Header list of 1yse.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 08-FEB-05 1YSE
TITLE SOLUTION STRUCTURE OF THE MAR-BINDING DOMAIN OF SATB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN SATB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MAR-BINDING DOMAIN;
COMPND 5 SYNONYM: SPECIAL AT-RICH SEQUENCE BINDING PROTEIN 1;
COMPND 6 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: SATB1;
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: PET15B
KEYWDS ALL HELICAL, DNA-BINDING DOMAIN, T-CELL DEVELOPMENT, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.YAMASAKI,H.YAMAGUCHI
REVDAT 5 02-MAR-22 1YSE 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1YSE 1 VERSN
REVDAT 3 28-FEB-06 1YSE 1 JRNL
REVDAT 2 17-JAN-06 1YSE 1 JRNL
REVDAT 1 03-JAN-06 1YSE 0
JRNL AUTH H.YAMAGUCHI,M.TATENO,K.YAMASAKI
JRNL TITL SOLUTION STRUCTURE AND DNA-BINDING MODE OF THE MATRIX
JRNL TITL 2 ATTACHMENT REGION-BINDING DOMAIN OF THE TRANSCRIPTION FACTOR
JRNL TITL 3 SATB1 THAT REGULATES THE T-CELL MATURATION
JRNL REF J.BIOL.CHEM. V. 281 5319 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16371359
JRNL DOI 10.1074/JBC.M510933200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1184 RESTRAINTS: 989 NOE-DERIVED DISTANCE CONSTRAINTS, 109
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,AND 86 DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS.
REMARK 4
REMARK 4 1YSE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031876.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM SATB1 MAR-BINDING DOMAIN,
REMARK 210 50MM PHOSPHATE BUFFER NA; 95%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 350
REMARK 465 SER A 351
REMARK 465 HIS A 352
REMARK 465 VAL A 353
REMARK 465 SER A 354
REMARK 465 ARG A 355
REMARK 465 SER A 356
REMARK 465 MET A 357
REMARK 465 ASN A 358
REMARK 465 LYS A 359
REMARK 465 PRO A 360
REMARK 465 LEU A 361
REMARK 465 GLU A 362
REMARK 465 GLN A 363
REMARK 465 GLN A 364
REMARK 465 VAL A 365
REMARK 465 SER A 366
REMARK 465 THR A 367
REMARK 465 SER A 456
REMARK 465 ALA A 457
REMARK 465 MET A 458
REMARK 465 GLY A 459
REMARK 465 PRO A 460
REMARK 465 ALA A 461
REMARK 465 PRO A 462
REMARK 465 LEU A 463
REMARK 465 ILE A 464
REMARK 465 SER A 465
REMARK 465 THR A 466
REMARK 465 PRO A 467
REMARK 465 PRO A 468
REMARK 465 SER A 469
REMARK 465 ARG A 470
REMARK 465 PRO A 471
REMARK 465 PRO A 472
REMARK 465 GLN A 473
REMARK 465 VAL A 474
REMARK 465 LYS A 475
REMARK 465 THR A 476
REMARK 465 ALA A 477
REMARK 465 THR A 478
REMARK 465 ILE A 479
REMARK 465 ALA A 480
REMARK 465 THR A 481
REMARK 465 GLU A 482
REMARK 465 ARG A 483
REMARK 465 ASN A 484
REMARK 465 GLY A 485
REMARK 465 LYS A 486
REMARK 465 PRO A 487
REMARK 465 GLU A 488
REMARK 465 ASN A 489
REMARK 465 ASN A 490
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 THR A 369 30.99 -145.97
REMARK 500 1 PHE A 398 89.26 -154.92
REMARK 500 1 ARG A 400 -72.14 -161.91
REMARK 500 1 ASP A 446 104.46 -59.23
REMARK 500 1 GLU A 447 -46.48 -131.14
