Header list of 1plo.pdb file
Complete list - t 27 2 Bytes
HEADER CYTOKINE RECEPTOR 08-JUN-03 1PLO TITLE TRANSFORMING GROWTH FACTOR-BETA TYPE II RECEPTOR EXTRACELLULAR DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TGF-BETA RECEPTOR TYPE II; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TGFR-2, TGF-BETA TYPE II RECEPTOR; COMPND 5 EC: 2.7.1.37; 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: TGFBR2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS THREE-FINGER TOXIN FOLD, CYTOKINE RECEPTOR EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR S.DEEP,K.P.WALKER III,Z.SHU,A.P.HINCK REVDAT 3 27-OCT-21 1PLO 1 REMARK SEQADV REVDAT 2 24-FEB-09 1PLO 1 VERSN REVDAT 1 23-SEP-03 1PLO 0 JRNL AUTH S.DEEP,K.P.WALKER III,Z.SHU,A.P.HINCK JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE TGF-BETA JRNL TITL 2 TYPE II RECEPTOR EXTRACELLULAR DOMAIN JRNL REF BIOCHEMISTRY V. 42 10126 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12939140 JRNL DOI 10.1021/BI034366A REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR_NIH 1.06 REMARK 3 AUTHORS : CLORE, G.M., KUSZEWSKI, J., SCHWIETERS, C.D., REMARK 3 TJANDRA, N. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 STRUCTURES ARE BASED ON A TOTAL OF 1583 CONSTRAINTS, REMARK 3 1168 ARE NOE DISTANCE, REMARK 3 138 ARE DIHEDREDRAL ANGLE, REMARK 3 58 ARE 3JHNHA COUPLING CONSTANT, REMARK 3 219 ARE RESIDUAL DIPOLAR COUPLINGS, REMARK 4 REMARK 4 1PLO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-03. REMARK 100 THE DEPOSITION ID IS D_1000019411. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 313 REMARK 210 PH : 5.5; 5.1; 5.5 REMARK 210 IONIC STRENGTH : 25MM SODIUM ACETATE, 25MM NACL, REMARK 210 PH 5.5; 25MM SODIUM ACETATE, REMARK 210 25MM NACL; 25MM SODIUM ACETATE, REMARK 210 25MM NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM ECTBR2 U-15N, 25MM SODIUM REMARK 210 ACETATE, 25MM NACL, 95% H2O, 5% D2O; 1MM ECTBR2 U-15N, 13C, 25MM REMARK 210 SODIUM ACETATE, 25MM NACL, 95% H2O, 5% D2O; 1MM ECTBR2 U-15N, REMARK 210 13C, 25MM SODIUM ACETATE, 25MM NACL, 99.99% D2O; 1MM ECTBR2 U- REMARK 210 15N, 25MM SODIUM ACETATE, 25MM NACL, 4% (W/V) 1,2-DI-O-HEXYL-SN- REMARK 210 GLYCERO-3-PHOSPHOCHOLINE (6-O-PC) AND 1,2-DI-O-TETRADECYL-SN- REMARK 210 GLYCERO-3-PHOSPHOCHOLINE (14-O-PC) MIXED IN A MOLAR RATIO OF 1:3, REMARK 210 95% H2O, 5% D2O; 1MM ECTBR2 U-15N, 13C, 25MM SODIUM ACETATE, REMARK 210 25MM NACL, 4% (W/V) 1,2-DI-O-HEXYL-SN-GLYCERO-3-PHOSPHOCHOLINE REMARK 210 (6-O-PC) AND 1,2-DI-O-TETRADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE (14- REMARK 210 O-PC) MIXED IN A MOLAR RATIO OF 1:3, 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; 3D 15N EDITED, REMARK 210 13C-EDITED 