Header list of 1t3k.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE 27-APR-04 1T3K
TITLE NMR STRUCTURE OF A CDC25-LIKE DUAL-SPECIFICITY TYROSINE PHOSPHATASE OF
TITLE 2 ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL-SPECIFICITY TYROSINE PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ARATH CDC25;
COMPND 5 EC: 3.1.3.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: CDC25;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CDC25, CELL CYCLE, PHOSPHORYLATION, PLANT, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.LANDRIEU,M.DA COSTA,L.DE VEYLDER,F.DEWITTE,K.VANDEPOELE,S.HASSAN,
AUTHOR 2 J.M.WIERUSZESKI,J.D.FAURE,D.INZE,G.LIPPENS
REVDAT 3 27-OCT-21 1T3K 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1T3K 1 VERSN
REVDAT 1 07-SEP-04 1T3K 0
JRNL AUTH I.LANDRIEU,M.DA COSTA,L.DE VEYLDER,F.DEWITTE,K.VANDEPOELE,
JRNL AUTH 2 S.HASSAN,J.M.WIERUSZESKI,J.D.FAURE,M.VAN MONTAGU,D.INZE,
JRNL AUTH 3 G.LIPPENS
JRNL TITL A SMALL CDC25 DUAL-SPECIFICITY TYROSINE-PHOSPHATASE ISOFORM
JRNL TITL 2 IN ARABIDOPSIS THALIANA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 13380 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15329414
JRNL DOI 10.1073/PNAS.0405248101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T3K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022267.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 400 MICROM U-15N,13C
REMARK 210 ARATH;CDC25; 400 MICROM U-15N
REMARK 210 ARATH;CDC25; 400 MICROM 13C
REMARK 210 ARATH;CDC25
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_HNCACO; 3D HNCO; 3D
REMARK 210 CBCA(CO)NH; 3D HNCA; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SNARF, CNS 1.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: CRYO-PROBEHEAD
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 O ASN A 23 H THR A 67 1.57
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 ALA A 2 80.90 60.04
REMARK 500 1 MET A 3 35.26 -163.66
REMARK 500 1 ALA A 4 81.53 -152.95
REMARK 500 1 SER A 6 154.46 61.18
REMARK 500 1 LEU A 18 -88.52 -96.99
REMARK 500 1 ARG A 21 -174.10 157.64
REMARK 500 1 PRO A 22 -13.07 -46.13
REMARK 500 1 ASN A 23 -9.20 -56.43
REMARK 500 1 ARG A 30 -32.69 178.25
REMARK 500 1 ASP A 31 -21.19 154.14
REMARK 500 1 GLU A 32 -59.18 75.19
REMARK 500 1 ILE A 40 -174.92 -170.14
REMARK 500 1 SER A 43 131.59 59.46
REMARK 500 1 ALA A 47 -160.40 -65.27
REMARK 500 1 SER A 48 28.05 -168.48
REMARK 500 1 PHE A 51 -13.10 75.13
REMARK 500 1 ASP A 64 -65.82 66.97
REMARK 500 1 HIS A 71 -70.04 98.45
REMARK 500 1 SER A 72 -12.24 99.31
REMARK 500 1 ALA A 73 -83.32 -113.40
REMARK 500 1 LEU A 74 35.55 -169.56
REMARK 500 1 VAL A 77 -29.35 178.85
REMARK 500 1 LYS A 93 -74.73 -109.40
REMARK 500 1 LYS A 94 134.28 131.40
REMARK 500 1 ASP A 96 -93.96 -54.99
REMARK 500 1 THR A 97 70.98 39.29
REMARK 500 1 PHE A 109 20.80 -155.88
REMARK 500 1 LYS A 117 158.60 64.20
REMARK 500 1 PRO A 118 -94.19 -40.52
REMARK 500 1 CYS A 120 140.17 -31.35
REMARK 500 1 ARG A 121 -81.96 -112.53
REMARK 500 1 CYS A 122 -161.82 43.70
REMARK 500 1 ALA A 123 31.63 -159.08
REMARK 500 1 LYS A 128 176.88 60.80
REMARK 500 2 ALA A 2 83.10 65.50
REMARK 500 2 ARG A 5 152.98 72.78
REMARK 500 2 ILE A 7 -179.41 -51.99
REMARK 500 2 ARG A 20 -27.39 86.60
REMARK 500 2 ARG A 21 123.62 60.75
REMARK 500 2 ASN A 23 67.96 -67.16
REMARK 500 2 ARG A 30 -41.19 -168.81
REMARK 500 2 ASP A 31 -154.66 85.85
REMARK 500 2 ILE A 40 90.23 -43.74
REMARK 500 2 SER A 43 -95.07 -104.51
REMARK 500 2 TYR A 46 -153.70 -154.52