REMARK 500 1 ARG A 450 52.70 -90.63
REMARK 500 1 SER A 451 106.01 -59.51
REMARK 500 2 THR A 369 -52.83 -151.10
REMARK 500 2 PHE A 398 111.38 -166.98
REMARK 500 2 GLU A 447 -46.87 -152.31
REMARK 500 3 ALA A 397 -72.24 -67.86
REMARK 500 3 ARG A 400 -74.62 -143.92
REMARK 500 3 GLU A 447 -43.46 -167.03
REMARK 500 4 THR A 369 31.04 -156.21
REMARK 500 4 ASN A 399 93.87 -59.60
REMARK 500 4 GLU A 413 98.63 -64.19
REMARK 500 4 ASP A 446 93.12 -59.58
REMARK 500 4 GLU A 447 -49.95 -153.16
REMARK 500 5 ALA A 397 -72.35 -66.13
REMARK 500 5 ARG A 400 -70.92 -154.24
REMARK 500 5 SER A 419 -178.17 -65.66
REMARK 500 5 ASP A 446 -174.32 -64.16
REMARK 500 6 ALA A 397 -76.11 -85.06
REMARK 500 6 ARG A 400 -70.22 -154.17
REMARK 500 6 ASN A 453 -59.08 -131.72
REMARK 500 7 ASN A 399 99.75 -56.33
REMARK 500 7 ARG A 400 -168.07 -169.39
REMARK 500 7 GLU A 449 -165.40 -60.91
REMARK 500 7 LEU A 452 36.76 -163.41
REMARK 500 8 THR A 369 160.27 59.75
REMARK 500 8 ASN A 399 109.08 -59.59
REMARK 500 8 THR A 417 32.17 -147.02
REMARK 500 8 GLU A 447 116.42 61.96
REMARK 500 9 ARG A 400 -71.37 -135.87
REMARK 500 9 SER A 451 -71.43 -54.43
REMARK 500 9 LEU A 452 90.17 -160.86
REMARK 500 10 ALA A 397 -70.29 -84.74
REMARK 500 10 ARG A 400 -172.45 -170.10
REMARK 500 10 ARG A 450 -74.51 -87.57
REMARK 500 10 ALA A 454 76.39 -100.09
REMARK 500 11 ARG A 400 -65.94 -159.59
REMARK 500 11 ARG A 450 30.76 -97.80
REMARK 500 11 LEU A 452 30.67 -143.20
REMARK 500 12 ARG A 400 -65.35 -146.21
REMARK 500 12 ASP A 446 30.67 -97.50
REMARK 500 12 ARG A 448 81.52 -64.41
REMARK 500 12 ALA A 454 -64.06 -90.97
REMARK 500 13 ARG A 400 -70.11 -141.92
REMARK 500 13 PRO A 415 46.49 -83.70
REMARK 500 13 ASN A 453 -73.62 -141.80
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YSE A 353 490 UNP Q01826 SATB1_HUMAN 353 490
SEQADV 1YSE GLY A 350 UNP Q01826 CLONING ARTIFACT
SEQADV 1YSE SER A 351 UNP Q01826 CLONING ARTIFACT
SEQADV 1YSE HIS A 352 UNP Q01826 CLONING ARTIFACT
SEQRES 1 A 141 GLY SER HIS VAL SER ARG SER MET ASN LYS PRO LEU GLU
SEQRES 2 A 141 GLN GLN VAL SER THR ASN THR GLU VAL SER SER GLU ILE
SEQRES 3 A 141 TYR GLN TRP VAL ARG ASP GLU LEU LYS ARG ALA GLY ILE
SEQRES 4 A 141 SER GLN ALA VAL PHE ALA ARG VAL ALA PHE ASN ARG THR
SEQRES 5 A 141 GLN GLY LEU LEU SER GLU ILE LEU ARG LYS GLU GLU ASP
SEQRES 6 A 141 PRO LYS THR ALA SER GLN SER LEU LEU VAL ASN LEU ARG
SEQRES 7 A 141 ALA MET GLN ASN PHE LEU GLN LEU PRO GLU ALA GLU ARG
SEQRES 8 A 141 ASP ARG ILE TYR GLN ASP GLU ARG GLU ARG SER LEU ASN
SEQRES 9 A 141 ALA ALA SER ALA MET GLY PRO ALA PRO LEU ILE SER THR
SEQRES 10 A 141 PRO PRO SER ARG PRO PRO GLN VAL LYS THR ALA THR ILE
SEQRES 11 A 141 ALA THR GLU ARG ASN GLY LYS PRO GLU ASN ASN
HELIX 1 1 SER A 373 GLY A 387 1 15
HELIX 2 2 SER A 389 PHE A 398 1 10
HELIX 3 3 GLY A 403 GLU A 412 1 10
HELIX 4 4 ASP A 414 ALA A 418 5 5
HELIX 5 5 SER A 419 LEU A 435 1 17
HELIX 6 6 PRO A 436 ASP A 446 1 11
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 2 2 Bytes