HEADER OXIDOREDUCTASE 08-SEP-13 2MDA
TITLE THE SOLUTION STRUCTURE OF THE REGULATORY DOMAIN OF TYROSINE
TITLE 2 HYDROXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE 3-MONOOXYGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: REGULATORY DOMAIN (UNP RESIDUES 65-159);
COMPND 5 SYNONYM: TYROSINE 3-HYDROXYLASE, TH;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: TH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETNTERM
KEYWDS TYROSINE HYDROXYLASE, REGULATION, ACT DOMAIN, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.ZHANG,T.HUANG,A.HINCK,P.FITZPATRICK
REVDAT 3 26-MAR-14 2MDA 1 JRNL
REVDAT 2 15-JAN-14 2MDA 1 JRNL
REVDAT 1 01-JAN-14 2MDA 0
JRNL AUTH S.ZHANG,T.HUANG,U.ILANGOVAN,A.P.HINCK,P.F.FITZPATRICK
JRNL TITL THE SOLUTION STRUCTURE OF THE REGULATORY DOMAIN OF TYROSINE
JRNL TITL 2 HYDROXYLASE.
JRNL REF J.MOL.BIOL. V. 426 1483 2014
JRNL REFN ISSN 0022-2836
JRNL PMID 24361276
JRNL DOI 10.1016/J.JMB.2013.12.015
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 2MDA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB103500.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.11
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM [U-95% 15N] RDTYRH65, 50
REMARK 210 MM SODIUM PHOSPHATE, 95% H2O/5%
REMARK 210 D2O; 1.0-1.2 MM [U-95% 13C; U-95%
REMARK 210 15N] RDTYRH65, 50 MM SODIUM
REMARK 210 PHOSPHATE, 95% H2O/5% D2O; 0.9 MM
REMARK 210 RDTYRH65, 0.9 MM [U-2H;U-15N]
REMARK 210 RDTYRH65, 50 MM SODIUM PHOSPHATE,
REMARK 210 95% H2O/5% D2O; 0.8 MM [U-95%
REMARK 210 15N] RDTYRH65, 50 MM SODIUM
REMARK 210 PHOSPHATE, 8 MG/ML PF1 PHAGE, 95%
REMARK 210 H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210 HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HBHA(CO)NH; 3D HN(CO)CA; 3D
REMARK 210 H(CCO)NH; 3D HCCH-TOCSY; 3D HNHA;
REMARK 210 3D 1H-15N NOESY; 3D 1H-13C NOESY;
REMARK 210 2D IPAP-HSQC; T1; T2; RELAX_NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA, MODELFREE, NMRDRAW,
REMARK 210 NMRPIPE, NMRVIEW, PECAN,
REMARK 210 PROCHECKNMR, TALOS, TOPSPIN
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 PRO A 94 79.42 -67.74
REMARK 500 1 SER A 96 43.32 -70.98
REMARK 500 1 ARG A 117 95.27 -161.92
REMARK 500 1 ALA A 119 -163.31 -74.22
REMARK 500 1 GLN A 120 -55.17 76.07
REMARK 500 1 SER A 126 -51.65 -161.45
REMARK 500 1 LEU A 129 142.75 -38.50
REMARK 500 1 TYR A 131 99.76 -164.62
REMARK 500 1 PRO A 138 132.44 -35.00
REMARK 500 1 ASP A 154 -37.94 -149.85
REMARK 500 1 ASP A 155 34.46 -91.91
REMARK 500 1 PRO B 94 79.50 -67.79
REMARK 500 1 SER B 96 42.17 -70.86
REMARK 500 1 ARG B 117 95.34 -161.98
REMARK 500 1 ALA B 119 -163.22 -74.13
REMARK 500 1 GLN B 120 -55.20 75.99
REMARK 500 1 SER B 126 -51.71 -161.39
REMARK 500 1 LEU B 129 142.82 -38.52
REMARK 500 1 TYR B 131 99.70 -164.63
REMARK 500 1 PRO B 138 132.35 -35.00
REMARK 500 1 ASP B 154 -37.88 -149.83
REMARK 500 1 ASP B 155 34.34 -91.88
