Header list of 1mzk.pdb file
Complete list - c 21 2 Bytes
HEADER HYDROLASE 08-OCT-02 1MZK
TITLE NMR STRUCTURE OF KINASE-INTERACTING FHA DOMAIN OF KINASE ASSOCIATED
TITLE 2 PROTEIN PHOSPHATASE, KAPP IN ARABIDOPSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINASE ASSOCIATED PROTEIN PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE INTERACTION DOMAIN;
COMPND 5 EC: 3.1.3.16;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 STRAIN: COLUMBIA;
SOURCE 6 GENE: KAPP;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS BETA SANDWICH, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.LEE,Z.DING,J.C.WALKER,S.R.VAN DOREN
REVDAT 5 21-DEC-22 1MZK 1 SEQADV
REVDAT 4 23-FEB-22 1MZK 1 REMARK
REVDAT 3 24-FEB-09 1MZK 1 VERSN
REVDAT 2 23-SEP-03 1MZK 1 JRNL
REVDAT 1 09-SEP-03 1MZK 0
JRNL AUTH G.LEE,Z.DING,J.C.WALKER,S.R.VAN DOREN
JRNL TITL NMR STRUCTURE OF THE FORKHEAD-ASSOCIATED DOMAIN FROM THE
JRNL TITL 2 ARABIDOPSIS RECEPTOR KINASE-ASSOCIATED PROTEIN PHOSPHATASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 11261 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 14500786
JRNL DOI 10.1073/PNAS.2031918100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR 1.3, CNS 1.0
REMARK 3 AUTHORS : BRUKER (UXNMR), A.T.BRUNGER, P.D.ADAMS, G.M.CLORE,
REMARK 3 W.L.DELANO, P.GROS, R.W.GROSSE-KUNSTLEVE, J.-
REMARK 3 S.JIANG, J.KUSZEWSKI, M.NILGES, N.S.PANNU,
REMARK 3 R.J.READ, L.M.RICE, T.SIMONSON, G.L.WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 1313 INTERRESIDUE NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 176 DIHEDRAL ANGLE RESTRAINTS, 54 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS,AS WELL AS 131 1DNH, 55 1DCAHA, 37 1DNCO, 58
REMARK 3 1DCACO RESIDUAL DIPOLAR COUPLING RESTRAINTS.
REMARK 3 THE COVALENT BOND ANGLE DEVIATIONS, LISTED IN REMARK 500, RESULT
REMARK 3 FROM REFINEMENT USING RESIDUAL DIPOLAR
REMARK 3 COUPLINGS AND HAVE OCCURRED IN SOME STRUCTURES WITH HIGH ENERGY.
REMARK 3 THE RESIDUES WITH TORSION ANGLE DEVIATIONS
REMARK 3 ARE RELATIVELY MOBILE AND POORLY DEFINED IN THE MODEL.
REMARK 4
REMARK 4 1MZK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017334.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295; 293; 298; 298
REMARK 210 PH : 6.3; 6.3; 6.3; 6.3
REMARK 210 IONIC STRENGTH : 20MM PHOSPHASTE/120MM NACL; 20MM
REMARK 210 PHOSPHASTE/120MM NACL; 20MM
REMARK 210 PHOSPHASTE/120MM NACL; 20MM
REMARK 210 PHOSPHASTE/120MM NACL/5%PEG/
REMARK 210 HEXANO
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM KINASE INTERACTING FHA
REMARK 210 DOMAIN; 20MM PHOSPHATE PH6.3;
REMARK 210 120MM NACL, 93% H2O, 7%D2O;
REMARK 210 0.6MM KINASE INTERACTING FHA
REMARK 210 DOMAIN; 20MM PHOSPHATE PH6.3;
REMARK 210 120MM NACL, 100%D2O; 0.5MM
REMARK 210 KINASE INTERACTING FHA DOMAIN;
REMARK 210 20MM PHOSPHATE PH6.3; 120MM NACL,
REMARK 210 9.5MG/ML PF1 PHAGE, 90%H2O, 10%
REMARK 210 D2O; 0.4MM KINASE INTERACTING
REMARK 210 FHA DOMAIN; 20MM PHOSPHATE PH6.3;
REMARK 210 120MM NACL, 5% C12H6/HEXANOL,90%
REMARK 210 H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HMQC-J; 15N
REMARK 210 HSQC FOR H/D EXHANGE; 3D_HNCO
REMARK 210 FOR 1DNCO, 1DCACO; 15N HSQC FOR
REMARK 210 1DNH; 3D_HNCA FOR 1DCAHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, SYBYL 6.3, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING IN CARTESIAN
REMARK 210 SPACE AND RESIDUAL DIPOLAR
REMARK 210 COUPLINGS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY,STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
REMARK 210 RESIDUES PRECEDING 180 ORIGINATED FROM LINKER OF GST TAG.
