Header list of 2gw6.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 03-MAY-06 2GW6
TITLE NMR STRUCTURE OF THE HUMAN TRNA ENDONUCLEASE SEN15 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN15;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRNA-INTRON ENDONUCLEASE SEN15, HSSEN15;
COMPND 5 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: TSEN15, C1ORF19, SEN15;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVP13
KEYWDS SEN15_HUMAN, TRNA ENDONUCLEASE, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS,
KEYWDS 3 CESG, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.SONG,J.L.MARKLEY,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 4 09-MAR-22 2GW6 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GW6 1 VERSN
REVDAT 2 30-SEP-08 2GW6 1 JRNL
REVDAT 1 16-MAY-06 2GW6 0
JRNL AUTH J.SONG,J.L.MARKLEY
JRNL TITL THREE-DIMENSIONAL STRUCTURE DETERMINED FOR A SUBUNIT OF
JRNL TITL 2 HUMAN TRNA SPLICING ENDONUCLEASE (SEN15) REVEALS A NOVEL
JRNL TITL 3 DIMERIC FOLD.
JRNL REF J.MOL.BIOL. V. 366 155 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17166513
JRNL DOI 10.1016/J.JMB.2006.11.024
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 1.1, XPLOR-NIH 2.9.8
REMARK 3 AUTHORS : SCHWIETERS, C.D. ET AL. (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 4516 NOE RESTRAINTS (1704 INTRA, 1038 SEQUENTIAL, 802 MEDIUM,
REMARK 3 862 LONG RANGE INTERMOLECULAR AND 110 INTERMOLECULAR), 182 H BOND
REMARK 3 RESTRAINTS, AND 326 PHI AND PSI
REMARK 3 DIHEDRAL ANGLE CONSTRAINTS
REMARK 4
REMARK 4 2GW6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037622.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20 MM BIS-TRIS, 100MM NACL, 10
REMARK 210 MM DTT, 0.5 MM 13C, 15N-LABELED
REMARK 210 SEN15_HUMAN, 90% H2O, 10% D2O;
REMARK 210 20 MM BIS-TRIS,100MM NACL, 10 MM
REMARK 210 DTT, 0.5 MM 13C, 15N-LABELED
REMARK 210 SEN15_HUMAN, 0.5 MM UNLABELED
REMARK 210 SEN15_HUMAN, 90% H2O, 10% D2O;
REMARK 210 20 MM BIS-TRIS,100MM NACL, 10 MM
REMARK 210 DTT, 0.5 MM 15N-LABELED SEN15_
REMARK 210 HUMAN, 17MG/ML PF1 PHAGE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H,15N-HSQC; 1H,13C-HSQC;
REMARK 210 HNCACB; CBCACONH; CCONH;
REMARK 210 HCCHTOCSY; HBACONH; 13C-EDITED
REMARK 210 1H,1H-NOESY; 15C-EDITED 1H,1H-
REMARK 210 NOESY; 13C,15N FILTERED, 13C
REMARK 210 EDITED 1H,1H-NOESY; IPAP 1H,15N-
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE
REMARK 210 97.027.12.56, SPARKY 3.72, CYANA
REMARK 210 2.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,SIMULATED
REMARK 210 ANNEALING,DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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: DIMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 ASP A 3 26.06 -149.06
REMARK 500 1 THR A 8 0.93 176.37
REMARK 500 1 ASP A 19 21.34 -74.82
REMARK 500 1 SER A 41 104.91 53.42
REMARK 500 1 GLU A 66 -159.16 -86.19
REMARK 500 1 GLN A 69 116.46 -160.39
REMARK 500 1 ALA B 304 25.45 -150.86
REMARK 500 1 TRP B 305 -40.07 -135.00
REMARK 500 1 ASP B 319 39.56 -76.04
REMARK 500 1 SER B 341 81.15 29.08
REMARK 500 1 GLN B 354 14.95 80.19
REMARK 500 1 GLU B 366 -160.85 -103.57
REMARK 500 1 PRO B 399 92.20 -66.69
REMARK 500 1 ASP B 400 65.74 36.82
REMARK 500 1 SER B 414 -18.10 174.59
REMARK 500 2 THR A 8 -64.80 -151.09
REMARK 500 2 ASP A 19 -18.75 39.12
REMARK 500 2 ILE A 20 -67.30 -156.21
REMARK 500 2 GLN A 69 116.64 -166.27
REMARK 500 2 ASP A 100 94.11 53.84
REMARK 500 2 PRO A 102 109.89 -55.80
REMARK 500 2 SER A 114 -38.71 176.23
REMARK 500 2 THR A 115 107.13 -50.46
REMARK 500 2 LEU B 318 172.78 -58.62