REMARK 500 2 ALA A 47 -169.56 -164.84
REMARK 500 2 SER A 50 33.48 -148.83
REMARK 500 2 ASP A 52 32.67 -95.98
REMARK 500 2 VAL A 62 -30.14 85.32
REMARK 500 2 LYS A 65 72.78 -114.35
REMARK 500
REMARK 500 THIS ENTRY HAS 673 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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 ND1
REMARK 620 2 CYS A 120 SG 128.6
REMARK 620 3 CYS A 122 SG 115.4 86.8
REMARK 620 4 CYS A 127 SG 116.9 110.8 84.1
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 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6195 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGMENT
DBREF 1T3K A 1 132 UNP Q8GY31 CDC25_ARATH 15 146
SEQADV 1T3K MET A -19 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K GLY A -18 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K SER A -17 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K SER A -16 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A -15 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A -14 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A -13 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A -12 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A -11 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A -10 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K SER A -9 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K SER A -8 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K GLY A -7 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K LEU A -6 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K VAL A -5 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K PRO A -4 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K ARG A -3 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K GLY A -2 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K SER A -1 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K HIS A 0 UNP Q8GY31 CLONING ARTIFACT
SEQADV 1T3K SER A 72 UNP Q8GY31 CYS 86 ENGINEERED MUTATION
SEQRES 1 A 152 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 152 LEU VAL PRO ARG GLY SER HIS MET ALA MET ALA ARG SER
SEQRES 3 A 152 ILE SER TYR ILE THR SER THR GLN LEU LEU PRO LEU HIS
SEQRES 4 A 152 ARG ARG PRO ASN ILE ALA ILE ILE ASP VAL ARG ASP GLU
SEQRES 5 A 152 GLU ARG ASN TYR ASP GLY HIS ILE ALA GLY SER LEU HIS
SEQRES 6 A 152 TYR ALA SER GLY SER PHE ASP ASP LYS ILE SER HIS LEU
SEQRES 7 A 152 VAL GLN ASN VAL LYS ASP LYS ASP THR LEU VAL PHE HIS
SEQRES 8 A 152 SER ALA LEU SER GLN VAL ARG GLY PRO THR CYS ALA ARG
SEQRES 9 A 152 ARG LEU VAL ASN TYR LEU ASP GLU LYS LYS GLU ASP THR
SEQRES 10 A 152 GLY ILE LYS ASN ILE MET ILE LEU GLU ARG GLY PHE ASN
SEQRES 11 A 152 GLY TRP GLU ALA SER GLY LYS PRO VAL CYS ARG CYS ALA
SEQRES 12 A 152 GLU VAL PRO CYS LYS GLY ASP CYS ALA
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLU A 32 ASP A 37 1 6
HELIX 2 2 LYS A 54 ASN A 61 1 8
HELIX 3 3 ARG A 78 LYS A 93 1 16
HELIX 4 4 PHE A 109 GLY A 116 1 8
SHEET 1 A 5 SER A 8 ILE A 10 0
SHEET 2 A 5 ASN A 101 LEU A 105 1 O ILE A 104 N ILE A 10
SHEET 3 A 5 THR A 67 PHE A 70 1 N LEU A 68 O ASN A 101
SHEET 4 A 5 ILE A 24 VAL A 29 1 N ALA A 25 O VAL A 69
SHEET 5 A 5 LEU A 44 TYR A 46 1 O LEU A 44 N ILE A 26
LINK ND1 HIS A 39 ZN ZN A 201 1555 1555 2.05
LINK SG CYS A 120 ZN ZN A 201 1555 1555 2.26
LINK SG CYS A 122 ZN ZN A 201 1555 1555 2.55
LINK SG CYS A 127 ZN ZN A 201 1555 1555 2.36
SITE 1 AC1 4 HIS A 39 CYS A 120 CYS A 122 CYS A 127
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 - t 27 2 Bytes