1H-1H NOESY; 3D 15N- REMARK 210 EDITED,15N-EDITED 1H-1H NOESY; REMARK 210 1H-15H 1-BOND RESIDUAL DIPOLAR REMARK 210 COUPLING (2D IPAP-HSQC); 13C- REMARK 210 13CO RESIDUAL DIPOLAR COUPLING REMARK 210 (3D (HA)CA(CO)NH; 13CALPHA-13CO REMARK 210 RESIDUAL DIPOLAR COUPLING (3D CA- REMARK 210 COUPLED HNCO) REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SUBSTRUCTURE DISTANCE GEOMETRY, REMARK 210 FULL STRUCTURE DISTANCE GEOMETRY- REMARK 210 SIMULATED ANNEALING; TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY, STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 THIS STRUCTURE WAS DETERMINED BY REFINING SIMULTANEOUSLY AGAINST REMARK 210 NOE, J-COUPLING, DIHEDRAL ANGLE, REMARK 210 AND RESIDUAL DIPOLAR COUPLING CONSTRAINTS 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 CYS A 28 H SER A 52 1.53 REMARK 500 H VAL A 60 O HIS A 79 1.59 REMARK 500 H ASN A 68 O ASN A 71 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 VAL A 22 34.78 -178.60 REMARK 500 1 ASP A 32 -142.71 68.84 REMARK 500 1 ASP A 39 -95.57 -90.70 REMARK 500 1 GLN A 41 -143.10 -77.88 REMARK 500 1 LYS A 42 102.46 55.32 REMARK 500 1 SER A 43 84.23 43.51 REMARK 500 1 CYS A 48 -42.96 -147.89 REMARK 500 1 VAL A 60 -166.94 -121.78 REMARK 500 1 ASP A 69 -77.58 56.55 REMARK 500 1 GLU A 91 7.88 -159.96 REMARK 500 1 GLU A 102 149.53 47.10 REMARK 500 1 CYS A 113 114.82 -168.71 REMARK 500 1 ASP A 118 -101.17 -38.27 REMARK 500 1 SER A 127 3.95 -156.55 REMARK 500 1 GLU A 128 -74.54 58.36 REMARK 500 2 ALA A 19 174.46 52.90 REMARK 500 2 ALA A 21 -37.63 -172.20 REMARK 500 2 ASP A 32 -161.91 80.89 REMARK 500 2 ASN A 40 95.84 32.66 REMARK 500 2 GLN A 41 -86.19 -160.86 REMARK 500 2 LYS A 42 -55.57 -156.18 REMARK 500 2 VAL A 60 -163.01 -114.96 REMARK 500 2 ASP A 69 -66.73 66.99 REMARK 500 2 GLU A 70 -21.90 -140.48 REMARK 500 2 PRO A 81 49.41 -82.38 REMARK 500 2 ASP A 87 30.90 70.46 REMARK 500 2 GLU A 91 57.10 -162.24 REMARK 500 2 ASP A 92 -0.86 -148.54 REMARK 500 2 MET A 100 99.29 55.11 REMARK 500 2 GLU A 102 118.37 25.04 REMARK 500 2 CYS A 113 146.23 -178.90 REMARK 500 2 GLU A 119 78.87 53.00 REMARK 500 2 GLU A 128 -72.79 -157.51 REMARK 500 2 TYR A 130 -29.40 -179.63 REMARK 500 2 ASN A 131 58.01 -172.29 REMARK 500 2 THR A 132 -92.58 54.10 REMARK 500 3 ASP A 32 -160.46 80.43 REMARK 500 3 ASN A 40 95.12 34.08 REMARK 500 3 GLN A 41 -84.90 -161.92 REMARK 500 3 LYS A 42 -57.43 -156.85 REMARK 500 3 SER A 46 148.08 60.34 REMARK 500 3 ASP A 69 -68.49 64.39 REMARK 500 3 GLU A 70 -36.15 -131.66 REMARK 500 3 HIS A 86 -51.72 69.48 REMARK 500 3 ASP A 87 -18.46 -160.28 REMARK 500 3 GLU A 91 64.47 -159.92 REMARK 500 3 ASP A 92 3.85 -151.12 REMARK 500 3 ILE A 99 75.59 -66.94 REMARK 500 3 GLU A 119 119.89 54.26 