Header list of 1pms.pdb file
Complete list - v 3 2 Bytes
HEADER SIGNAL TRANSDUCTION 18-FEB-97 1PMS
TITLE PLECKSTRIN HOMOLOGY DOMAIN OF SON OF SEVENLESS 1 (SOS1) WITH GLYCINE-
TITLE 2 SERINE ADDED TO THE N-TERMINUS, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOS 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN;
COMPND 5 SYNONYM: SON OF SEVENLESS;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-4T3
KEYWDS PLECKSTRIN, SON OF SEVENLESS, SIGNAL TRANSDUCTION, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.KOSHIBA,T.KIGAWA,J.KIM,M.SHIROUZU,D.BOWTELL,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 03-NOV-21 1PMS 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PMS 1 VERSN
REVDAT 1 15-MAY-97 1PMS 0
JRNL AUTH S.KOSHIBA,T.KIGAWA,J.H.KIM,M.SHIROUZU,D.BOWTELL,S.YOKOYAMA
JRNL TITL THE SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
JRNL TITL 2 MOUSE SON-OF-SEVENLESS 1 (MSOS1).
JRNL REF J.MOL.BIOL. V. 269 579 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9217262
JRNL DOI 10.1006/JMBI.1997.1041
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS VIA A SIMULATED
REMARK 3 ANNEALING PROTOCOL USING NMR-DERIVED RESTRAINTS AND X-PLOR 3.1.
REMARK 3 RMSD BACKBONE HEAVY ATOMS (SECONDARY STRUCTURE ELEMENTS) 0.70 +/-
REMARK 3 0.34; ALL HEAVY ATOMS (SECONDARY STRUCTURE ELEMENTS) 1.24 +/-
REMARK 3 0.35.
REMARK 4
REMARK 4 1PMS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175742.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 430
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 LYS A 432 59.03 -94.84
REMARK 500 1 ASP A 447 -142.16 74.02
REMARK 500 1 CYS A 457 26.78 -154.24
REMARK 500 1 CYS A 458 32.76 -148.73
REMARK 500 1 ASN A 459 -113.55 -158.99
REMARK 500 1 GLU A 460 20.93 41.75
REMARK 500 1 PHE A 461 72.41 21.23
REMARK 500 1 THR A 468 -169.27 -112.04
REMARK 500 1 VAL A 470 -149.81 77.47
REMARK 500 1 PHE A 481 51.37 -95.75
REMARK 500 1 ASP A 482 28.10 41.18
REMARK 500 1 LYS A 489 148.46 176.10
REMARK 500 1 HIS A 492 51.53 -93.43
REMARK 500 1 SER A 502 141.80 172.36
REMARK 500 1 ARG A 506 174.32 179.98
REMARK 500 1 LEU A 507 173.64 -47.58
REMARK 500 1 LYS A 508 -80.82 -115.40
REMARK 500 1 ARG A 514 -37.02 -139.53
REMARK 500 1 ASP A 522 53.69 -118.87
REMARK 500 1 ASP A 523 -145.55 -78.98
REMARK 500 1 TYR A 527 -177.44 -178.21
REMARK 500 1 ALA A 530 -146.35 -97.81
REMARK 500 1 LYS A 546 45.14 -83.49
REMARK 500 1 ARG A 564 -84.19 -135.97
REMARK 500 2 MET A 439 -27.98 -39.75
