HEADER PROTEIN BINDING 29-SEP-10 2L42
TITLE THE SOLUTION STRUCTURE OF RAP1 BRCT DOMAIN FROM SACCHAROMYCES
TITLE 2 CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN RAP1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRCT DOMAIN, UNP RESIDUES 116-212;
COMPND 5 SYNONYM: REPRESSOR/ACTIVATOR SITE-BINDING PROTEIN, SBF-E, TUF;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: RAP1, GRF1, TUF1, YNL216W, N1310;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET22
KEYWDS RAP1, BRCT DOMAIN, DNA BINDING PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.ZHANG,J.ZHANG,X.TU
REVDAT 2 23-FEB-11 2L42 1 JRNL
REVDAT 1 26-JAN-11 2L42 0
JRNL AUTH W.ZHANG,J.ZHANG,X.ZHANG,C.XU,X.TU
JRNL TITL SOLUTION STRUCTURE OF RAP1 BRCT DOMAIN FROM SACCHAROMYCES
JRNL TITL 2 CEREVISIAE REVEALS A NOVEL FOLD
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 404 1055 2011
JRNL REFN ISSN 0006-291X
JRNL PMID 21187076
JRNL DOI 10.1016/J.BBRC.2010.12.109
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L42 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB101930.
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 : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM SODIUM PHOSPHATE-1, 100 MM
REMARK 210 SODIUM CHLORIDE-2, 90% H2O/10%
REMARK 210 D2O; 20 MM SODIUM PHOSPHATE-3,
REMARK 210 100 MM SODIUM CHLORIDE-4, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D C(CO)NH; 3D HNCO; 3D HNCACB;
REMARK 210 3D HBHA(CO)NH; 3D H(CCO)NH; 3D 1H
REMARK 210 -15N NOESY; 3D HCCH-COSY; 3D HCCH
REMARK 210 -TOCSY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS, SPARKY
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 MET A 0
REMARK 465 LEU A 98
REMARK 465 GLU A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
REMARK 465 HIS A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
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 OD1 ASN A 41 H GLY A 43 1.66
REMARK 500 O ILE A 76 H CYS A 80 1.72
REMARK 500 O THR A 70 H VAL A 93 1.77
REMARK 500 O ILE A 31 H ALA A 35 1.80
REMARK 500 O TYR A 75 H CYS A 79 1.82
REMARK 500 O ALA A 35 H ARG A 39 1.83
REMARK 500 O SER A 82 H SER A 84 1.93
REMARK 500 O ASN A 87 H ASN A 90 1.93
REMARK 500 O PHE A 16 H VAL A 60 2.00
REMARK 500 O ASP A 30 H GLN A 33 2.05
REMARK 500 O SER A 61 H ASN A 64 2.09
REMARK 500 O THR A 74 H LYS A 77 2.09
REMARK 500 O THR A 70 HA LEU A 92 2.10
REMARK 500 O ALA A 78 H SER A 82 2.16
REMARK 500 O ILE A 59 H VAL A 71 2.16
REMARK 500 O CYS A 79 HA ASN A 83 2.17
REMARK 500 O ILE A 31 HG LEU A 34 2.18
REMARK 500 O THR A 66 HD2 PRO A 69 2.19
REMARK 500 O PHE A 16 HG13 ILE A 59 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 1 GLN A 5 110.10 67.02
REMARK 500 1 VAL A 6 -51.26 -133.29
REMARK 500 1 SER A 12 102.22 61.60
REMARK 500 1 ASN A 13 -83.36 -142.73
REMARK 500 1 MET A 14 127.04 -179.39
REMARK 500 1 ARG A 20 -90.51 -68.01
REMARK 500 1 ASP A 21 44.11 174.45
REMARK 500 1 ALA A 24 156.68 168.63
REMARK 500 1 HIS A 25 -74.28 -174.11