REMARK 500 3 CYS A 120 20.21 -159.91 REMARK 500 REMARK 500 THIS ENTRY HAS 182 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 34 0.24 SIDE CHAIN REMARK 500 1 ARG A 66 0.21 SIDE CHAIN REMARK 500 2 ARG A 34 0.24 SIDE CHAIN REMARK 500 2 ARG A 66 0.32 SIDE CHAIN REMARK 500 3 ARG A 34 0.32 SIDE CHAIN REMARK 500 3 ARG A 66 0.25 SIDE CHAIN REMARK 500 4 ARG A 34 0.30 SIDE CHAIN REMARK 500 4 ARG A 66 0.32 SIDE CHAIN REMARK 500 5 ARG A 34 0.31 SIDE CHAIN REMARK 500 5 ARG A 66 0.26 SIDE CHAIN REMARK 500 6 ARG A 34 0.30 SIDE CHAIN REMARK 500 6 ARG A 66 0.32 SIDE CHAIN REMARK 500 7 ARG A 34 0.24 SIDE CHAIN REMARK 500 7 ARG A 66 0.29 SIDE CHAIN REMARK 500 8 ARG A 34 0.26 SIDE CHAIN REMARK 500 8 ARG A 66 0.31 SIDE CHAIN REMARK 500 9 ARG A 34 0.29 SIDE CHAIN REMARK 500 9 ARG A 66 0.23 SIDE CHAIN REMARK 500 10 ARG A 34 0.17 SIDE CHAIN REMARK 500 10 ARG A 66 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4779 RELATED DB: BMRB REMARK 900 BACKBONE AND SIDECHAIN 1H, 13C, AND 15N NMR CHEMICAL SHIFT REMARK 900 ASSIGNMENTS DBREF 1PLO A 15 136 UNP P37173 TGFR2_HUMAN 38 159 SEQADV 1PLO ALA A 19 UNP P37173 ASN 42 ENGINEERED MUTATION SEQRES 1 A 122 VAL THR ASP ASN ALA GLY ALA VAL LYS PHE PRO GLN LEU SEQRES 2 A 122 CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN SEQRES 3 A 122 GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE SEQRES 4 A 122 CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG SEQRES 5 A 122 LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS SEQRES 6 A 122 ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP SEQRES 7 A 122 ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS SEQRES 8 A 122 PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP SEQRES 9 A 122 GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR ASN SEQRES 10 A 122 THR SER ASN PRO ASP SHEET 1 A 2 LEU A 27 LYS A 29 0 SHEET 2 A 2 THR A 51 ILE A 53 -1 O SER A 52 N CYS A 28 SHEET 1 B 4 ASP A 32 PHE A 35 0 SHEET 2 B 4 ILE A 72 HIS A 79 -1 O LEU A 74 N ARG A 34 SHEET 3 B 4 VAL A 60 LYS A 67 -1 N VAL A 60 O HIS A 79 SHEET 4 B 4 THR A 109 PHE A 110 -1 O THR A 109 N LYS A 67 SHEET 1 C 4 ASP A 32 PHE A 35 0 SHEET 2 C 4 ILE A 72 HIS A 79 -1 O LEU A 74 N ARG A 34 SHEET 3 C 4 VAL A 60 LYS A 67 -1 N VAL A 60 O HIS A 79 SHEET 4 C 4 SER A 114 CYS A 115 -1 O CYS A 115 N CYS A 61 SHEET 1 D 2 CYS A 44 MET A 45 0 SHEET 2 D 2 ASN A 123 ILE A 124 -1 O ILE A 124 N CYS A 44 SSBOND 1 CYS A 28 CYS A 61 1555 1555 2.02 SSBOND 2 CYS A 31 CYS A 48 1555 1555 2.02 SSBOND 3 CYS A 38 CYS A 44 1555 1555 2.02 SSBOND 4 CYS A 54 CYS A 78 1555 1555 2.02 SSBOND 5 CYS A 98 CYS A 113 1555 1555 2.02 SSBOND 6 CYS A 115 CYS A 120 1555 1555 2.02 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