HEADER SIGNALING PROTEIN 12-FEB-10 2KU3
TITLE SOLUTION STRUCTURE OF BRD1 PHD1 FINGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHD ZINC FINGER DOMAIN, RESIDUES 208-269;
COMPND 5 SYNONYM: BR140-LIKE PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BRD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: P28
KEYWDS PHD FINGER, BROMODOMAIN, CHROMATIN REGULATOR, METAL-BINDING, ZINC-
KEYWDS 2 FINGER, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.QIN,J.ZHANG,J.WU,Y.SHI
REVDAT 2 01-MAY-24 2KU3 1 REMARK SEQADV LINK
REVDAT 1 16-FEB-11 2KU3 0
JRNL AUTH S.QIN,J.ZHANG,J.WU,Y.SHI
JRNL TITL SOLUTION STRUCTURE OF BRD1 PHD1 FINGER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CNS 1.2
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), BRUNGER, ADAMS, CLORE, GROS, NILGES AND
REMARK 3 READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000101573.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293
REMARK 210 PH : 6.7; NULL
REMARK 210 IONIC STRENGTH : 0.15; 0.15
REMARK 210 PRESSURE : AMBIENT; NULL
REMARK 210 SAMPLE CONTENTS : 2MM ZINC ION; 1MM [U-100% 13C; U
REMARK 210 -100% 15N] PROTEIN; 150MM SODIUM
REMARK 210 CHLORIDE; 20MM BIS-TRIS; 90% H2O/
REMARK 210 10% D2O; 2MM ZINC ION; 1MM [U-
REMARK 210 100% 13C; U-100% 15N] PROTEIN;
REMARK 210 20MM BIS-TRIS; 150MM SODIUM
REMARK 210 CHLORIDE; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB; 3D HNCO; 3D HBHA(CO)
REMARK 210 NH; 3D C(CO)NH; 3D H(CCO)NH; 3D
REMARK 210 1H-15N NOESY; 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 : SPARKY 3, CNS 1.2, TALOS, MOLMOL
REMARK 210 2K.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 MET A -8
REMARK 465 GLY A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 SER A 2 -71.08 -123.39
REMARK 500 1 ASP A 5 -50.57 -167.24
REMARK 500 1 ALA A 8 37.84 -95.39
REMARK 500 1 CYS A 27 -170.34 -67.43
REMARK 500 1 ASN A 31 25.49 82.18
REMARK 500 1 TYR A 43 -169.80 -164.65
REMARK 500 1 GLN A 48 -155.86 -100.81
REMARK 500 2 SER A 2 -67.62 -151.93
REMARK 500 2 ILE A 4 -44.49 -134.74
REMARK 500 2 ALA A 8 48.11 -90.75
REMARK 500 2 MET A 14 74.32 60.16
REMARK 500 2 ASN A 22 85.48 -153.30
REMARK 500 2 MET A 29 -64.49 -132.15
REMARK 500 2 ASN A 31 25.81 84.11
REMARK 500 2 GLN A 48 -156.53 -92.07
REMARK 500 3 ASP A 5 48.13 -95.47
REMARK 500 3 ALA A 8 33.47 -95.20
REMARK 500 3 MET A 14 78.48 67.19
REMARK 500 3 ASP A 15 116.47 -160.42
REMARK 500 3 ASN A 22 87.00 -151.61
REMARK 500 3 CYS A 27 -169.67 -73.39
REMARK 500 3 MET A 29 -64.73 -121.54
REMARK 500 3 ASN A 31 25.14 81.98
REMARK 500 3 GLN A 48 -155.57 -104.67
REMARK 500 4 SER A 2 38.51 -99.29
REMARK 500 4 GLU A 6 -70.81 72.50
REMARK 500 4 ASP A 7 27.72 -151.81
REMARK 500 4 MET A 14 70.61 63.39
REMARK 500 4 MET A 29 -64.43 -128.40
REMARK 500 4 ASN A 31 26.34 81.28
REMARK 500 4 GLN A 48 -155.67 -104.45
REMARK 500 5 MET A 14 70.69 54.74
REMARK 500 5 ASP A 15 117.06 -160.61
REMARK 500 5 CYS A 27 -169.91 -71.35
REMARK 500 5 ASN A 31 23.83 83.24