REMARK 500 1 ASP A 26 -62.24 -143.63
REMARK 500 1 LEU A 28 -62.03 -135.67
REMARK 500 1 ARG A 51 34.60 -152.61
REMARK 500 1 THR A 66 105.00 49.60
REMARK 500 1 PRO A 69 -169.81 -74.29
REMARK 500 1 ASN A 83 -73.45 70.40
REMARK 500 1 SER A 84 36.16 -171.82
REMARK 500 1 LEU A 86 75.23 -156.67
REMARK 500 1 PRO A 94 165.27 -44.09
REMARK 500 2 LEU A 11 -163.03 -129.79
REMARK 500 2 ASN A 13 -73.46 -142.68
REMARK 500 2 MET A 14 136.52 -171.95
REMARK 500 2 LEU A 18 86.84 -157.60
REMARK 500 2 ASP A 23 -37.01 169.89
REMARK 500 2 ALA A 24 121.78 -170.72
REMARK 500 2 HIS A 25 -75.25 -125.15
REMARK 500 2 ASP A 26 -71.05 -163.83
REMARK 500 2 LEU A 28 -49.17 -146.94
REMARK 500 2 ARG A 51 -74.12 -124.49
REMARK 500 2 LYS A 54 24.20 -140.45
REMARK 500 2 THR A 66 99.10 57.96
REMARK 500 2 LEU A 68 -57.77 -132.92
REMARK 500 2 PRO A 69 -168.58 -72.23
REMARK 500 2 ASN A 83 -76.00 70.45
REMARK 500 2 SER A 84 37.24 -154.99
REMARK 500 2 LEU A 86 95.17 -172.18
REMARK 500 2 TYR A 95 -65.04 -138.58
REMARK 500 2 ASP A 96 77.09 -100.09
REMARK 500 3 GLU A 4 171.43 68.42
REMARK 500 3 GLN A 5 -43.81 -136.43
REMARK 500 3 SER A 12 90.26 44.93
REMARK 500 3 ASN A 13 -78.88 -147.58
REMARK 500 3 MET A 14 133.20 -171.40
REMARK 500 3 LEU A 18 73.98 -160.63
REMARK 500 3 ASP A 21 51.78 -96.12
REMARK 500 3 ALA A 24 156.30 173.39
REMARK 500 3 HIS A 25 -51.68 -174.26
REMARK 500 3 ASP A 26 -58.51 -169.96
REMARK 500 3 LEU A 28 -63.79 -140.90
REMARK 500 3 ARG A 51 -68.24 -153.05
REMARK 500 3 LYS A 54 26.67 -149.32
REMARK 500
REMARK 500 THIS ENTRY HAS 355 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17212 RELATED DB: BMRB
DBREF 2L42 A 1 97 UNP P11938 RAP1_YEAST 116 212
SEQADV 2L42 MET A 0 UNP P11938 EXPRESSION TAG
SEQADV 2L42 LEU A 98 UNP P11938 EXPRESSION TAG
SEQADV 2L42 GLU A 99 UNP P11938 EXPRESSION TAG
SEQADV 2L42 HIS A 100 UNP P11938 EXPRESSION TAG
SEQADV 2L42 HIS A 101 UNP P11938 EXPRESSION TAG
SEQADV 2L42 HIS A 102 UNP P11938 EXPRESSION TAG
SEQADV 2L42 HIS A 103 UNP P11938 EXPRESSION TAG
SEQADV 2L42 HIS A 104 UNP P11938 EXPRESSION TAG
SEQADV 2L42 HIS A 105 UNP P11938 EXPRESSION TAG
SEQRES 1 A 106 MET GLU LYS LYS GLU GLN VAL SER GLY PRO PRO LEU SER
SEQRES 2 A 106 ASN MET LYS PHE TYR LEU ASN ARG ASP ALA ASP ALA HIS
SEQRES 3 A 106 ASP SER LEU ASN ASP ILE ASP GLN LEU ALA ARG LEU ILE
SEQRES 4 A 106 ARG ALA ASN GLY GLY GLU VAL LEU ASP SER LYS PRO ARG
SEQRES 5 A 106 GLU SER LYS GLU ASN VAL PHE ILE VAL SER PRO TYR ASN
SEQRES 6 A 106 HIS THR ASN LEU PRO THR VAL THR PRO THR TYR ILE LYS
SEQRES 7 A 106 ALA CYS CYS GLN SER ASN SER LEU LEU ASN MET GLU ASN
SEQRES 8 A 106 TYR LEU VAL PRO TYR ASP ASN LEU GLU HIS HIS HIS HIS
SEQRES 9 A 106 HIS HIS
HELIX 1 1 ASP A 30 ALA A 40 1 11
HELIX 2 2 THR A 74 SER A 82 1 9
HELIX 3 3 LEU A 86 TYR A 91 5 6
SHEET 1 A 2 TYR A 17 LEU A 18 0
SHEET 2 A 2 ASP A 47 SER A 48 1 O SER A 48 N TYR A 17
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
(ATOM LINES ARE NOT SHOWN.)
END