REMARK 500 2 ALA A 71 -39.17 -149.11
REMARK 500 2 PHE A 87 99.92 -166.88
REMARK 500 2 ARG A 90 -94.25 -160.99
REMARK 500 2 THR A 92 63.16 33.01
REMARK 500 2 HIS A 113 96.95 -163.33
REMARK 500 2 THR A 116 -169.03 -76.40
REMARK 500 2 ARG A 121 -59.41 -155.16
REMARK 500 2 PRO A 122 -77.12 -58.78
REMARK 500 2 ALA A 124 129.95 75.68
REMARK 500 2 PRO A 127 96.89 -45.99
REMARK 500 2 HIS A 128 129.39 -173.07
REMARK 500 2 LEU A 129 -179.90 -179.24
REMARK 500 2 GLU A 130 154.29 178.67
REMARK 500 2 PRO A 138 128.99 -36.13
REMARK 500 2 ASP A 154 -42.94 -147.18
REMARK 500 2 ASP A 155 39.28 -91.16
REMARK 500 2 VAL A 156 -165.55 -128.00
REMARK 500 2 ALA B 71 -39.24 -149.04
REMARK 500 2 PHE B 87 99.85 -166.79
REMARK 500 2 ARG B 90 -94.21 -160.98
REMARK 500 2 THR B 92 63.11 32.98
REMARK 500 2 HIS B 113 97.01 -163.32
REMARK 500 2 THR B 116 -169.11 -76.32
REMARK 500 2 GLN B 120 133.79 -170.04
REMARK 500 2 ARG B 121 -59.35 -155.22
REMARK 500 2 PRO B 122 -76.97 -58.84
REMARK 500 2 ALA B 124 129.92 75.88
REMARK 500 2 PRO B 127 96.77 -45.88
REMARK 500
REMARK 500 THIS ENTRY HAS 327 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19482 RELATED DB: BMRB
DBREF 2MDA A 65 159 UNP P04177 TY3H_RAT 65 159
DBREF 2MDA B 65 159 UNP P04177 TY3H_RAT 65 159
SEQRES 1 A 95 PRO GLY ASN PRO LEU GLU ALA VAL VAL PHE GLU GLU ARG
SEQRES 2 A 95 ASP GLY ASN ALA VAL LEU ASN LEU LEU PHE SER LEU ARG
SEQRES 3 A 95 GLY THR LYS PRO SER SER LEU SER ARG ALA VAL LYS VAL
SEQRES 4 A 95 PHE GLU THR PHE GLU ALA LYS ILE HIS HIS LEU GLU THR
SEQRES 5 A 95 ARG PRO ALA GLN ARG PRO LEU ALA GLY SER PRO HIS LEU
SEQRES 6 A 95 GLU TYR PHE VAL ARG PHE GLU VAL PRO SER GLY ASP LEU
SEQRES 7 A 95 ALA ALA LEU LEU SER SER VAL ARG ARG VAL SER ASP ASP
SEQRES 8 A 95 VAL ARG SER ALA
SEQRES 1 B 95 PRO GLY ASN PRO LEU GLU ALA VAL VAL PHE GLU GLU ARG
SEQRES 2 B 95 ASP GLY ASN ALA VAL LEU ASN LEU LEU PHE SER LEU ARG
SEQRES 3 B 95 GLY THR LYS PRO SER SER LEU SER ARG ALA VAL LYS VAL
SEQRES 4 B 95 PHE GLU THR PHE GLU ALA LYS ILE HIS HIS LEU GLU THR
SEQRES 5 B 95 ARG PRO ALA GLN ARG PRO LEU ALA GLY SER PRO HIS LEU
SEQRES 6 B 95 GLU TYR PHE VAL ARG PHE GLU VAL PRO SER GLY ASP LEU
SEQRES 7 B 95 ALA ALA LEU LEU SER SER VAL ARG ARG VAL SER ASP ASP
SEQRES 8 B 95 VAL ARG SER ALA
HELIX 1 1 LEU A 97 PHE A 107 1 11
HELIX 2 2 GLY A 140 ARG A 151 1 12
HELIX 3 3 LEU B 97 PHE B 107 1 11
HELIX 4 4 GLY B 140 ARG B 151 1 12
SHEET 1 A 8 GLU A 75 ARG A 77 0
SHEET 2 A 8 ASN A 80 ASN A 84 -1 O ASN A 80 N ARG A 77
SHEET 3 A 8 VAL A 133 PRO A 138 -1 O VAL A 137 N ALA A 81
SHEET 4 A 8 LYS A 110 THR A 116 -1 N LYS A 110 O GLU A 136
SHEET 5 A 8 LYS B 110 THR B 116 -1 O LEU B 114 N THR A 116
SHEET 6 A 8 VAL B 133 PRO B 138 -1 O GLU B 136 N LYS B 110
SHEET 7 A 8 ASN B 80 ASN B 84 -1 N ALA B 81 O VAL B 137
SHEET 8 A 8 GLU B 75 ARG B 77 -1 N ARG B 77 O ASN B 80
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
