Header list of 2ct6.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 23-MAY-05 2CT6 TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE TITLE 2 PROTEIN 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3BGRL2; 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: SH3BGRL2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040614-04; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS SH3BGRL2, FASH3, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.MIYAMOTO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CT6 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CT6 1 VERSN REVDAT 1 23-NOV-05 2CT6 0 JRNL AUTH K.MIYAMOTO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN-BINDING GLUTAMIC JRNL TITL 2 ACID-RICH-LIKE PROTEIN 2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 1.0.7 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CT6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000024595. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.95MM SH3BGRL2 U-13C,15N; 20MM REMARK 210 D-TRIS-HCL; 100MM NACL; 1MM D- REMARK 210 DTT; 0.02% NAN3; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.925, CYANA 1.0.7 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS 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: 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 34 H ILE A 39 1.51 REMARK 500 O PHE A 33 HD21 ASN A 37 1.53 REMARK 500 O THR A 97 H PHE A 101 1.55 REMARK 500 O PHE A 99 H LEU A 104 1.56 REMARK 500 O GLN A 28 H ARG A 32 1.56 REMARK 500 H VAL A 12 O GLU A 42 1.58 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 2 107.48 62.25 REMARK 500 1 SER A 5 114.50 178.67 REMARK 500 1 ARG A 11 102.03 -57.97 REMARK 500 1 SER A 16 -30.54 -38.51 REMARK 500 1 ASP A 29 -31.20 -38.54 REMARK 500 1 VAL A 30 -74.90 -68.53 REMARK 500 1 PHE A 41 -179.85 -173.99 REMARK 500 1 ASP A 45 91.13 -64.01 REMARK 500 1 LYS A 65 120.15 -39.84 REMARK 500 1 THR A 67 -97.29 37.45 REMARK 500 1 ASN A 70 156.10 -46.71 REMARK 500 1 CYS A 83 -75.86 -70.79 REMARK 500 1 ASP A 85 -178.46 -69.31 REMARK 500 1 LEU A 104 55.95 -100.11 REMARK 500 1 LYS A 105 81.82 -177.16 REMARK 500 1 SER A 106 84.05 -176.41 REMARK 500 1 SER A 109 -57.72 178.29 REMARK 500 2 SER A 3 -61.23 -156.85 REMARK 500 2 SER A 5 -55.14 -161.47 REMARK 500 2 SER A 6 106.36 62.98 REMARK 500 2 ARG A 11 95.97 -61.47 REMARK 500 2 SER A 16 -82.76 -37.93 REMARK 500 2 SER A 17 77.55 -63.77 REMARK 500 2 PHE A 20 88.01 -58.43 REMARK 500 2 VAL A 30 -89.44 -67.00 REMARK 500 2 PHE A 41 -176.64 -174.54 REMARK 500 2 ASP A 45 84.46 -62.45 REMARK 500 2 THR A 67 -105.08 35.52 REMARK 500 2 LYS A 105 119.27 66.03 REMARK 500 2 SER A 106 73.48 178.28 REMARK 500 2 SER A 110 95.32 49.15 REMARK 500 3 SER A 3 152.22 61.60 REMARK 500 3 ARG A 11 96.17 -59.27 REMARK 500 3 SER A 17 73.33 -104.30 REMARK 500 3 ASP A 29 -35.71 -36.71 REMARK 500 3 VAL A 30 -88.34 -63.80 REMARK 500 3 ASP A 45 96.88 -58.38 REMARK 500 3 LYS A 65 123.85 -39.45 REMARK 500 3 THR A 67 -96.63 36.42 REMARK 500 3 ASN A 