Header list of 1ri9.pdb file
Complete list - g 9 2 Bytes
HEADER SIGNALING PROTEIN 17-NOV-03 1RI9 TITLE STRUCTURE OF A HELICALLY EXTENDED SH3 DOMAIN OF THE T CELL ADAPTER TITLE 2 PROTEIN ADAP COMPND MOL_ID: 1; COMPND 2 MOLECULE: FYN-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 683-771 OF ADAP PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FYB, SLAP130; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTFT74 KEYWDS SH3-LIKE, HELICALLY EXTENDED, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.HEUER,M.KOFLER,G.LANGDON,K.THIEMKE,C.FREUND REVDAT 4 14-JUN-23 1RI9 1 REMARK REVDAT 3 05-FEB-20 1RI9 1 REMARK SEQADV REVDAT 2 24-FEB-09 1RI9 1 VERSN REVDAT 1 20-APR-04 1RI9 0 JRNL AUTH K.HEUER,M.KOFLER,G.LANGDON,K.THIEMKE,C.FREUND JRNL TITL STRUCTURE OF A HELICALLY EXTENDED SH3 DOMAIN OF THE T CELL JRNL TITL 2 ADAPTER PROTEIN ADAP. JRNL REF STRUCTURE V. 12 603 2004 JRNL REFN ISSN 0969-2126 JRNL PMID 15062083 JRNL DOI 10.1016/J.STR.2004.02.021 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.6 REMARK 3 AUTHORS : BRUKER GMBH (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1136 RESTRAINTS, 718 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 388 DIHEDRAL ANGLE RESTRAINTS,30 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1RI9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-03. REMARK 100 THE DEPOSITION ID IS D_1000020768. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : 0.05 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.8MM ADAP-HSH3 DOMAIN "[U-95% REMARK 210 13C; U-90% 15N]" REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, CYANA 1.0.6 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 51 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 ARE THE 20 STRUCTURES WITH THE REMARK 210 LOWEST ENERGY. REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES. 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 -12 REMARK 465 GLY A -11 REMARK 465 SER A -10 REMARK 465 SER A -9 REMARK 465 HIS A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 SER A -2 REMARK 465 SER A -1 REMARK 465 GLY A 0 REMARK 465 LYS A 1 REMARK 465 LYS A 2 REMARK 465 LEU A 3 REMARK 465 LYS A 4 REMARK 465 LYS A 5 REMARK 465 GLN A 6 REMARK 465 ASN A 84 REMARK 465 ASP A 85 REMARK 465 GLY A 86 REMARK 465 GLU A 87 REMARK 465 ILE A 88 REMARK 465 TYR A 89 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 PHE A 17 H TYR A 19 1.09 REMARK 500 HG21 ILE A 56 H GLN A 57 1.14 REMARK 500 HD11 LEU A 81 H ALA A 82 1.26 REMARK 500 C PHE A 17 H TYR A 19 1.43 REMARK 500 O THR A 32 H ILE A 35 1.48 REMARK 500 O PHE A 13 H PHE A 17 1.53 REMARK 500 O PHE A 17 N TYR A 19 1.74 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 LYS A 18 7.90 -35.53 REMARK 500 1 VAL A 25 99.46 -66.31 REMARK 500 1 THR A 33 -19.92 -43.51 REMARK 500 1 GLN A 46 31.28 -88.07 REMARK 500 1 ILE A 56 -138.06 -91.46 REMARK 500 1 THR A 59 -74.28 -54.24 REMARK 500 1 ASP A 60 -91.58 -104.64 REMARK 500 1 THR A 62 69.98 -117.84 REMARK 500 2 LYS A 18 8.43 -36.01 REMARK 