REMARK 500 2 ASP A 447 -4.54 81.60
REMARK 500 2 LYS A 452 -155.64 -97.82
REMARK 500 2 ILE A 454 -32.28 -130.88
REMARK 500 2 CYS A 457 -71.61 -100.65
REMARK 500 2 ASN A 459 69.35 82.84
REMARK 500 2 GLU A 460 -150.40 -118.88
REMARK 500 2 PHE A 461 65.71 -119.08
REMARK 500 2 ARG A 469 41.69 -96.50
REMARK 500 2 VAL A 470 178.85 47.63
REMARK 500 2 ASP A 482 -89.00 57.93
REMARK 500 2 LYS A 489 54.07 -91.68
REMARK 500 2 GLN A 494 102.99 -42.66
REMARK 500 2 PRO A 495 -159.10 -77.45
REMARK 500 2 ALA A 500 -82.70 -68.81
REMARK 500 2 GLU A 504 108.87 60.72
REMARK 500 2 ARG A 506 -157.58 -100.15
REMARK 500 2 ASP A 522 42.78 -92.67
REMARK 500 2 ASP A 523 -169.69 -78.11
REMARK 500 2 HIS A 529 63.47 61.69
REMARK 500 2 ALA A 530 -152.38 -99.84
REMARK 500 2 LYS A 546 44.33 -83.09
REMARK 500 2 ARG A 564 -72.61 -116.83
REMARK 500 3 LYS A 432 53.89 -94.40
REMARK 500 3 ASP A 447 -41.36 81.98
REMARK 500 3 TRP A 449 90.71 36.06
REMARK 500
REMARK 500 THIS ENTRY HAS 526 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 1 ARG A 469 0.32 SIDE CHAIN
REMARK 500 1 ARG A 476 0.17 SIDE CHAIN
REMARK 500 1 ARG A 496 0.17 SIDE CHAIN
REMARK 500 1 ARG A 506 0.32 SIDE CHAIN
REMARK 500 1 ARG A 514 0.24 SIDE CHAIN
REMARK 500 1 ARG A 564 0.30 SIDE CHAIN
REMARK 500 2 ARG A 469 0.31 SIDE CHAIN
REMARK 500 2 ARG A 476 0.32 SIDE CHAIN
REMARK 500 2 ARG A 496 0.21 SIDE CHAIN
REMARK 500 2 ARG A 506 0.26 SIDE CHAIN
REMARK 500 2 ARG A 514 0.22 SIDE CHAIN
REMARK 500 2 ARG A 564 0.11 SIDE CHAIN
REMARK 500 3 ARG A 469 0.30 SIDE CHAIN
REMARK 500 3 ARG A 476 0.32 SIDE CHAIN
REMARK 500 3 ARG A 496 0.25 SIDE CHAIN
REMARK 500 3 ARG A 506 0.31 SIDE CHAIN
REMARK 500 3 ARG A 514 0.20 SIDE CHAIN
REMARK 500 3 ARG A 564 0.17 SIDE CHAIN
REMARK 500 4 ARG A 469 0.29 SIDE CHAIN
REMARK 500 4 ARG A 476 0.29 SIDE CHAIN
REMARK 500 4 ARG A 496 0.20 SIDE CHAIN
REMARK 500 4 ARG A 514 0.31 SIDE CHAIN
REMARK 500 5 ARG A 469 0.26 SIDE CHAIN
REMARK 500 5 ARG A 476 0.26 SIDE CHAIN
REMARK 500 5 ARG A 496 0.28 SIDE CHAIN
REMARK 500 5 ARG A 506 0.32 SIDE CHAIN
REMARK 500 5 ARG A 514 0.23 SIDE CHAIN
REMARK 500 5 ARG A 564 0.27 SIDE CHAIN
REMARK 500 6 ARG A 469 0.30 SIDE CHAIN
REMARK 500 6 ARG A 476 0.22 SIDE CHAIN
REMARK 500 6 ARG A 496 0.20 SIDE CHAIN
REMARK 500 6 ARG A 506 0.31 SIDE CHAIN
REMARK 500 6 ARG A 514 0.29 SIDE CHAIN
REMARK 500 6 ARG A 564 0.25 SIDE CHAIN
REMARK 500 7 ARG A 469 0.19 SIDE CHAIN
REMARK 500 7 ARG A 476 0.27 SIDE CHAIN
REMARK 500 7 ARG A 496 0.32 SIDE CHAIN