70 157.24 -40.85 REMARK 500 3 CYS A 83 -70.48 -88.89 REMARK 500 3 LEU A 104 59.21 -106.44 REMARK 500 3 SER A 106 -61.25 69.93 REMARK 500 3 SER A 109 95.42 62.35 REMARK 500 4 SER A 2 90.25 56.29 REMARK 500 4 ARG A 11 87.28 -65.13 REMARK 500 4 SER A 16 -88.92 -38.17 REMARK 500 4 SER A 18 -72.09 -104.54 REMARK 500 4 ASP A 29 -31.29 -38.59 REMARK 500 4 VAL A 30 -71.17 -68.24 REMARK 500 REMARK 500 THIS ENTRY HAS 347 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001001006.1 RELATED DB: TARGETDB DBREF 2CT6 A 8 105 UNP Q9UJC5 SH3L2_HUMAN 1 98 SEQADV 2CT6 GLY A 1 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 2 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 3 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 GLY A 4 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 5 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 6 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 GLY A 7 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 106 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 GLY A 107 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 PRO A 108 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 109 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 SER A 110 UNP Q9UJC5 CLONING ARTIFACT SEQADV 2CT6 GLY A 111 UNP Q9UJC5 CLONING ARTIFACT SEQRES 1 A 111 GLY SER SER GLY SER SER GLY MET VAL ILE ARG VAL PHE SEQRES 2 A 111 ILE ALA SER SER SER GLY PHE VAL ALA ILE LYS LYS LYS SEQRES 3 A 111 GLN GLN ASP VAL VAL ARG PHE LEU GLU ALA ASN LYS ILE SEQRES 4 A 111 GLU PHE GLU GLU VAL ASP ILE THR MET SER GLU GLU GLN SEQRES 5 A 111 ARG GLN TRP MET TYR LYS ASN VAL PRO PRO GLU LYS LYS SEQRES 6 A 111 PRO THR GLN GLY ASN PRO LEU PRO PRO GLN ILE PHE ASN SEQRES 7 A 111 GLY ASP ARG TYR CYS GLY ASP TYR ASP SER PHE PHE GLU SEQRES 8 A 111 SER LYS GLU SER ASN THR VAL PHE SER PHE LEU GLY LEU SEQRES 9 A 111 LYS SER GLY PRO SER SER GLY HELIX 1 1 VAL A 21 ALA A 36 1 16 HELIX 2 2 GLU A 50 LYS A 58 1 9 HELIX 3 3 TYR A 86 LYS A 93 1 8 HELIX 4 4 VAL A 98 LEU A 102 1 5 SHEET 1 A 4 PHE A 41 ASP A 45 0 SHEET 2 A 4 ILE A 10 ILE A 14 1 N VAL A 12 O GLU A 42 SHEET 3 A 4 GLN A 75 ASN A 78 -1 O PHE A 77 N ARG A 11 SHEET 4 A 4 ARG A 81 ASP A 85 -1 O ARG A 81 N ASN A 78 CISPEP 1 PRO A 73 PRO A 74 1 0.04 CISPEP 2 PRO A 73 PRO A 74 2 0.00 CISPEP 3 PRO A 73 PRO A 74 3 -0.03 CISPEP 4 PRO A 73 PRO A 74 4 0.02 CISPEP 5 PRO A 73 PRO A 74 5 -0.01 CISPEP 6 PRO A 73 PRO A 74 6 0.02 CISPEP 7 PRO A 73 PRO A 74 7 -0.04 CISPEP 8 PRO A 73 PRO A 74 8 -0.06 CISPEP 9 PRO A 73 PRO A 74 9 0.09 CISPEP 10 PRO A 73 PRO A 74 10 -0.03 CISPEP 11 PRO A 73 PRO A 74 11 0.00 CISPEP 12 PRO A 73 PRO A 74 12 0.05 CISPEP 13 PRO A 73 PRO A 74 13 -0.06 CISPEP 14 PRO A 73 PRO A 74 14 0.04 CISPEP 15 PRO A 73 PRO A 74 15 0.00 CISPEP 16 PRO A 73 PRO A 74 16 -0.07 CISPEP 17 PRO A 73 PRO A 74 17 -0.03 CISPEP 18 PRO A 73 PRO A 74 18 -0.01 CISPEP 19 PRO A 73 PRO A 74 19 -0.06 CISPEP 20 PRO A 73 PRO A 74 20 -0.01 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 - r 9 2 Bytes