500 2 THR A 33 -17.85 -44.57 REMARK 500 2 GLN A 46 30.78 -88.05 REMARK 500 2 ILE A 56 -137.91 -91.97 REMARK 500 2 THR A 59 -74.10 -54.67 REMARK 500 2 ASP A 60 -92.01 -104.58 REMARK 500 2 THR A 62 69.44 -117.56 REMARK 500 3 LYS A 18 7.01 -35.04 REMARK 500 3 VAL A 25 99.59 -65.82 REMARK 500 3 GLN A 46 31.48 -89.20 REMARK 500 3 ILE A 56 -138.69 -91.64 REMARK 500 3 THR A 59 -75.16 -55.11 REMARK 500 3 ASP A 60 -91.63 -104.78 REMARK 500 3 THR A 62 68.74 -117.47 REMARK 500 3 GLU A 70 -9.30 -59.16 REMARK 500 4 LYS A 18 7.75 -35.59 REMARK 500 4 THR A 33 -16.89 -44.80 REMARK 500 4 GLN A 46 31.10 -87.48 REMARK 500 4 ILE A 56 -138.09 -92.45 REMARK 500 4 THR A 59 -75.33 -54.81 REMARK 500 4 ASP A 60 -91.33 -105.24 REMARK 500 4 THR A 62 69.16 -117.67 REMARK 500 5 LYS A 18 7.39 -35.20 REMARK 500 5 GLN A 46 33.60 -88.98 REMARK 500 5 ILE A 56 -137.19 -93.15 REMARK 500 5 THR A 59 -74.38 -55.34 REMARK 500 5 ASP A 60 -91.72 -104.71 REMARK 500 5 THR A 62 69.56 -117.68 REMARK 500 5 ALA A 82 174.23 -54.58 REMARK 500 6 PHE A 17 30.10 -87.42 REMARK 500 6 LYS A 18 6.64 -34.54 REMARK 500 6 VAL A 25 98.86 -65.62 REMARK 500 6 GLN A 46 31.38 -88.21 REMARK 500 6 ILE A 56 -140.02 -92.72 REMARK 500 6 THR A 59 -75.40 -61.21 REMARK 500 6 ASP A 60 -92.64 -105.42 REMARK 500 6 THR A 62 67.76 -115.38 REMARK 500 6 ALA A 82 174.53 -55.08 REMARK 500 7 LYS A 18 7.75 -35.52 REMARK 500 7 THR A 33 -11.51 -47.39 REMARK 500 7 GLN A 46 31.53 -87.60 REMARK 500 7 ILE A 56 -138.29 -92.33 REMARK 500 REMARK 500 THIS ENTRY HAS 150 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5467 RELATED DB: BMRB REMARK 900 THE SAME PROTEIN DBREF 1RI9 A 1 89 UNP O15117 FYB_HUMAN 683 771 SEQADV 1RI9 MET A -12 UNP O15117 INSERTION SEQADV 1RI9 GLY A -11 UNP O15117 INSERTION SEQADV 1RI9 SER A -10 UNP O15117 INSERTION SEQADV 1RI9 SER A -9 UNP O15117 INSERTION SEQADV 1RI9 HIS A -8 UNP O15117 INSERTION SEQADV 1RI9 HIS A -7 UNP O15117 INSERTION SEQADV 1RI9 HIS A -6 UNP O15117 INSERTION SEQADV 1RI9 HIS A -5 UNP O15117 INSERTION SEQADV 1RI9 HIS A -4 UNP O15117 INSERTION SEQADV 1RI9 HIS A -3 UNP O15117 INSERTION SEQADV 1RI9 SER A -2 UNP O15117 INSERTION SEQADV 1RI9 SER A -1 UNP O15117 INSERTION SEQADV 1RI9 GLY A 0 UNP O15117 INSERTION SEQRES 1 A 102 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 102 LYS LYS LEU LYS LYS GLN GLU LYS GLU GLU LYS ASP PHE SEQRES 3 A 102 ARG LYS LYS PHE LYS TYR ASP GLY GLU ILE ARG VAL LEU SEQRES 4 A 102 TYR SER THR LYS VAL THR THR SER ILE THR SER LYS LYS SEQRES 5 A 102 TRP GLY THR ARG ASP LEU GLN VAL LYS PRO GLY GLU SER SEQRES 6 A 102 LEU GLU VAL ILE GLN THR THR ASP ASP THR LYS VAL LEU SEQRES 7 A 102 CYS ARG ASN GLU GLU GLY LYS TYR GLY TYR VAL LEU ARG SEQRES 8 A 102 SER TYR LEU ALA ASP ASN ASP GLY GLU ILE TYR HELIX 1 1 GLU A 7 PHE A 17 1 11 HELIX 2 2 SER A 79 LEU A 81 5 3 SHEET 1 A 3 GLU A 54 THR A 58 0 SHEET 2 A 3 LYS A 63 ASN A 68 -1 O ARG A 67 N GLU A 54 SHEET 3 A 3 LYS A 72 LEU A 77 -1 O GLY A 74 N CYS A 66 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 - g 9 2 Bytes