 420 N GLU A 343
SHEET 1 B 3 ASN A 358 THR A 360 0
SHEET 2 B 3 CYS A 402 VAL A 405 -1 O GLN A 404 N ASN A 358
SHEET 3 B 3 THR A 412 LEU A 414 -1 O LEU A 414 N LEU A 403
SHEET 1 C 2 GLN A 367 LEU A 373 0
SHEET 2 C 2 GLN A 377 VAL A 383 -1 O VAL A 379 N LEU A 371
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 2 20 Bytes