REMARK 500 2 ASP B 319 -5.88 -40.06
REMARK 500 2 ILE B 320 -62.04 -152.61
REMARK 500 2 GLU B 366 -161.43 -101.62
REMARK 500 2 LEU B 368 112.77 -163.01
REMARK 500 2 GLN B 369 114.34 -168.38
REMARK 500 2 THR B 377 9.94 -69.45
REMARK 500 2 PRO B 399 99.60 -62.94
REMARK 500 2 ASP B 400 47.06 33.25
REMARK 500 2 MET B 403 -165.84 -119.16
REMARK 500 3 ASP A 3 32.13 -53.33
REMARK 500 3 THR A 8 -5.30 175.69
REMARK 500 3 ASP A 19 35.17 -69.26
REMARK 500 3 ILE A 20 -60.03 -162.53
REMARK 500 3 SER A 41 72.72 39.28
REMARK 500 3 GLN A 69 117.90 -165.44
REMARK 500 3 ASP A 100 35.31 -49.73
REMARK 500 3 MET A 103 -167.99 -112.46
REMARK 500 3 SER A 114 16.35 161.64
REMARK 500 3 ASP B 319 39.47 -71.00
REMARK 500 3 ILE B 320 -54.75 -170.60
REMARK 500 3 SER B 341 73.32 37.36
REMARK 500 3 MET B 403 -153.16 -127.92
REMARK 500 3 SER B 414 0.64 164.48
REMARK 500 4 THR A 8 -46.47 99.19
REMARK 500 4 GLU A 66 -157.08 -86.16
REMARK 500 4 GLN A 69 118.77 -166.12
REMARK 500
REMARK 500 THIS ENTRY HAS 348 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 4 ARG B 393 0.08 SIDE CHAIN
REMARK 500 7 ARG B 384 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.78856 RELATED DB: TARGETDB
DBREF 2GW6 A 2 123 UNP Q8WW01 SEN15_HUMAN 36 157
DBREF 2GW6 B 302 423 UNP Q8WW01 SEN15_HUMAN 36 157
SEQADV 2GW6 SER A 1 UNP Q8WW01 CLONING ARTIFACT
SEQADV 2GW6 SER B 301 UNP Q8WW01 CLONING ARTIFACT
SEQRES 1 A 123 SER GLU ASP ALA TRP MET GLY THR HIS PRO LYS TYR LEU
SEQRES 2 A 123 GLU MET MET GLU LEU ASP ILE GLY ASP ALA THR GLN VAL
SEQRES 3 A 123 TYR VAL ALA PHE LEU VAL TYR LEU ASP LEU MET GLU SER
SEQRES 4 A 123 LYS SER TRP HIS GLU VAL ASN CYS VAL GLY LEU PRO GLU
SEQRES 5 A 123 LEU GLN LEU ILE CYS LEU VAL GLY THR GLU ILE GLU GLY
SEQRES 6 A 123 GLU GLY LEU GLN THR VAL VAL PRO THR PRO ILE THR ALA
SEQRES 7 A 123 SER LEU SER HIS ASN ARG ILE ARG GLU ILE LEU LYS ALA
SEQRES 8 A 123 SER ARG LYS LEU GLN GLY ASP PRO ASP LEU PRO MET SER
SEQRES 9 A 123 PHE THR LEU ALA ILE VAL GLU SER ASP SER THR ILE VAL
SEQRES 10 A 123 TYR TYR LYS LEU THR ASP
SEQRES 1 B 123 SER GLU ASP ALA TRP MET GLY THR HIS PRO LYS TYR LEU
SEQRES 2 B 123 GLU MET MET GLU LEU ASP ILE GLY ASP ALA THR GLN VAL
SEQRES 3 B 123 TYR VAL ALA PHE LEU VAL TYR LEU ASP LEU MET GLU SER
SEQRES 4 B 123 LYS SER TRP HIS GLU VAL ASN CYS VAL GLY LEU PRO GLU
SEQRES 5 B 123 LEU GLN LEU ILE CYS LEU VAL GLY THR GLU ILE GLU GLY
SEQRES 6 B 123 GLU GLY LEU GLN THR VAL VAL PRO THR PRO ILE THR ALA
SEQRES 7 B 123 SER LEU SER HIS ASN ARG ILE ARG GLU ILE LEU LYS ALA
SEQRES 8 B 123 SER ARG LYS LEU GLN GLY ASP PRO ASP LEU PRO MET SER
SEQRES 9 B 123 PHE THR LEU ALA ILE VAL GLU SER ASP SER THR ILE VAL
SEQRES 10 B 123 TYR TYR LYS LEU THR ASP
HELIX 1 1 HIS A 9 GLU A 17 1 9
HELIX 2 2 ASP A 22 SER A 39 1 18
HELIX 3 3 HIS A 82 GLN A 96 1 15
HELIX 4 4 HIS B 309 GLU B 317 1 9
HELIX 5 5 ASP B 322 LYS B 340 1 19
HELIX 6 6 HIS B 382 GLY B 397 1 16
SHEET 1 A 6 GLU A 44 LEU A 50 0
SHEET 2 A 6 LEU A 55 THR A 61 -1 O CYS A 57 N VAL A 48
SHEET 3 A 6 THR A 70 PRO A 75 -1 O VAL A 71 N LEU A 58
SHEET 4 A 6 SER A 104 VAL A 110 1 O ALA A 108 N THR A 74
SHEET 5 A 6 ILE A 116 THR A 122 -1 O VAL A 117 N ILE A 109
SHEET 6 A 6 LEU B 380 SER B 381 1 O LEU B 380 N THR A 122
SHEET 1 B 6 SER A 79 SER A 81 0
SHEET 2 B 6 ILE B 416 THR B 422 1 O LYS B 420 N LEU A 80
SHEET 3 B 6 SER B 404 VAL B 410 -1 N LEU B 407 O TYR B 419
SHEET 4 B 6 LEU B 368 PRO B 375 1 N THR B 370 O THR B 406
SHEET 5 B 6 LEU B 355 THR B 361 -1 N LEU B 358 O VAL B 371
SHEET 6 B 6 GLU B 344 LEU B 350 -1 N VAL B 348 O CYS B 357
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
MODEL 1
Complete list - r 9 2 Bytes