REMARK 210 RESIDUES BEYOND 298 ARE UNSTRUCTURED. NOTE THAT IN ALL THE MODELS
REMARK 210 THE RESIDUES A175-A176 AND A299-A313 ARE DISORDERED AND MISSING
REMARK 210 FROM THE MODEL
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 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 LEU A 220 H ASP A 222 1.53
REMARK 500 O LEU A 243 H VAL A 273 1.59
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 SER A 179 -72.41 -165.08
REMARK 500 1 ALA A 188 92.41 -161.85
REMARK 500 1 PRO A 190 30.58 -79.88
REMARK 500 1 ALA A 191 23.95 -162.28
REMARK 500 1 ILE A 192 113.04 -39.63
REMARK 500 1 SER A 203 -87.30 -90.56
REMARK 500 1 PRO A 207 96.20 -42.83
REMARK 500 1 ARG A 212 -76.16 -71.46
REMARK 500 1 SER A 214 179.81 171.40
REMARK 500 1 PRO A 215 -3.42 -56.65
REMARK 500 1 SER A 216 158.62 -43.24
REMARK 500 1 LEU A 220 66.74 -100.94
REMARK 500 1 LYS A 221 54.35 -62.07
REMARK 500 1 SER A 258 87.78 -58.17
REMARK 500 1 LEU A 264 -85.78 -54.20
REMARK 500 1 ARG A 267 22.52 49.50
REMARK 500 1 ASP A 278 7.84 86.05
REMARK 500 1 THR A 286 -0.40 -148.37
REMARK 500 2 SER A 179 -89.74 -179.54
REMARK 500 2 ALA A 188 97.02 -168.54
REMARK 500 2 PRO A 190 30.12 -81.13
REMARK 500 2 ALA A 191 24.68 -161.48
REMARK 500 2 ILE A 192 106.57 -39.65
REMARK 500 2 SER A 203 -85.67 -90.22
REMARK 500 2 PRO A 207 97.01 -42.86
REMARK 500 2 ARG A 212 -77.27 -69.33
REMARK 500 2 SER A 214 -178.61 171.98
REMARK 500 2 PRO A 215 12.64 -61.68
REMARK 500 2 SER A 216 -173.61 -57.51
REMARK 500 2 LYS A 221 65.04 -58.94
REMARK 500 2 LYS A 238 23.47 -145.87
REMARK 500 2 PHE A 239 62.16 36.97
REMARK 500 2 SER A 248 64.67 -68.50
REMARK 500 2 THR A 252 159.20 -46.24
REMARK 500 2 SER A 258 98.73 -58.79
REMARK 500 2 SER A 260 170.81 -59.80
REMARK 500 2 PRO A 262 79.93 -55.43
REMARK 500 2 ARG A 267 22.60 46.58
REMARK 500 2 ASP A 278 -2.95 81.28
REMARK 500 3 SER A 179 -86.98 -179.81
REMARK 500 3 ALA A 188 99.66 -162.08
REMARK 500 3 PRO A 190 30.85 -83.67
REMARK 500 3 ALA A 191 24.30 -162.83
REMARK 500 3 ILE A 192 108.64 -39.32
REMARK 500 3 SER A 203 -89.93 -72.72
REMARK 500 3 LEU A 206 -56.30 -143.58
REMARK 500 3 PRO A 207 100.60 -41.36
REMARK 500 3 ARG A 212 -72.32 -69.04
REMARK 500 3 VAL A 213 -142.05 -128.86
REMARK 500 3 SER A 214 -179.42 66.90
REMARK 500
REMARK 500 THIS ENTRY HAS 624 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MZK A 180 313 UNP P46014 KAPP_ARATH 180 313
SEQADV 1MZK GLY A 175 UNP P46014 EXPRESSION TAG
SEQADV 1MZK PRO A 176 UNP P46014 EXPRESSION TAG
SEQADV 1MZK LEU A 177 UNP P46014 EXPRESSION TAG
SEQADV 1MZK GLY A 178 UNP P46014 EXPRESSION TAG
SEQADV 1MZK SER A 179 UNP P46014 EXPRESSION TAG
SEQRES 1 A 139 GLY PRO LEU GLY SER SER TRP LEU PHE LEU GLU VAL ILE
SEQRES 2 A 139 ALA GLY PRO ALA ILE GLY LEU GLN HIS ALA VAL ASN SER
SEQRES 3 A 139 THR SER SER SER LYS LEU PRO VAL LYS LEU GLY ARG VAL
SEQRES 4 A 139 SER PRO SER ASP LEU ALA LEU LYS ASP SER GLU VAL SER
SEQRES 5 A 139 GLY LYS HIS ALA GLN ILE THR TRP ASN SER THR LYS PHE
SEQRES 6 A 139 LYS TRP GLU LEU VAL ASP MET GLY SER LEU ASN GLY THR
SEQRES 7 A 139 LEU VAL ASN SER HIS SER ILE SER HIS PRO ASP LEU GLY
SEQRES 8 A 139 SER ARG LYS TRP GLY ASN PRO VAL GLU LEU ALA SER ASP
SEQRES 9 A 139 ASP ILE ILE THR LEU GLY THR THR THR LYS VAL TYR VAL
SEQRES 10 A 139 ARG ILE SER SER GLN ASN GLU PHE GLN ILE PRO PHE LYS
SEQRES 11 A 139 ILE GLY VAL ALA SER ASP PRO MET ALA
SHEET 1 A 6 GLN A 195 VAL A 198 0
SHEET 2 A 6 SER A 180 VAL A 186 -1 N LEU A 182 O VAL A 198
SHEET 3 A 6 LYS A 288 SER A 295 -1 O ARG A 292 N PHE A 183
SHEET 4 A 6 ASP A 279 THR A 282 -1 N ILE A 281 O VAL A 289
SHEET 5 A 6 LEU A 253 VAL A 254 -1 N LEU A 253 O THR A 282
SHEET 6 A 6 HIS A 257 SER A 258 -1 O HIS A 257 N VAL A 254
SHEET 1 B 5 LEU A 218 ALA A 219 0
SHEET 2 B 5 VAL A 208 GLY A 211 1 N GLY A 211 O LEU A 218
SHEET 3 B 5 LYS A 228 ASN A 235 -1 O ALA A 230 N LEU A 210
SHEET 4 B 5 LYS A 240 ASP A 245 -1 O LYS A 240 N ASN A 235
SHEET 5 B 5 VAL A 273 GLU A 274 -1 O VAL A 273 N LEU A 243
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 - c 21 2 Bytes