REMARK 500 5 GLN A 48 -156.00 -120.71
REMARK 500 5 ALA A 59 -76.68 -95.83
REMARK 500 6 LEU A 3 -72.71 -95.76
REMARK 500 6 ASP A 5 57.03 -96.41
REMARK 500 6 ASP A 7 45.52 -102.02
REMARK 500 6 MET A 14 83.61 64.49
REMARK 500 6 CYS A 27 -171.01 -66.17
REMARK 500 6 MET A 29 -48.66 -138.50
REMARK 500 6 TYR A 43 -174.19 -170.74
REMARK 500 6 GLN A 48 -155.73 -93.66
REMARK 500 6 CYS A 51 170.07 -55.35
REMARK 500 7 ILE A 4 43.35 -158.05
REMARK 500 7 ASP A 5 -47.92 -133.00
REMARK 500 7 MET A 14 76.84 56.77
REMARK 500 7 CYS A 27 -170.89 -69.23
REMARK 500
REMARK 500 THIS ENTRY HAS 148 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 64 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 13 SG 109.1
REMARK 620 3 HIS A 35 ND1 101.3 111.6
REMARK 620 4 CYS A 38 SG 108.3 110.3 115.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 63 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 27 SG
REMARK 620 2 CYS A 30 SG 105.4
REMARK 620 3 CYS A 51 SG 109.6 109.4
REMARK 620 4 CYS A 54 SG 106.8 118.1 107.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 63
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 64
DBREF 2KU3 A 1 62 UNP O95696 BRD1_HUMAN 208 269
SEQADV 2KU3 MET A -8 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 GLY A -7 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 HIS A -6 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 HIS A -5 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 HIS A -4 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 HIS A -3 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 HIS A -2 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 HIS A -1 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 MET A 0 UNP O95696 EXPRESSION TAG
SEQADV 2KU3 SER A 11 UNP O95696 CYS 218 ENGINEERED MUTATION
SEQADV 2KU3 SER A 18 UNP O95696 CYS 225 ENGINEERED MUTATION
SEQRES 1 A 71 MET GLY HIS HIS HIS HIS HIS HIS MET GLN SER LEU ILE
SEQRES 2 A 71 ASP GLU ASP ALA VAL CYS SER ILE CYS MET ASP GLY GLU
SEQRES 3 A 71 SER GLN ASN SER ASN VAL ILE LEU PHE CYS ASP MET CYS
SEQRES 4 A 71 ASN LEU ALA VAL HIS GLN GLU CYS TYR GLY VAL PRO TYR
SEQRES 5 A 71 ILE PRO GLU GLY GLN TRP LEU CYS ARG HIS CYS LEU GLN
SEQRES 6 A 71 SER ARG ALA ARG PRO ALA
HET ZN A 63 1
HET ZN A 64 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLN A 36 GLY A 40 1 5
HELIX 2 2 CYS A 51 ARG A 60 1 10
SHEET 1 A 2 ILE A 24 PHE A 26 0
SHEET 2 A 2 ALA A 33 HIS A 35 -1 O VAL A 34 N LEU A 25
LINK SG CYS A 10 ZN ZN A 64 1555 1555 2.29
LINK SG CYS A 13 ZN ZN A 64 1555 1555 2.29
LINK SG CYS A 27 ZN ZN A 63 1555 1555 2.30
LINK SG CYS A 30 ZN ZN A 63 1555 1555 2.30
LINK ND1 HIS A 35 ZN ZN A 64 1555 1555 2.01
LINK SG CYS A 38 ZN ZN A 64 1555 1555 2.30
LINK SG CYS A 51 ZN ZN A 63 1555 1555 2.30
LINK SG CYS A 54 ZN ZN A 63 1555 1555 2.30
SITE 1 AC1 4 CYS A 27 CYS A 30 CYS A 51 CYS A 54
SITE 1 AC2 4 CYS A 10 CYS A 13 HIS A 35 CYS A 38
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