REMARK 500 7 ARG A 506 0.30 SIDE CHAIN
REMARK 500 7 ARG A 514 0.14 SIDE CHAIN
REMARK 500 7 ARG A 564 0.32 SIDE CHAIN
REMARK 500 8 ARG A 469 0.23 SIDE CHAIN
REMARK 500 8 ARG A 476 0.30 SIDE CHAIN
REMARK 500 8 ARG A 496 0.22 SIDE CHAIN
REMARK 500 8 ARG A 506 0.30 SIDE CHAIN
REMARK 500 8 ARG A 514 0.29 SIDE CHAIN
REMARK 500 9 ARG A 469 0.29 SIDE CHAIN
REMARK 500 9 ARG A 476 0.18 SIDE CHAIN
REMARK 500 9 ARG A 496 0.28 SIDE CHAIN
REMARK 500 9 ARG A 514 0.32 SIDE CHAIN
REMARK 500 9 ARG A 564 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 115 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MY_001000016.1 RELATED DB: TARGETDB
DBREF 1PMS A 430 565 UNP Q62245 SOS1_MOUSE 414 548
SEQADV 1PMS SER A 431 UNP Q62245 GLY 414 ENGINEERED MUTATION
SEQRES 1 A 136 GLY SER LYS GLN LEU ALA ILE LYS LYS MET ASN GLU ILE
SEQRES 2 A 136 GLN LYS ASN ILE ASP GLY TRP GLU GLY LYS ASP ILE GLY
SEQRES 3 A 136 GLN CYS CYS ASN GLU PHE ILE MET GLU GLY THR LEU THR
SEQRES 4 A 136 ARG VAL GLY ALA LYS HIS GLU ARG HIS ILE PHE LEU PHE
SEQRES 5 A 136 ASP GLY LEU MET ILE CYS CYS LYS SER ASN HIS GLY GLN
SEQRES 6 A 136 PRO ARG LEU PRO GLY ALA SER SER ALA GLU TYR ARG LEU
SEQRES 7 A 136 LYS GLU LYS PHE PHE MET ARG LYS VAL GLN ILE ASN ASP
SEQRES 8 A 136 LYS ASP ASP THR SER GLU TYR LYS HIS ALA PHE GLU ILE
SEQRES 9 A 136 ILE LEU LYS ASP GLY ASN SER VAL ILE PHE SER ALA LYS
SEQRES 10 A 136 SER ALA GLU GLU LYS ASN ASN TRP MET ALA ALA LEU ILE
SEQRES 11 A 136 SER LEU GLN TYR ARG SER
HELIX 1 A1 GLN A 433 GLN A 443 1 11
HELIX 2 A2 ALA A 548 GLN A 562 1 15
SHEET 1 SH1 4 MET A 463 THR A 468 0
SHEET 2 SH1 4 ARG A 476 PHE A 481 -1 O ARG A 476 N LEU A 467
SHEET 3 SH1 4 LEU A 484 CYS A 488 -1 N LEU A 484 O PHE A 481
SHEET 4 SH1 4 GLU A 509 PHE A 512 -1 N GLU A 509 O CYS A 487
SHEET 1 SH2 4 THR A 468 ARG A 469 0
SHEET 2 SH2 4 SER A 540 SER A 544 -1 N SER A 544 O THR A 468
SHEET 3 SH2 4 ALA A 530 ILE A 534 -1 N PHE A 531 O PHE A 543
SHEET 4 SH2 4 GLN A 517 ASP A 520 -1 O GLN A 517 N ILE A 534
SHEET 1 SH3 4 MET A 463 THR A 468 0
SHEET 2 SH3 4 ARG A 476 PHE A 481 -1 O ARG A 476 N LEU A 467
SHEET 3 SH3 4 LEU A 484 CYS A 488 -1 N LEU A 484 O PHE A 481
SHEET 4 SH3 4 GLU A 509 PHE A 512 -1 N GLU A 509 O CYS A 487
SHEET 1 SH4 4 THR A 468 ARG A 469 0
SHEET 2 SH4 4 SER A 540 SER A 544 -1 N SER A 544 O THR A 468
SHEET 3 SH4 4 ALA A 530 ILE A 534 -1 N PHE A 531 O PHE A 543
SHEET 4 SH4 4 GLN A 517 ASP A 520 -1 O GLN A 517 N ILE A 534
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 - v 3 2 Bytes